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I am WeigelaPen and I have started editing pages of protein domains, making links to the Pfam database of protein families/domains.
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Notes
editTemplate for Pfam-box or info-box Template:Infobox protein family
Glucose-6-phosphate dehydrogenase, NAD binding domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | G6PD_N | ||||||||
Pfam | PF00479 | ||||||||
Pfam clan | CL0063 | ||||||||
InterPro | IPR022674 | ||||||||
PROSITE | PDOC00067 | ||||||||
SCOP2 | 1dpg / SCOPe / SUPFAM | ||||||||
|
Template for Table Table cell templates provide a set of templates to configure text and color in cells in a standard way, using phrases such as Yes, No or n/a.
Table
editCol 1 | Human gene | C. elegans gene | D. melanogaster gene | S. cerevisiae gene | Sch. pombe gene |
---|---|---|---|---|---|
Ex for col 1, row1 | Ex for col 2 | Ex for col3 | Ex for col4 | Ex for col5 | Ex for col6 |
Ex col1 row 2 a | |||||
CDK8 | CDK8 | cdk-8 | Cdk8 | SSN3 | srb10 |
- a Fungal-specific
- b Protein-name in Sch. pombe
Table of conserved subunits of cytochrome oxidase c complex
editNo. | Subunit name | Human protein | Protein description from UniProt | Pfam family with Human protein
|
---|---|---|---|---|
1 | Cox1 | COX1_HUMAN | Cytochrome c oxidase subunit 1 | Pfam PF00115 |
2 | Cox2 | COX2_HUMAN | Cytochrome c oxidase subunit 2 | Pfam PF02790, Pfam PF00116 |
3 | Cox3 | COX3_HUMAN | Cytochrome c oxidase subunit 3 | Pfam PF00510 |
4 | Cox4i1 | COX41_HUMAN | Cytochrome c oxidase subunit 4 isoform 1, mitochondrial | Pfam PF02936 |
5 | Cox4a2 | COX42_HUMAN | Cytochrome c oxidase subunit 4 isoform 2, mitochondrial | Pfam PF02936 |
6 | Cox5a | COX5A_HUMAN | Cytochrome c oxidase subunit 5A, mitochondrial | Pfam PF02284 |
7 | Cox5b | COX5B_HUMAN | Cytochrome c oxidase subunit 5B, mitochondrial | Pfam PF01215 |
8 | Cox6a1 | CX6A1_HUMAN | Cytochrome c oxidase subunit 6A1, mitochondrial | Pfam PF02046 |
9 | Cox6a2 | CX6A2_HUMAN | Cytochrome c oxidase subunit 6A2, mitochondrial | Pfam PF02046 |
10 | Cox6b1 | CX6B1_HUMAN | Cytochrome c oxidase subunit 6B1 | Pfam PF02297 |
11 | Cox6b2 | CX6B2_HUMAN | Cytochrome c oxidase subunit 6B2 | Pfam PF02297 |
12 | Cox6c | COX6C_HUMAN | Cytochrome c oxidase subunit 6C | Pfam PF02937 |
13 | Cox7a1 | CX7A1_HUMAN | Cytochrome c oxidase subunit 7A1, mitochondrial | Pfam PF02238 |
14 | Cox7a2 | CX7A2_HUMAN | Cytochrome c oxidase subunit 7A2, mitochondrial | Pfam PF02238 |
15 | Cox7a3 | COX7S_HUMAN | Putative cytochrome c oxidase subunit 7A3, mitochondrial | Pfam PF02238 |
16 | Cox7b | COX7B_HUMAN | Cytochrome c oxidase subunit 7B, mitochondrial | Pfam PF05392 |
17 | Cox7c | COX7C_HUMAN | Cytochrome c oxidase subunit 7C, mitochondrial | Pfam PF02935 |
18 | Cox7r | COX7R_HUMAN | Cytochrome c oxidase subunit 7A-related protein, mitochondrial | Pfam PF02238 |
19 | Cox8a | COX8A_HUMAN | Cytochrome c oxidase subunit 8A, mitochondrial P | Pfam PF02285 |
20 | Cox8c | COX8C_HUMAN | Cytochrome c oxidase subunit 8C, mitochondrial | Pfam PF02285 |
Assembly subunits[1][2][3] | ||||
1 | Coa1 | COA1_HUMAN | Cytochrome c oxidase assembly factor 1 homolog | Pfam PF08695 |
2 | Coa3 | COA3_HUMAN | Cytochrome c oxidase assembly factor 3 homolog, mitochondrial | Pfam PF09813 |
3 | Coa4 | COA4_HUMAN | Cytochrome c oxidase assembly factor 4 homolog, mitochondrial | Pfam PF06747 |
4 | Coa5 | COA5_HUMAN | Cytochrome c oxidase assembly factor 5 | Pfam PF10203 |
5 | Coa6 | COA6_HUMAN | Cytochrome c oxidase assembly factor 6 homolog | Pfam PF02297 |
6 | Coa7 | COA7_HUMAN | Cytochrome c oxidase assembly factor 7, | Pfam PF08238 |
7 | Cox11 | COX11_HUMAN | Cytochrome c oxidase assembly protein COX11 mitochondrial | Pfam PF04442 |
8 | Cox14 | COX14_HUMAN | Cytochrome c oxidase assembly protein | Pfam PF14880 |
9 | Cox15 | COX15_HUMAN | Cytochrome c oxidase assembly protein COX15 homolog | Pfam PF02628 |
10 | Cox16 | COX16_HUMAN | Cytochrome c oxidase assembly protein COX16 homolog mitochondrial | Pfam PF14138 |
11 | Cox17 | COX17_HUMAN | Cytochrome c oxidase copper chaperone | Pfam PF05051 |
12 | Cox18[4] | COX18_HUMAN | Mitochondrial inner membrane protein (Cytochrome c oxidase assembly protein 18) | Pfam PF02096 |
13 | Cox19 | COX19_HUMAN | Cytochrome c oxidase assembly protein | Pfam PF06747 |
14 | Cox20 | COX20_HUMAN | Cytochrome c oxidase protein 20 homolog | Pfam PF12597 |
Table of Subunit composition of Complex III
editThe bc1 complex, or Complex III, contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1.[5][6]
No. | Subunit name | Human protein | Protein description from UniProt | Pfam family with Human protein |
---|---|---|---|---|
Respiratory subunit proteins | ||||
1 | MT-CYB / Cyt b | CYB_HUMAN | Cytochrome b | PF13631 |
2 | CYC1 / Cyt c1 | CY1_HUMAN | Cytochrome c1, heme protein, mitochondrial | PF02167 |
3 | Rieske / UCR1 | UCRI_HUMAN | Cytochrome b-c1 complex subunit Rieske, mitochondrial EC=1.10.2.2 | PF02921 , PF00355 |
Core protein subunits | ||||
4 | QCR1 / SU1 | QCR1_HUMAN | Cytochrome b-c1 complex subunit 1, mitochondrial | PF00675, PF05193 |
5 | QCR2 / SU2 | QCR2_HUMAN | Cytochrome b-c1 complex subunit 2, mitochondrial | PF00675, PF05193 |
Low-molucular weight protein subunits | ||||
6 | QCR6 / SU6 | QCR6_HUMAN | Cytochrome b-c1 complex subunit 6, mitochondrial | PF02320 |
7 | QCR7 / SU7 | QCR7_HUMAN | Cytochrome b-c1 complex subunit 7 | PF02271 |
8 | QCR8 / SU8 | QCR8_HUMAN | Cytochrome b-c1 complex subunit 8 | PF02939 |
9 | QCR9 / SU9 / UCRC | QCR9_HUMAN | Cytochrome b-c1 complex subunit 9 | PF05365 |
10 | QCR10 / SU10 | QCR10_HUMAN | Cytochrome b-c1 complex subunit 10 | PF08997 |
11 | QCR11 / SU11 a | UCRI_HUMAN | Cytochrome b-c1 complex subunit 11 | PF09165 |
- a A cleavage product of 8 kDa from the N-terminus of Rieske
|-
| 1 || SdhA || SDHA_HUMAN || Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial ||PF00890, PF02910
|-
| 2 || SdhB || SDHB_HUMAN || Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial ||PF13085, PF13183 |-
| 3 || SdhC || C560_HUMAN || Succinate dehydrogenase cytochrome b560 subunit, mitochondrial ||PF01127
|-
| 4 || SdhD || DHSD_HUMAN || Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial ||PF05328
|-
|}
Table of E.coli small Ribosomal subunits
editSubunit No. | Subunit name | E.coli protein | Pfam family with E.coli protein |
---|---|---|---|
1 | 30S ribosomal protein S1 | RS1_ECOLI | PF00575 |
2 | 30S ribosomal protein S2 | RS2_ECOLI | PF00318 |
3 | 30S ribosomal protein S3 | RS3_ECOLI | PF00189 ,PF07650 |
4 | 30S ribosomal protein S4 | RS4_ECOLI | PF00163 ,PF01479 |
5 | 30S ribosomal protein S5 | RS5_ECOLI | PF00333 ,PF03719 |
6 | 30S ribosomal protein S6 | RS6_ECOLI | PF01250 |
7 | 30S ribosomal protein S7 | RS7_ECOLI | PF00177 |
8 | 30S ribosomal protein S8 | RS8_ECOLI | PF00410 |
9 | 30S ribosomal protein S9 | RS9_ECOLI | PF00380 |
10 | 30S ribosomal protein S10 | RS10_ECOLI | PF00338 |
11 | 30S ribosomal protein S11 | RS11_ECOLI | PF00411 |
12 | 30S ribosomal protein S12 | RS12_ECOLI | PF00164 |
13 | 30S ribosomal protein S13 | RS13_ECOLI | PF00416 |
14 | 30S ribosomal protein S14 | RS14_ECOLI | PF00253 |
15 | 30S ribosomal protein S15 | RS15_ECOLI | PF00312 |
16 | 30S ribosomal protein S16 | RS16_ECOLI | PF00886 |
27 | 30S ribosomal protein S17 | RS17_ECOLI | PF00366 |
28 | 30S ribosomal protein S18 | RS18_ECOLI | PF01084 |
29 | 30S ribosomal protein S19 | RS19_ECOLI | PF00203 |
20 | 30S ribosomal protein S20 | RS20_ECOLI | PF01649 |
21 | 30S ribosomal protein S21 | RS21_ECOLI | PF01165 |
22 | aStationary-phase-induced ribosome-associated protein | SRA_ECOLI | PF08136 |
a : Alternative name 30S ribosomal protein S22 - Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein. It is not essential for bacterial growth.[7]
Table of Human small Ribosomal subunits
editSubunit No. | Subunit name | Human protein | Pfam family with Human protein | Pfam family description
|
---|---|---|---|---|
2 | ribosomal protein S2 | RS2_HUMAN | PF03719 | Ribosomal protein S5, C-terminal domain |
2 | ribosomal protein S2 | RS2_HUMAN | PF00333 | Ribosomal protein S5, N-terminal domain |
3 | ribosomal protein S3 | RS3_HUMAN | PF00189 | Ribosomal protein S3, C-terminal domain |
3a | ribosomal protein S3a | RS3A_HUMAN | PF01015 | Ribosomal S3Ae family |
4 | ribosomal protein S4, X isoform | RS4X_HUMAN | PF08071 | RS4NT (NUC023) domain |
4 | ribosomal protein S4, X isoform | RS4X_HUMAN | PF01479 | S4 domain |
4 | ribosomal protein S4, X isoform | RS4X_HUMAN | PF00900 | Ribosomal family S4e |
4 | ribosomal protein S4, X isoform | RS4X_HUMAN | PF16121 | 40S ribosomal protein S4 C-terminus |
4 | ribosomal protein S4, Y isoform 1 | RS4Y1_HUMAN | PF08071 | RS4NT (NUC023) domain |
4 | ribosomal protein S4, Y isoform 1 | RS4Y1_HUMAN | PF00900 | Ribosomal family S4e |
4 | ribosomal protein S4, Y isoform 1 | RS4Y1_HUMAN | PF16121 | 40S ribosomal protein S4 C-terminus |
4 | ribosomal protein S4, Y isoform 2 | RS4Y2_HUMAN | PF08071 | RS4NT (NUC023) domain |
4 | ribosomal protein S4, Y isoform 2 | RS4Y2_HUMAN | PF00900 | Ribosomal family S4e |
4 | ribosomal protein S4, Y isoform 2 | RS4Y2_HUMAN | PF16121 | 40S ribosomal protein S4 C-terminus |
5 | ribosomal protein S5 | RS5_HUMAN | PF00177 | Ribosomal protein S7p/S5e |
6 | ribosomal protein S6 | RS6_HUMAN | PF01092 | Ribosomal protein S6e |
7 | ribosomal protein S7 | RS7_HUMAN | PF01251 | Ribosomal protein S7e |
8 | ribosomal protein S8 | RS8_HUMAN | PF01201 | Ribosomal protein S8e |
9 | ribosomal protein S9 | RS9_HUMAN | PF01479 | S4 domain |
9 | ribosomal protein S9 | RS9_HUMAN | PF00163 | Ribosomal protein S4/S9 N-terminal domain |
10 | ribosomal protein S10 | RS10_HUMAN | PF03501 | Plectin/S10 domain |
11 | ribosomal protein S11 | RS11_HUMAN | PF16205 | Ribosomal_S17 N-terminal |
11 | ribosomal protein S11 | RS11_HUMAN | PF00366 | Ribosomal protein S17 |
12 | ribosomal protein S12 | RS12_HUMAN | PF01248 | Ribosomal protein L7Ae/L30e/S12e/Gadd45 family |
13 | ribosomal protein S13 | RS13_HUMAN | PF08069 | Ribosomal S13/S15 N-terminal domain |
13 | ribosomal protein S13 | RS13_HUMAN | PF00312 | Ribosomal protein S15 |
14 | ribosomal protein S14 | RS14_HUMAN | PF00411 | Ribosomal protein S11 |
15 | ribosomal protein S15 | RS15_HUMAN | PF00203 | Ribosomal protein S19 |
15a | ribosomal protein S15a | RS15A_HUMAN | PF00410 | Ribosomal protein S8 |
16 | ribosomal protein S16 | RS16_HUMAN | PF00380 | Ribosomal protein S9/S16 |
17 | ribosomal protein S17 | RS17_HUMAN | PF00833 | Ribosomal S17 |
18 | ribosomal protein S18 | RS18_HUMAN | PF00416 | Ribosomal protein S13/S18 |
19 | ribosomal protein S19 | RS19_HUMAN | PF01090 | Ribosomal protein S19e |
20 | ribosomal protein S20 | RS20_HUMAN | PF00338 | Ribosomal protein S10p/S20e |
21 | ribosomal protein S21 | RS21_HUMAN | PF01249 | Ribosomal protein S21e |
23 | ribosomal protein S23 | RS23_HUMAN | PF00164 | Ribosomal protein S12/S23 |
24 | ribosomal protein S24 | RS24_HUMAN | PF01282 | Ribosomal protein S24e |
25 | ribosomal protein S25 | RS25_HUMAN | PF03297 | S25 ribosomal protein |
26 | ribosomal protein S26 | RS26_HUMAN | PF01283 | Ribosomal protein S26e |
27 | ribosomal protein S27 | RS27_HUMAN | PF01667 | Ribosomal protein S27 |
28 | ribosomal protein S28 | RS28_HUMAN | PF01200 | Ribosomal protein S28e |
29 | ribosomal protein S29 | RS29_HUMAN | PF00253 | Ribosomal protein S14p/S29e |
30 | ribosomal protein S30 | RS30_HUMAN | PF04758 | Ribosomal protein S30 |
A | ribosomal protein SA | RSSA_HUMAN | PF16122 | 40S ribosomal protein SA C-terminus |
A | ribosomal protein SA | RSSA_HUMAN | PF00318 | Ribosomal protein S2 |
Assembly of the ribosome in eukaryotes
editRibosomes, which synthesize the proteome of cells, are complex ribonucleoproteins that, in eukaryotes, contain 79–80 proteins and four ribosomal RNAs(rRNAs). General or specialized chaperones solubilize the ribosomal proteins and facilitate their import into the nucleus. Assembly of the eukaryotic ribosome appears to be driven by the ribosomal proteins in vivo when assembly is also aided by chaperones. Most ribosomal proteins assemble with rRNA co-transcriptionally, becoming associated more stably as assembly proceeds, and the active sites of both subunits are constructed last.[8]
Recent de novo proteomics experiments where the authors characterized in vivo ribosome-assembly intermediates and associated assembly factors from wild-type Escherichia coli cells using a general quantitative mass spectrometry (qMS) approach have confirmed the presence of all the known small and large subunit components and have identified a total of 21 known and potentially new ribosome-assembly-factors that co-localise with various ribosomal particles.[9]
Bacterial and eukaryotic ribosomes, which share an evolutionarily conserved core, are thought to have evolved from a common ancestor by addition of proteins and RNA that bestow different functionalities to ribosomes from different domains of life.[10] The term 'the core' refers to the structurally conserved part of the 70S ribosomes (from T. thermophilus and Escherichia coli) and the 80S ribosomes (from S. cerevisiae), deduced by a standard procedure of structural alignment.[11]
Table of Human 60S large subunit components
editinfoboxes lost to ComplexI
editNADH-Ubiquinone/plastoquinone (complex I), various chains | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q1 | ||||||||
Pfam | PF00361 | ||||||||
Pfam clan | CL0425 | ||||||||
InterPro | IPR001750 | ||||||||
TCDB | 3.D.9 | ||||||||
OPM superfamily | 279 | ||||||||
OPM protein | 3rko | ||||||||
|
NADH-Ubiquinone oxidoreductase (complex I) subunit C-terminus | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q1_C | ||||||||
Pfam | PF01010 | ||||||||
InterPro | IPR002128 | ||||||||
|
NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q1_N | ||||||||
Pfam | PF00662 | ||||||||
InterPro | IPR001516 | ||||||||
|
NADH-ubiquinone/plastoquinone oxidoreductase chain 4L | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q2 | ||||||||
Pfam | PF00420 | ||||||||
InterPro | IPR001133 | ||||||||
|
NADH-ubiquinone/plastoquinone oxidoreductase chain 6 | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q3 | ||||||||
Pfam | PF00499 | ||||||||
InterPro | IPR001457 | ||||||||
|
NADH-ubiquinone/plastoquinone oxidoreductase, chain 3 | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q4 | ||||||||
Pfam | PF00507 | ||||||||
InterPro | IPR000440 | ||||||||
|
NADH-ubiquinone oxidoreductase chain 4, amino terminus | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q5_N | ||||||||
Pfam | PF01059 | ||||||||
InterPro | IPR000260 | ||||||||
|
NADH ubiquinone oxidoreductase, 20 Kd subunit | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | Oxidored_q6 | ||||||||
Pfam | PF01058 | ||||||||
InterPro | IPR006137 | ||||||||
PROSITE | PDOC00858 | ||||||||
|
Reference management
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No. | Human/Bovine subunit | Human protein | Protein description (UniProt) | Pfam family with Human protein |
---|---|---|---|---|
Core Subunitsa | ||||
1 | NDUFS7 / PSST / NUKM | NDUS7_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF01058 |
2 | NDUFS8 / TYKY / NUIM | NDUS8_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF12838 |
3 | NDUFV2 / 24kD / NUHM | NDUV2_HUMAN | NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF01257 |
4 | NDUFS3 / 30kD / NUGM | NDUS3_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF00329 |
5 | NDUFS2 / 49kD / NUCM | NDUS2_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF00346 |
6 | NDUFV1 / 51kD / NUBM | NDUV1_HUMAN | NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF01512 |
7 | NDUFS1 / 75kD / NUAM | NDUS1_HUMAN | NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial EC=1.6.5.3 EC=1.6.99.3 | PF00384 |
8 | ND1 / NU1M | NU1M_HUMAN | NADH-ubiquinone oxidoreductase chain 1 EC=1.6.5.3 | PF00146 |
9 | ND2 / NU2M | NU2M_HUMAN | NADH-ubiquinone oxidoreductase chain 2 EC=1.6.5.3 | PF00361, PF06444 |
10 | ND3 / NU3M | NU3M_HUMAN | NADH-ubiquinone oxidoreductase chain 3 EC=1.6.5.3 | PF00507 |
11 | ND4 / NU4M | NU4M_HUMAN | NADH-ubiquinone oxidoreductase chain 4 EC=1.6.5.3 | PF01059,PF00361 |
12 | ND4L / NULM | NU4LM_HUMAN | NADH-ubiquinone oxidoreductase chain 4L EC=1.6.5.3 | PF00420 |
13 | ND5 / NU5M | NU5M_HUMAN | NADH-ubiquinone oxidoreductase chain 5 EC=1.6.5.3 | PF00361 |
14 | ND6 / NU6M | NU6M_HUMAN | NADH-ubiquinone oxidoreductase chain 6 EC=1.6.5.3 | PF00499 |
Core accessory subunitsb | ||||
15 | NDUFS6 / 13A | NDUS6_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial | PF10276 |
16 | NDUFA12 / B17.2 | NDUAC_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 | PF05071 |
17 | NDUFS4 / AQDQ | NDUS4_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial | PF04800 |
18 | NDUFA9 / 39kDa | NDUA9_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial | PF01370 |
19 | NDUFAB1 / ACPM | ACPM_HUMAN | Acyl carrier protein, mitochondrial | PF00550 |
20 | NDUFA2 / B8 | NDUA2_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 | PF05047 |
21 | NDUFA1 / MFWE | NDUA1_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1 | PF15879 |
22 | NDUFB3 / B12 | NDUB3_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3 | PF08122 |
23 | NDUFA5 / AB13 | NDUA5_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 | - |
24 | NDUFA6 / B14 | NDUA6_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 | PF05347 |
25 | NDUFA11 / B14.7 | NDUAB_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 | PF02466 |
26 | NDUFB11 / ESSS | NDUBB_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial | PF10183 |
27 | NDUFS5 / PFFD | NDUS5_HUMAN | NADH dehydrogenase [ubiquinone] iron-sulfur protein 5 | PF10200 |
28 | NDUFB4 / B15 | NDUB4_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4 | PF07225 |
29 | NDUFA13 /A13 | NDUAD_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 | PF06212 |
30 | NDUFB7 / B18 | NDUB7_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 | PF05676 |
31 | NDUFA8 / PGIV | NDUA8_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 | PF06747 |
32 | NDUFB9 / B22 | NDUB9_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9 | PF05347 |
33 | NDUFB10 / PDSW | NDUBA_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10 | PF10249 |
34 | NDUFB8 / ASHI | NDUB8_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial | PF05821 |
35 | NDUFC2 / B14.5B | NDUC2_HUMAN | NADH dehydrogenase [ubiquinone] 1 subunit C2 | PF06374 |
36 | NDUFB2 / AGGG | NDUB2_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial | PF14813 |
37 | NDUFA7 / B14.5A | NDUA7_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 | PF07347 |
38 | NDUFA3 / B9 | NDUA3_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 3 | PF14987 |
39 | NDUFA4 / MLRQ | NDUA4_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4 | PF06522 |
40 | NDUFB5 / SGDH | NDUB5_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial | PF09781 |
41 | NDUFB1 / MNLL | NDUB1_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1 | PF08040 |
42 | NDUFC1 / KFYI | NDUC1_HUMAN | NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial | PF15088 |
43 | NDUFA10 / 42kD | NDUAA_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial | PF01712 |
44 | NDUFA4L2 | NUA4L_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4-like 2 | PF15880 |
45 | NDUFV3 | NDUV3_HUMAN | NADH dehydrogenase [ubiquinone] flavoprotein 3, 10kDa | - |
46 | NDUFB6 | NDUB6_HUMAN | NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6 | PF09782 |
Assembly factor proteins[14] | ||||
47 | NDUFAF1 | CIA30_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, assembly factor 1 | PF08547 |
48 | NDUFAF2 | MIMIT_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, assembly factor 2 | PF05071 |
49 | NDUFAF3 | NDUF3_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 3 | PF05071 |
50 | NDUFAF4 | NDUF4_HUMAN | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, assembly factor 4 | PF06784 |
- a Found in all species
- b May or may not be present in any species
Pages under construction
edit- User:WeigelaPen/Sandpit
Cyclin | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||||
Symbol | ? | ||||||||||
Pfam | PF08613 | ||||||||||
Pfam clan | CL0065 | ||||||||||
InterPro | IPR013922 | ||||||||||
PROSITE | PDOC00264 | ||||||||||
SCOP2 | 47954 / SCOPe / SUPFAM | ||||||||||
|
For Article on WINE, to add:See alsoedit
External links |
- ^ Szklarczyk R, Wanschers BF, Cuypers TD, Esseling JJ, Riemersma M, van den Brand MA; et al. (2012). "Iterative orthology prediction uncovers new mitochondrial proteins and identifies C12orf62 as the human ortholog of COX14, a protein involved in the assembly of cytochrome c oxidase". Genome Biol. 13 (2): R12. doi:10.1186/gb-2012-13-2-r12. PMC 3334569. PMID 22356826.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Mick DU, Dennerlein S, Wiese H, Reinhold R, Pacheu-Grau D, Lorenzi I; et al. (2012). "MITRAC links mitochondrial protein translocation to respiratory-chain assembly and translational regulation". Cell. 151 (7): 1528–41. doi:10.1016/j.cell.2012.11.053. PMID 23260140.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: multiple names: authors list (link) - ^ Kozjak-Pavlovic V, Prell F, Thiede B, Götz M, Wosiek D, Ott C; et al. (2014). "C1orf163/RESA1 is a novel mitochondrial intermembrane space protein connected to respiratory chain assembly". J Mol Biol. 426 (4): 908–20. doi:10.1016/j.jmb.2013.12.001. PMID 24333015.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: multiple names: authors list (link) - ^ Gaisne M, Bonnefoy N (2006). "The COX18 gene, involved in mitochondrial biogenesis, is functionally conserved and tightly regulated in humans and fission yeast". FEMS Yeast Res. 6 (6): 869–82. doi:10.1111/j.1567-1364.2006.00083.x. PMID 16911509.
- ^ Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW; et al. (1998). "Electron transfer by domain movement in cytochrome bc1". Nature. 392 (6677): 677–84. doi:10.1038/33612. PMID 9565029.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: multiple names: authors list (link) - ^ Hao GF, Wang F, Li H, Zhu XL, Yang WC, Huang LS; et al. (2012). "Computational discovery of picomolar Q(o) site inhibitors of cytochrome bc1 complex". J Am Chem Soc. 134 (27): 11168–76. doi:10.1021/ja3001908. PMID 22690928.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: multiple names: authors list (link) - ^ Bubunenko M, Baker T, Court DL (2007). "Essentiality of ribosomal and transcription antitermination proteins analyzed by systematic gene replacement in Escherichia coli". J Bacteriol. 189 (7): 2844–53. doi:10.1128/JB.01713-06. PMC 1855809. PMID 17277072.
{{cite journal}}
: CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) - ^ Ban N, Beckmann R, Cate JH, Dinman JD, Dragon F, Ellis SR; et al. (2014). "A new system for naming ribosomal proteins". Curr Opin Struct Biol. 24: 165–9. doi:10.1016/j.sbi.2014.01.002. PMID 24524803.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: multiple names: authors list (link) - ^ Chen SS, Williamson JR (2013). "Characterization of the ribosome biogenesis landscape in E. coli using quantitative mass spectrometry". J Mol Biol. 425 (4): 767–79. doi:10.1016/j.jmb.2012.11.040. PMC 3568210. PMID 23228329.
{{cite journal}}
: CS1 maint: PMC format (link) - ^ Melnikov S, Ben-Shem A, Garreau de Loubresse N, Jenner L, Yusupova G, Yusupov M (2012). "One core, two shells: bacterial and eukaryotic ribosomes". Nat Struct Mol Biol. 19 (6): 560–7. doi:10.1038/nsmb.2313. PMID 22664983.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ Ben-Shem A, Garreau de Loubresse N, Melnikov S, Jenner L, Yusupova G, Yusupov M (2011). "The structure of the eukaryotic ribosome at 3.0 Å resolution". Science. 334 (6062): 1524–9. doi:10.1126/science.1212642. PMID 22096102.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ Cardol P (2011). "Mitochondrial NADH:ubiquinone oxidoreductase (complex I) in eukaryotes: a highly conserved subunit composition highlighted by mining of protein databases". Biochim Biophys Acta. 1807 (11): 1390–7. doi:10.1016/j.bbabio.2011.06.015. PMID 21749854.
- ^ Vogel RO, Dieteren CE, van den Heuvel LP, Willems PH, Smeitink JA, Koopman WJ; et al. (2007). "Identification of mitochondrial complex I assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits". J Biol Chem. 282 (10): 7582–90. doi:10.1074/jbc.M609410200. PMID 17209039.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Ogilvie I, Kennaway NG, Shoubridge EA (2005). "A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy". J Clin Invest. 115 (10): 2784–92. doi:10.1172/JCI26020. PMC 1236688. PMID 16200211.
{{cite journal}}
: CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) - ^ Dunning CJ, McKenzie M, Sugiana C, Lazarou M, Silke J, Connelly A; et al. (2007). "Human CIA30 is involved in the early assembly of mitochondrial complex I and mutations in its gene cause disease". EMBO J. 26 (13): 3227–37. doi:10.1038/sj.emboj.7601748. PMC 1914096. PMID 17557076.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) - ^ Saada A, Vogel RO, Hoefs SJ, van den Brand MA, Wessels HJ, Willems PH; et al. (2009). "Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex I assembly protein, cause fatal neonatal mitochondrial disease". Am J Hum Genet. 84 (6): 718–27. doi:10.1016/j.ajhg.2009.04.020. PMC 2694978. PMID 19463981.
{{cite journal}}
: Explicit use of et al. in:|author=
(help)CS1 maint: PMC format (link) CS1 maint: multiple names: authors list (link) - ^ Brown NR, Noble (1995). "The crystal structure of cyclin A". Structure. 3 (11): 1235–47. PMID 8591034.
{{cite journal}}
: Text "10.1016/S0969-2126(01)00259-3" ignored (help); Text "ME, Endicott JA, et al." ignored (help)