P13671 (CO6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Complement component C6

Gene names

Name:

C6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	934 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.
Subunit structure	Component of the membrane attack complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and 12-14 copies of the pore-forming subunit C9. Ref.11
Subcellular location	Secreted.
Post-translational modification	All cysteine residues are assumed to be cross-linked to one another. Individual modules containing an even number of conserved cysteine residues are supposed to have disulfide linkages only within the same module.
Polymorphism	The sequence shown is that of allotype C6 B.
Involvement in disease	Complement component 6 deficiency (C6D) [MIM:612446]: A rare defect of the complement classical pathway associated with susceptibility to severe recurrent infections, predominantly by Neisseria gonorrhoeae or Neisseria meningitidis. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
Sequence similarities	Belongs to the complement C6/C7/C8/C9 family. Contains 1 EGF-like domain. Contains 2 Kazal-like domains. Contains 1 LDL-receptor class A domain. Contains 1 MACPF domain. Contains 2 Sushi (CCP/SCR) domains. Contains 3 TSP type-1 domains.

Ontologies

Keywords
Biological process	Complement pathway Cytolysis Immunity Innate immunity
Cellular component	Membrane attack complex Secreted
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Repeat Signal Sushi
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	complement activation Traceable author statement Ref.1. Source: ProtInc complement activation, classical pathway Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW in utero embryonic development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome positive regulation of activation of membrane attack complex Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Traceable author statement. Source: Reactome membrane attack complex Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-1753221,EBI-389883

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.1

Chain

22 – 934

913

Complement component C6

PRO_0000023579

Regions

Domain

22 – 79

58

TSP type-1 1

Domain

81 – 134

54

TSP type-1 2

Domain

138 – 175

38

LDL-receptor class A

Domain

176 – 522

347

MACPF

Domain

523 – 553

31

EGF-like

Domain

565 – 612

48

TSP type-1 3

Domain

642 – 701

60

Sushi 1

Domain

702 – 763

62

Sushi 2

Domain

780 – 839

60

Kazal-like 1

Domain

876 – 934

59

Kazal-like 2

Region

611 – 688

78

CCP 1

Region

642 – 934

293

C5b-binding domain

Region

689 – 765

77

CCP 2

Region

766 – 840

75

Factor I module (FIM) 1

Region

858 – 934

77

Factor I module (FIM) 2

Amino acid modifications

Glycosylation

29

1

C-linked (Man) Ref.9 Ref.11

Glycosylation

32

1

C-linked (Man); partial Ref.9 Ref.11

Glycosylation

38

1

O-linked (Fuc...) Probable

Glycosylation

90

1

C-linked (Man); partial Ref.9

Glycosylation

324

1

N-linked (GlcNAc...) Ref.10 Ref.11

Glycosylation

392

1

O-linked (Fuc...) Probable

Glycosylation

568

1

C-linked (Man); partial Ref.9 Ref.11

Glycosylation

571

1

C-linked (Man); partial Ref.9 Ref.11

Glycosylation

574

1

C-linked (Man); partial Ref.9

Glycosylation

855

1

N-linked (GlcNAc...) Ref.10

Disulfide bond

22 ↔ 61

Ref.8 Ref.11

Disulfide bond

24 ↔ 65

Ref.8 Ref.11

Disulfide bond

35 ↔ 73

Ref.8 Ref.11

Disulfide bond

39 ↔ 78

Ref.8 Ref.11

Disulfide bond

82 ↔ 117

Ref.8 Ref.11

Disulfide bond

93 ↔ 127

Ref.8 Ref.11

Disulfide bond

96 ↔ 133

Ref.8 Ref.11

Disulfide bond

140 ↔ 151

Ref.8 Ref.11

Disulfide bond

146 ↔ 164

Ref.8 Ref.11

Disulfide bond

158 ↔ 173

Ref.8 Ref.11

Disulfide bond

180 ↔ 218

Ref.8 Ref.11

Disulfide bond

399 ↔ 420

Ref.8 Ref.11

Disulfide bond

499 ↔ 623

Ref.8 Ref.11

Disulfide bond

521 ↔ 570

Ref.8 Ref.11

Disulfide bond

523 ↔ 539

Ref.8 Ref.11

Disulfide bond

526 ↔ 541

Ref.8 Ref.11

Disulfide bond

543 ↔ 552

Ref.8 Ref.11

Disulfide bond

577 ↔ 611

Ref.8 Ref.11

Disulfide bond

589 ↔ 601

Ref.8 Ref.11

Disulfide bond

644 ↔ 686

Ref.8 Ref.11

Disulfide bond

672 ↔ 699

Ref.8 Ref.11

Disulfide bond

704 ↔ 746

Ref.8 Ref.11

Disulfide bond

732 ↔ 761

Ref.8 Ref.11

Disulfide bond

773 ↔ 823

Ref.8 Ref.11

Disulfide bond

784 ↔ 801

Ref.8 Ref.11

Disulfide bond

786 ↔ 837

Ref.8 Ref.11

Disulfide bond

793 ↔ 816

Ref.8 Ref.11

Disulfide bond

862 ↔ 873

Ref.8 Ref.11

Disulfide bond

867 ↔ 919

Ref.8 Ref.11

Disulfide bond

880 ↔ 897

Ref.8 Ref.11

Disulfide bond

882 ↔ 932

Ref.8 Ref.11

Disulfide bond

888 ↔ 912

Ref.8 Ref.11

Natural variations

Natural variant

119

1

A → E in allotype C6 A. Ref.2 Ref.3 Ref.6 Ref.7 Ref.12
Corresponds to variant rs1801033 [ dbSNP | Ensembl ].

VAR_006056

Natural variant

397

1

K → E.
Corresponds to variant rs6896011 [ dbSNP | Ensembl ].

VAR_027647

Natural variant

470

1

S → F.
Corresponds to variant rs10462014 [ dbSNP | Ensembl ].

VAR_027648

Experimental info

Sequence conflict

567

1

Q → H in BAD02321. Ref.4

Sequence conflict

616

1

M → I in BAD02321. Ref.4

Sequence conflict

934

1

A → T in BAD02321. Ref.4

Secondary structure

1

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934

Helix Strand Turn

Details...

Helix

24 – 26

3

Beta strand

38 – 40

3

Beta strand

42 – 48

7

Helix

54 – 58

5

Helix

61 – 64

4

Beta strand

68 – 73

6

Beta strand

95 – 97

3

Beta strand

100 – 104

5

Beta strand

106 – 108

3

Beta strand

121 – 125

5

Beta strand

130 – 133

4

Beta strand

141 – 145

5

Beta strand

151 – 153

3

Helix

154 – 156

3

Beta strand

157 – 161

5

Beta strand

164 – 167

4

Helix

168 – 170

3

Beta strand

179 – 182

4

Helix

190 – 194

5

Beta strand

195 – 198

4

Turn

199 – 202

4

Beta strand

203 – 207

5

Beta strand

226 – 228

3

Beta strand

236 – 240

5

Helix

247 – 249

3

Beta strand

250 – 256

7

Helix

258 – 262

5

Beta strand

279 – 282

4

Turn

287 – 289

3

Helix

298 – 307

10

Beta strand

309 – 327

19

Beta strand

329 – 331

3

Helix

336 – 341

6

Helix

351 – 361

11

Beta strand

363 – 365

3

Beta strand

367 – 382

16

Helix

383 – 389

7

Helix

393 – 407

15

Helix

418 – 420

3

Helix

426 – 429

4

Helix

434 – 436

3

Beta strand

437 – 442

6

Beta strand

445 – 447

3

Helix

449 – 455

7

Beta strand

461 – 465

5

Helix

466 – 478

13

Beta strand

481 – 486

6

Beta strand

487 – 489

3

Helix

490 – 493

4

Helix

500 – 516

17

Helix

520 – 522

3

Turn

527 – 529

3

Beta strand

530 – 535

6

Beta strand

538 – 542

5

Beta strand

547 – 549

3

Helix

550 – 552

3

Beta strand

579 – 586

8

Beta strand

595 – 597

3

Beta strand

605 – 610

6

Beta strand

643 – 645

3

Beta strand

653 – 656

4

Beta strand

660 – 663

4

Beta strand

667 – 672

6

Beta strand

676 – 680

5

Beta strand

683 – 686

4

Beta strand

688 – 692

5

Beta strand

698 – 701

4

Beta strand

703 – 705

3

Beta strand

711 – 714

4

Beta strand

715 – 717

3

Beta strand

720 – 723

4

Beta strand

727 – 729

3

Beta strand

734 – 736

3

Beta strand

737 – 740

4

Beta strand

742 – 745

4

Beta strand

747 – 749

3

Beta strand

755 – 757

3

Turn

772 – 776

5

Beta strand

778 – 783

6

Helix

789 – 792

4

Beta strand

798 – 804

7

Turn

805 – 808

4

Beta strand

809 – 814

6

Helix

815 – 822

8

Helix

825 – 827

3

Beta strand

829 – 836

8

Helix

841 – 851

11

Beta strand

853 – 857

5

Beta strand

862 – 864

3

Beta strand

875 – 877

3

Beta strand

879 – 881

3

Helix

885 – 891

7

Beta strand

897 – 899

3

Beta strand

901 – 903

3

Beta strand

905 – 907

3

Helix

911 – 920

10

Beta strand

925 – 930

6

Sequences

	Sequence		Length	Mass (Da)
	P13671 [UniParc]. Last modified May 1, 2007. Version 3. Checksum: A88F4BED7CC349D3	FASTA	934	104,786
	10 20 30 40 50 60 MARRSVLYFI LLNALINKGQ ACFCDHYAWT QWTSCSKTCN SGTQSRHRQI VVDKYYQENF 70 80 90 100 110 120 CEQICSKQET RECNWQRCPI NCLLGDFGPW SDCDPCIEKQ SKVRSVLRPS QFGGQPCTAP 130 140 150 160 170 180 LVAFQPCIPS KLCKIEEADC KNKFRCDSGR CIARKLECNG ENDCGDNSDE RDCGRTKAVC 190 200 210 220 230 240 TRKYNPIPSV QLMGNGFHFL AGEPRGEVLD NSFTGGICKT VKSSRTSNPY RVPANLENVG 250 260 270 280 290 300 FEVQTAEDDL KTDFYKDLTS LGHNENQQGS FSSQGGSSFS VPIFYSSKRS ENINHNSAFK 310 320 330 340 350 360 QAIQASHKKD SSFIRIHKVM KVLNFTTKAK DLHLSDVFLK ALNHLPLEYN SALYSRIFDD 370 380 390 400 410 420 FGTHYFTSGS LGGVYDLLYQ FSSEELKNSG LTEEEAKHCV RIETKKRVLF AKKTKVEHRC 430 440 450 460 470 480 TTNKLSEKHE GSFIQGAEKS ISLIRGGRSE YGAALAWEKG SSGLEEKTFS EWLESVKENP 490 500 510 520 530 540 AVIDFELAPI VDLVRNIPCA VTKRNNLRKA LQEYAAKFDP CQCAPCPNNG RPTLSGTECL 550 560 570 580 590 600 CVCQSGTYGE NCEKQSPDYK SNAVDGQWGC WSSWSTCDAT YKRSRTRECN NPAPQRGGKR 610 620 630 640 650 660 CEGEKRQEED CTFSIMENNG QPCINDDEEM KEVDLPEIEA DSGCPQPVPP ENGFIRNEKQ 670 680 690 700 710 720 LYLVGEDVEI SCLTGFETVG YQYFRCLPDG TWRQGDVECQ RTECIKPVVQ EVLTITPFQR 730 740 750 760 770 780 LYRIGESIEL TCPKGFVVAG PSRYTCQGNS WTPPISNSLT CEKDTLTKLK GHCQLGQKQS 790 800 810 820 830 840 GSECICMSPE EDCSHHSEDL CVFDTDSNDY FTSPACKFLA EKCLNNQQLH FLHIGSCQDG 850 860 870 880 890 900 RQLEWGLERT RLSSNSTKKE SCGYDTCYDW EKCSASTSKC VCLLPPQCFK GGNQLYCVKM 910 920 930 GSSTSEKTLN ICEVGTIRCA NRKMEILHPG KCLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6." Haefliger J.-A., Tschopp J., Vial N., Jenne D.E. J. Biol. Chem. 264:18041-18051(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-31 AND 633-640.
[2]	"The molecular architecture of human complement component C6." Discipio R.G., Hugli T.E. J. Biol. Chem. 264:16197-16206(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLU-119.
[3]	"Structure of the human C6 gene." Hobart M.J., Fernie B., Discipio R.G. Biochemistry 32:6198-6205(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-119. Tissue: Blood.
[4]	"Sequence variation in C6 locus." Soejima M., Koda Y. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-119. Tissue: Ovary.
[7]	"Structural homology of complement protein C6 with other channel-forming proteins of complement." Chakravarti D.N., Chakravarti B., Parra C.A., Mueller-Eberhard H.J. Proc. Natl. Acad. Sci. U.S.A. 86:2799-2803(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-491, VARIANT GLU-119.
[8]	"Elucidation of the disulfide-bonding pattern in the factor I modules of the sixth component (C6) of human complement." Lengweiler S., Schaller J., DiScipio R.G., Rickli E.E. Biochim. Biophys. Acta 1342:13-18(1997) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS IN FACTOR I MODULE 1 REGION.
[9]	"The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues." Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O. J. Biol. Chem. 274:32786-32794(1999) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT TRP-29; TRP-32; TRP-90; TRP-568; TRP-571 AND TRP-574.
[10]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-324 AND ASN-855, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)." Aleshin A.E., Schraufstatter I.U., Stec B., Bankston L.A., Liddington R.C., DiScipio R.G. J. Biol. Chem. 287:10210-10222(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 22-934, GLYCOSYLATION AT TRP-29; TRP-32; THR-38; ASN-324; THR-392; TRP-568 AND TRP-571, SUBUNIT, DISULFIDE BONDS.
[12]	"Polymorphism of human complement component C6: an amino acid substitution (Glu/Ala) within the second thrombospondin repeat differentiates between the two common allotypes C6 A and C6 B." Dewald G., Nothen M.M., Cichon S. Biochem. Biophys. Res. Commun. 194:458-464(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALLOTYPE C6 A GLU-119.
[13]	"Meningococccal meningitis and complement component 6 deficiency associated with oculocutaneous albinism." Ikinciogullari A., Tekin M., Dogu F., Reisli I., Tanir G., Yi Z., Garrison N., Brilliant M.H., Babacan E. Eur. J. Pediatr. 164:177-179(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN COMPLEMENT COMPONENT 6 DEFICIENCY.
+	Additional computationally mapped references.

Web resources

C6base

C6 mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05064 mRNA. Translation: AAA51860.1.
J05024 mRNA. Translation: AAA59668.1.
X72177 Genomic DNA. Translation: CAA50994.1.
AB126592 mRNA. Translation: BAD02321.1.
AC008863 Genomic DNA. No translation available.
AC091871 Genomic DNA. No translation available.
BC035723 mRNA. Translation: AAH35723.1.
J04506 mRNA. Translation: AAB59433.1.

IPI

IPI00879709.

PIR

A34372.

RefSeq

NP_000056.2. NM_000065.3.
NP_001108603.2. NM_001115131.2.

UniGene

Hs.481992.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3T5O	X-ray	2.87	A	22-934	[»]
4A5W	X-ray	3.50	B	22-934	[»]
4E0S	X-ray	4.21	B	22-934	[»]

ProteinModelPortal

P13671.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13671. 5 interactions.

MINT

MINT-7241404.

STRING

9606.ENSP00000263413.

PTM databases

PhosphoSite

P13671.

Polymorphism databases

DMDM

146345396.

Proteomic databases

PaxDb

P13671.

PRIDE

P13671.

Protocols and materials databases

DNASU

729.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263413; ENSP00000263413; ENSG00000039537.
ENST00000337836; ENSP00000338861; ENSG00000039537.

GeneID

729.

KEGG

hsa:729.

UCSC

uc003jmk.2. human.

Organism-specific databases

CTD

729.

GeneCards

GC05M041178.

H-InvDB

HIX0024838.

HGNC

HGNC:1339. C6.

HPA

HPA043823.

MIM

217050. gene.
612446. phenotype.

neXtProt

NX_P13671.

Orphanet

169150. Immunodeficiency due to a late component of complements deficiency.

PharmGKB

PA25921.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG145238.

HOGENOM

HOG000111865.

HOVERGEN

HBG005366.

InParanoid

P13671.

KO

K03995.

OMA

CVCQSGT.

OrthoDB

EOG4QRH3K.

PhylomeDB

P13671.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P13671.

Bgee

P13671.

CleanEx

HS_C6.

Genevestigator

P13671.

GermOnline

ENSG00000039537. Homo sapiens.

Family and domain databases

InterPro

IPR003884. FacI_MAC.
IPR002350. Kazal_dom.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001862. MAC_perforin.
IPR020864. MACPF.
IPR020863. MACPF_CS.
IPR000436. Sushi_SCR_CCP.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]

Pfam

PF07648. Kazal_2. 1 hit.
PF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00084. Sushi. 2 hits.
PF00090. TSP_1. 3 hits.
[Graphical view]

PRINTS

PR00764. COMPLEMENTC9.

SMART

SM00032. CCP. 2 hits.
SM00057. FIMAC. 2 hits.
SM00280. KAZAL. 1 hit.
SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 2 hits.
SSF57424. LDL_rcpt_classA_cys-rich. 1 hit.
SSF82895. TSP1. 3 hits.

PROSITE

PS00022. EGF_1. 1 hit.
PS01186. EGF_2. False negative.
PS50026. EGF_3. False negative.
PS51465. KAZAL_2. 2 hits.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
PS50923. SUSHI. 2 hits.
PS50092. TSP1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

C6. human.

GenomeRNAi

729.

NextBio

2968.

SOURCE

Search...

Entry information

Entry name

CO6_HUMAN

Accession

Primary (citable) accession number: P13671

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 147 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.