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P10643

- CO7_HUMAN

UniProt

P10643 - CO7_HUMAN

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Protein
Complement component C7
Gene
C7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. C7 serves as a membrane anchor.

GO - Biological processi

  1. cellular sodium ion homeostasis Source: Ensembl
  2. complement activation Source: ProtInc
  3. complement activation, alternative pathway Source: UniProtKB-KW
  4. complement activation, classical pathway Source: UniProtKB-KW
  5. cytolysis Source: UniProtKB-KW
  6. innate immune response Source: Reactome
  7. regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Complement alternate pathway, Complement pathway, Cytolysis, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.
REACT_8028. Terminal pathway of complement.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement component C7
Gene namesi
Name:C7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1346. C7.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. membrane attack complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane attack complex, Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 7 deficiency (C7D) [MIM:610102]: 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.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti220 – 2201R → Q in C7D. 1 Publication
VAR_012643
Natural varianti379 – 3791G → R in C7D. 1 Publication
VAR_012644
Natural varianti521 – 5211R → S in C7D. 1 Publication
Corresponds to variant rs121964920 [ dbSNP | Ensembl ].
VAR_012645
Natural varianti682 – 6821E → Q in C7D. 1 Publication
VAR_012646
Natural varianti687 – 6871R → H in C7D. 1 Publication
VAR_012647

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610102. phenotype.
Orphaneti169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBiPA25941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222
Add
BLAST
Chaini23 – 843821Complement component C7
PRO_0000023583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361C-linked (Man)1 Publication
Disulfide bondi85 ↔ 96 By similarity
Disulfide bondi91 ↔ 109 By similarity
Disulfide bondi103 ↔ 119 By similarity
Disulfide bondi128 ↔ 165 By similarity
Glycosylationi202 – 2021N-linked (GlcNAc...)2 Publications
Disulfide bondi337 ↔ 3531 Publication
Glycosylationi503 – 5031C-linked (Man); partial1 Publication
Glycosylationi506 – 5061C-linked (Man); partial1 Publication
Glycosylationi509 – 5091C-linked (Man); partial1 Publication
Disulfide bondi571 ↔ 613 By similarity
Disulfide bondi599 ↔ 626 By similarity
Disulfide bondi631 ↔ 673 By similarity
Disulfide bondi659 ↔ 688 By similarity
Glycosylationi696 – 6961O-linked (GalNAc...)1 Publication
Disulfide bondi702 ↔ 7131 Publication
Disulfide bondi715 ↔ 7501 Publication
Disulfide bondi721 ↔ 7431 Publication
Disulfide bondi728 ↔ 7631 Publication
Glycosylationi754 – 7541N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi773 ↔ 7821 Publication
Disulfide bondi776 ↔ 7891 Publication
Disulfide bondi791 ↔ 8251 Publication
Disulfide bondi797 ↔ 8181 Publication
Disulfide bondi805 ↔ 8381 Publication

Post-translational modificationi

C7 has 28 disulfide bridges.
O- and C-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP10643.
PaxDbiP10643.
PRIDEiP10643.

PTM databases

PhosphoSiteiP10643.

Expressioni

Gene expression databases

BgeeiP10643.
CleanExiHS_C7.
GenevestigatoriP10643.

Organism-specific databases

HPAiHPA001465.

Interactioni

Subunit structurei

Monomer or dimer; as a C5b-7 complex it can also form multimeric rosettes. MAC assembly is initiated by protelytic cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the pore-forming subunit C9.

Protein-protein interaction databases

BioGridi107191. 3 interactions.
IntActiP10643. 2 interactions.
MINTiMINT-7032139.
STRINGi9606.ENSP00000322061.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi706 – 7094
Beta strandi712 – 7154
Helixi718 – 7203
Beta strandi726 – 7316
Turni732 – 7343
Beta strandi737 – 7415
Helixi742 – 7509
Beta strandi755 – 7573
Beta strandi766 – 7694
Beta strandi778 – 7825
Beta strandi784 – 7918
Helixi794 – 7963
Beta strandi803 – 8086
Beta strandi811 – 8166
Helixi817 – 82610
Beta strandi831 – 8366

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WCYNMR-A693-843[»]
ProteinModelPortaliP10643.
SMRiP10643. Positions 25-843.

Miscellaneous databases

EvolutionaryTraceiP10643.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 8054TSP type-1 1
Add
BLAST
Domaini83 – 12139LDL-receptor class A
Add
BLAST
Domaini124 – 456333MACPF
Add
BLAST
Domaini457 – 48731EGF-like
Add
BLAST
Domaini500 – 54950TSP type-1 2
Add
BLAST
Domaini569 – 62860Sushi 1
Add
BLAST
Domaini629 – 69062Sushi 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni545 – 61571CCP 1
Add
BLAST
Regioni616 – 69378CCP 2
Add
BLAST
Regioni695 – 77076Factor I module (FIM) 1
Add
BLAST
Regioni771 – 84373Factor I module (FIM) 2
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.
Contains 1 MACPF domain.
Contains 2 TSP type-1 domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG145238.
HOGENOMiHOG000111868.
HOVERGENiHBG005367.
InParanoidiP10643.
KOiK03996.
OMAiLLEPHCF.
OrthoDBiEOG7ZSHS9.
PhylomeDBiP10643.
TreeFamiTF330498.

Family and domain databases

Gene3Di4.10.400.10. 1 hit.
InterProiIPR003884. FacI_MAC.
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]
PfamiPF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00084. Sushi. 2 hits.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR00764. COMPLEMENTC9.
SMARTiSM00032. CCP. 2 hits.
SM00057. FIMAC. 2 hits.
SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 2 hits.
SSF82895. SSF82895. 2 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10643-1 [UniParc]FASTAAdd to Basket

« Hide

MKVISLFILV GFIGEFQSFS SASSPVNCQW DFYAPWSECN GCTKTQTRRR    50
SVAVYGQYGG QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS 100
LVCNGDSDCD EDSADEDRCE DSERRPSCDI DKPPPNIELT GNGYNELTGQ 150
FRNRVINTKS FGGQCRKVFS GDGKDFYRLS GNVLSYTFQV KINNDFNYEF 200
YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTSHTN EIHKGKSYQL 250
LVVENTVEVA QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG 300
THYLQSGSLG GEYRVLFYVD SEKLKQNDFN SVEEKKCKSS GWHFVVKFSS 350
HGCKELENAL KAASGTQNNV LRGEPFIRGG GAGFISGLSY LELDNPAGNK 400
RRYSAWAESV TNLPQVIKQK LTPLYELVKE VPCASVKKLY LKWALEEYLD 450
EFDPCHCRPC QNGGLATVEG THCLCHCKPY TFGAACEQGV LVGNQAGGVD 500
GGWSCWSSWS PCVQGKKTRS RECNNPPPSG GGRSCVGETT ESTQCEDEEL 550
EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN 600
EGYSLIGNPV ARCGEDLRWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT 650
VGEKVTVSCS GGMSLEGPSA FLCGSSLKWS PEMKNARCVQ KENPLTQAVP 700
KCQRWEKLQN SRCVCKMPYE CGPSLDVCAQ DERSKRILPL TVCKMHVLHC 750
QGRNYTLTGR DSCTLPASAE KACGACPLWG KCDAESSKCV CREASECEEE 800
GFSICVEVNG KEQTMSECEA GALRCRGQSI SVTSIRPCAA ETQ 843
Length:843
Mass (Da):93,518
Last modified:March 15, 2005 - v2
Checksum:iDBD5D7C92DF71FA5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281C → R.
Corresponds to variant rs2271708 [ dbSNP | Ensembl ].
VAR_050480
Natural varianti220 – 2201R → Q in C7D. 1 Publication
VAR_012643
Natural varianti379 – 3791G → R in C7D. 1 Publication
VAR_012644
Natural varianti389 – 3891S → T Polymorphism confirmed at protein level. 2 Publications
Corresponds to variant rs1063499 [ dbSNP | Ensembl ].
VAR_033798
Natural varianti420 – 4201K → Q.
Corresponds to variant rs3792646 [ dbSNP | Ensembl ].
VAR_022023
Natural varianti521 – 5211R → S in C7D. 1 Publication
Corresponds to variant rs121964920 [ dbSNP | Ensembl ].
VAR_012645
Natural varianti587 – 5871T → P Polymorphism confirmed at protein level. 2 Publications
Corresponds to variant rs13157656 [ dbSNP | Ensembl ].
VAR_033799
Natural varianti682 – 6821E → Q in C7D. 1 Publication
VAR_012646
Natural varianti687 – 6871R → H in C7D. 1 Publication
VAR_012647

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521R → V in CAA60121. 1 Publication
Sequence conflicti821 – 8222GA → AL1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03507 mRNA. Translation: AAA51861.1.
BC063851 mRNA. Translation: AAH63851.1.
X86328
, X86329, X86330, X86331, X86332, X86333, X86334, X86335, X86336, X86337, X86338, X86339, X86340, X86341, X86342, X86343, X86344 Genomic DNA. Translation: CAA60121.1.
CCDSiCCDS47201.1.
PIRiA27340.
RefSeqiNP_000578.2. NM_000587.2.
UniGeneiHs.78065.

Genome annotation databases

EnsembliENST00000313164; ENSP00000322061; ENSG00000112936.
GeneIDi730.
KEGGihsa:730.
UCSCiuc003jmh.3. human.

Polymorphism databases

DMDMi61252057.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C7base

C7 mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03507 mRNA. Translation: AAA51861.1 .
BC063851 mRNA. Translation: AAH63851.1 .
X86328
, X86329 , X86330 , X86331 , X86332 , X86333 , X86334 , X86335 , X86336 , X86337 , X86338 , X86339 , X86340 , X86341 , X86342 , X86343 , X86344 Genomic DNA. Translation: CAA60121.1 .
CCDSi CCDS47201.1.
PIRi A27340.
RefSeqi NP_000578.2. NM_000587.2.
UniGenei Hs.78065.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WCY NMR - A 693-843 [» ]
ProteinModelPortali P10643.
SMRi P10643. Positions 25-843.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107191. 3 interactions.
IntActi P10643. 2 interactions.
MINTi MINT-7032139.
STRINGi 9606.ENSP00000322061.

PTM databases

PhosphoSitei P10643.

Polymorphism databases

DMDMi 61252057.

Proteomic databases

MaxQBi P10643.
PaxDbi P10643.
PRIDEi P10643.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313164 ; ENSP00000322061 ; ENSG00000112936 .
GeneIDi 730.
KEGGi hsa:730.
UCSCi uc003jmh.3. human.

Organism-specific databases

CTDi 730.
GeneCardsi GC05P040909.
HGNCi HGNC:1346. C7.
HPAi HPA001465.
MIMi 217070. gene.
610102. phenotype.
neXtProti NX_P10643.
Orphaneti 169150. Immunodeficiency due to a late component of complements deficiency.
PharmGKBi PA25941.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145238.
HOGENOMi HOG000111868.
HOVERGENi HBG005367.
InParanoidi P10643.
KOi K03996.
OMAi LLEPHCF.
OrthoDBi EOG7ZSHS9.
PhylomeDBi P10643.
TreeFami TF330498.

Enzyme and pathway databases

Reactomei REACT_118707. Regulation of Complement cascade.
REACT_8028. Terminal pathway of complement.

Miscellaneous databases

ChiTaRSi C7. human.
EvolutionaryTracei P10643.
GenomeRNAii 730.
NextBioi 2972.
PROi P10643.
SOURCEi Search...

Gene expression databases

Bgeei P10643.
CleanExi HS_C7.
Genevestigatori P10643.

Family and domain databases

Gene3Di 4.10.400.10. 1 hit.
InterProi IPR003884. FacI_MAC.
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 ]
Pfami PF00057. Ldl_recept_a. 1 hit.
PF01823. MACPF. 1 hit.
PF00084. Sushi. 2 hits.
PF00090. TSP_1. 2 hits.
[Graphical view ]
PRINTSi PR00764. COMPLEMENTC9.
SMARTi SM00032. CCP. 2 hits.
SM00057. FIMAC. 2 hits.
SM00192. LDLa. 1 hit.
SM00457. MACPF. 1 hit.
SM00209. TSP1. 2 hits.
[Graphical view ]
SUPFAMi SSF57535. SSF57535. 2 hits.
SSF82895. SSF82895. 2 hits.
PROSITEi PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
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. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of human complement component C7 and the C5b-7 complex."
    Discipio R.G., Chakravari D.N., Mueller-Eberhard H.J., Fey G.H.
    J. Biol. Chem. 263:549-560(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT PRO-587.
  2. "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].
    Tissue: PNS.
  3. "Structure of the human C7 gene and comparison with the C6, C8A, C8B and C9 genes."
    Hobart M.J., Fernie B.A., DiScipio R.G.
    J. Immunol. 154:5188-5194(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-822, VARIANT THR-389.
  4. "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-36; TRP-503; TRP-506 AND TRP-509.
  5. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202.
    Tissue: Plasma.
  6. "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-202 AND ASN-754.
    Tissue: Plasma.
  7. Cited for: GLYCOSYLATION AT ASN-754.
  8. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
    Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
    Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-696, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement."
    Phelan M.M., Thai C.-T., Soares D.C., Ogata R.T., Barlow P.N., Bramham J.
    J. Biol. Chem. 284:19637-19649(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 693-843, DISULFIDE BONDS.
  10. "Molecular bases of combined subtotal deficiencies of C6 and C7: their effects in combination with other C6 and C7 deficiencies."
    Fernie B.A., Wurzner R., Orren A., Morgan B.P., Potter P.C., Platonov A.E., Vershinina I.V., Shipulin G.A., Lachmann P.J., Hobart M.J.
    J. Immunol. 157:3648-3657(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT C7D SER-521.
  11. "Molecular bases of C7 deficiency: three different defects."
    Fernie B.A., Orren A., Sheehan G., Schlesinger M., Hobart M.J.
    J. Immunol. 159:1019-1026(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT C7D ARG-379.
  12. "Complement C7 deficiency: seven further molecular defects and their associated marker haplotypes."
    Fernie B.A., Hobart M.J.
    Hum. Genet. 103:513-519(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS C7D GLN-220; GLN-682 AND HIS-687.
  13. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
    Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
    J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-389 AND PRO-587, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCO7_HUMAN
AccessioniPrimary (citable) accession number: P10643
Secondary accession number(s): Q6P3T5, Q92489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 15, 2005
Last modified: September 3, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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