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P02745

- C1QA_HUMAN

UniProt

P02745 - C1QA_HUMAN

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Protein
Complement C1q subcomponent subunit A
Gene
C1QA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca2+-dependent C1r2C1s2 proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. complement activation Source: Reactome
  3. complement activation, classical pathway Source: Reactome
  4. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1q subcomponent subunit A
Gene namesi
Name:C1QA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1241. C1QA.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. complement component C1 complex Source: ProtInc
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component C1q deficiency (C1QD) [MIM:613652]: A disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi613652. phenotype.
Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBiPA25622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22221 Publication
Add
BLAST
Chaini23 – 245223Complement C1q subcomponent subunit A
PRO_0000003517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 – 26Interchain (with C-29 in B chain)
Modified residuei33 – 3315-hydroxylysine; alternate
Glycosylationi33 – 331O-linked (Gal...); alternate
Modified residuei39 – 3914-hydroxyproline
Modified residuei45 – 4514-hydroxyproline
Modified residuei48 – 4815-hydroxylysine; alternate
Glycosylationi48 – 481O-linked (Gal...); alternate
Modified residuei54 – 5414-hydroxyproline
Modified residuei57 – 5714-hydroxyproline
Modified residuei67 – 6715-hydroxylysine; alternate
Glycosylationi67 – 671O-linked (Gal...); alternate
Modified residuei73 – 7314-hydroxyproline
Modified residuei79 – 7914-hydroxyproline
Modified residuei85 – 8514-hydroxyproline
Modified residuei100 – 10015-hydroxylysine; alternate
Glycosylationi100 – 1001O-linked (Gal...); alternate
Glycosylationi146 – 1461N-linked (GlcNAc...)2 Publications

Post-translational modificationi

O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP02745.
PeptideAtlasiP02745.
PRIDEiP02745.

Expressioni

Gene expression databases

BgeeiP02745.
CleanExiHS_C1QA.
GenevestigatoriP02745.

Organism-specific databases

HPAiCAB009823.
HPA002350.

Interactioni

Subunit structurei

C1 is a calcium-dependent trimolecular complex of C1q, R and S in the molar ration of 1:2:2. C1q subcomponent is composed of nine subunits, six of which are disulfide-linked dimers of the A and B chains, and three of which are disulfide-linked dimers of the C chain.

Binary interactionsi

WithEntry#Exp.IntActNotes
C1QBP027464EBI-1220209,EBI-2813376

Protein-protein interaction databases

BioGridi107173. 16 interactions.
IntActiP02745. 15 interactions.
MINTiMINT-1195525.
STRINGi9606.ENSP00000363773.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi116 – 1205
Beta strandi128 – 1314
Beta strandi135 – 1406
Turni146 – 1483
Beta strandi150 – 1523
Beta strandi157 – 16913
Beta strandi171 – 1799
Beta strandi182 – 1843
Beta strandi188 – 1914
Beta strandi195 – 1973
Beta strandi199 – 20911
Beta strandi214 – 22411
Beta strandi229 – 2324
Beta strandi235 – 2439

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PK6X-ray1.85A112-244[»]
2JG8X-ray2.05A/D112-245[»]
2JG9X-ray1.90A/D112-245[»]
2WNUX-ray2.30A/D112-245[»]
2WNVX-ray1.25A/D112-245[»]
ProteinModelPortaliP02745.
SMRiP02745. Positions 112-244.

Miscellaneous databases

EvolutionaryTraceiP02745.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 10979Collagen-like
Add
BLAST
Domaini110 – 245136C1q
Add
BLAST

Sequence similaritiesi

Contains 1 C1q domain.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG126311.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
KOiK03986.
OMAiYYYFTFQ.
OrthoDBiEOG70ZZPW.
PhylomeDBiP02745.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02745-1 [UniParc]FASTAAdd to Basket

« Hide

MEGPRGWLVL CVLAISLASM VTEDLCRAPD GKKGEAGRPG RRGRPGLKGE    50
QGEPGAPGIR TGIQGLKGDQ GEPGPSGNPG KVGYPGPSGP LGARGIPGIK 100
GTKGSPGNIK DQPRPAFSAI RRNPPMGGNV VIFDTVITNQ EEPYQNHSGR 150
FVCTVPGYYY FTFQVLSQWE ICLSIVSSSR GQVRRSLGFC DTTNKGLFQV 200
VSGGMVLQLQ QGDQVWVEKD PKKGHIYQGS EADSVFSGFL IFPSA 245
Length:245
Mass (Da):26,017
Last modified:July 1, 1993 - v2
Checksum:i8FF6B6AE02D49C4C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231E → K.1 Publication
Corresponds to variant rs17887074 [ dbSNP | Ensembl ].
VAR_021090

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971P → K AA sequence 1 Publication
Sequence conflicti103 – 1031K → P AA sequence 1 Publication
Sequence conflicti172 – 1721C → N AA sequence 1 Publication
Sequence conflicti178 – 1781S → W AA sequence 1 Publication
Sequence conflicti240 – 2434LIFP → ILPGF AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135157 mRNA. Translation: AAD32626.1.
AY789471 Genomic DNA. Translation: AAV40828.1.
AL158086 Genomic DNA. Translation: CAI22892.1.
AK311980 mRNA. Translation: BAG34919.1.
AL158086 Genomic DNA. Translation: CAI22893.1.
CH471134 Genomic DNA. Translation: EAW95014.1.
BC030153 mRNA. Translation: AAH30153.1.
BC071986 mRNA. Translation: AAH71986.1.
CCDSiCCDS226.1.
PIRiS14350. C1HUQA.
RefSeqiNP_057075.1. NM_015991.2.
UniGeneiHs.632379.

Genome annotation databases

EnsembliENST00000374642; ENSP00000363773; ENSG00000173372.
ENST00000402322; ENSP00000385564; ENSG00000173372.
GeneIDi712.
KEGGihsa:712.
UCSCiuc001bfy.3. human.

Polymorphism databases

DMDMi399138.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C1QAbase

C1QA mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF135157 mRNA. Translation: AAD32626.1 .
AY789471 Genomic DNA. Translation: AAV40828.1 .
AL158086 Genomic DNA. Translation: CAI22892.1 .
AK311980 mRNA. Translation: BAG34919.1 .
AL158086 Genomic DNA. Translation: CAI22893.1 .
CH471134 Genomic DNA. Translation: EAW95014.1 .
BC030153 mRNA. Translation: AAH30153.1 .
BC071986 mRNA. Translation: AAH71986.1 .
CCDSi CCDS226.1.
PIRi S14350. C1HUQA.
RefSeqi NP_057075.1. NM_015991.2.
UniGenei Hs.632379.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PK6 X-ray 1.85 A 112-244 [» ]
2JG8 X-ray 2.05 A/D 112-245 [» ]
2JG9 X-ray 1.90 A/D 112-245 [» ]
2WNU X-ray 2.30 A/D 112-245 [» ]
2WNV X-ray 1.25 A/D 112-245 [» ]
ProteinModelPortali P02745.
SMRi P02745. Positions 112-244.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107173. 16 interactions.
IntActi P02745. 15 interactions.
MINTi MINT-1195525.
STRINGi 9606.ENSP00000363773.

Chemistry

DrugBanki DB00054. Abciximab.
DB00051. Adalimumab.
DB00092. Alefacept.
DB00087. Alemtuzumab.
DB00074. Basiliximab.
DB00112. Bevacizumab.
DB00002. Cetuximab.
DB00111. Daclizumab.
DB00095. Efalizumab.
DB00005. Etanercept.
DB00056. Gemtuzumab ozogamicin.
DB00078. Ibritumomab.
DB00028. Immune globulin.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

Polymorphism databases

DMDMi 399138.

Proteomic databases

PaxDbi P02745.
PeptideAtlasi P02745.
PRIDEi P02745.

Protocols and materials databases

DNASUi 712.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374642 ; ENSP00000363773 ; ENSG00000173372 .
ENST00000402322 ; ENSP00000385564 ; ENSG00000173372 .
GeneIDi 712.
KEGGi hsa:712.
UCSCi uc001bfy.3. human.

Organism-specific databases

CTDi 712.
GeneCardsi GC01P022962.
HGNCi HGNC:1241. C1QA.
HPAi CAB009823.
HPA002350.
MIMi 120550. gene.
613652. phenotype.
neXtProti NX_P02745.
Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBi PA25622.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG126311.
HOGENOMi HOG000085653.
HOVERGENi HBG108220.
KOi K03986.
OMAi YYYFTFQ.
OrthoDBi EOG70ZZPW.
PhylomeDBi P02745.
TreeFami TF329591.

Enzyme and pathway databases

Reactomei REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

ChiTaRSi C1QA. human.
EvolutionaryTracei P02745.
GeneWikii C1QA.
GenomeRNAii 712.
NextBioi 2894.
PROi P02745.
SOURCEi Search...

Gene expression databases

Bgeei P02745.
CleanExi HS_C1QA.
Genevestigatori P02745.

Family and domain databases

Gene3Di 2.60.120.40. 1 hit.
InterProi IPR001073. C1q.
IPR008160. Collagen.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view ]
Pfami PF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
[Graphical view ]
PRINTSi PR00007. COMPLEMNTC1Q.
SMARTi SM00110. C1Q. 1 hit.
[Graphical view ]
SUPFAMi SSF49842. SSF49842. 1 hit.
PROSITEi PS50871. C1Q. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q."
    Sellar G.C., Blake D.J., Reid K.B.M.
    Biochem. J. 274:481-490(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Monocyte.
  2. Wan T., Zhang W., Cao X.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. SeattleSNPs variation discovery resource
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-23.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Spleen.
  8. "Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
    Reid K.B.M.
    Biochem. J. 179:367-371(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-130, HYDROXYLATION AT LYS-33; PRO-39; PRO-45; LYS-48; PRO-54; PRO-57; LYS-67; PRO-73; PRO-79; PRO-85 AND LYS-100.
  9. "Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement."
    Reid K.B.M., Gagnon J., Frampton J.
    Biochem. J. 203:559-569(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 131-245.
  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-146.
    Tissue: Plasma.
  11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146.
    Tissue: Liver.
  12. "The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties."
    Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.-C., Arlaud G.J.
    J. Biol. Chem. 278:46974-46982(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 112-244.
  13. "Molecular basis of hereditary C1q deficiency."
    Petry F.
    Immunobiology 199:286-294(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON C1Q DEFICIENCY.

Entry informationi

Entry nameiC1QA_HUMAN
AccessioniPrimary (citable) accession number: P02745
Secondary accession number(s): B2R4X2, Q5T963
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 160 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 1
    Human chromosome 1: 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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