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P02747

- C1QC_HUMAN

UniProt

P02747 - C1QC_HUMAN

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Protein

Complement C1q subcomponent subunit C

Gene

C1QC

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 - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, classical pathway Source: Reactome
  3. immune response Source: UniProtKB
  4. innate immune response Source: Reactome
  5. negative regulation of granulocyte differentiation Source: BHF-UCL
  6. negative regulation of macrophage differentiation Source: BHF-UCL
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 C
Gene namesi
Name:C1QC
Synonyms:C1QG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1245. C1QC.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. collagen trimer Source: UniProtKB-KW
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: UniProt
  5. 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341G → R in C1QD. 1 Publication
VAR_008542

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613652. phenotype.
Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBiPA25626.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 28281 PublicationAdd
BLAST
Chaini29 – 245217Complement C1q subcomponent subunit CPRO_0000003524Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 – 32Interchain
Modified residuei36 – 3614-hydroxyproline1 Publication
Modified residuei39 – 3914-hydroxyproline1 Publication
Modified residuei42 – 4214-hydroxyproline1 Publication
Modified residuei45 – 4514-hydroxyproline1 Publication
Modified residuei54 – 5414-hydroxyproline1 Publication
Modified residuei63 – 6314-hydroxyproline1 Publication
Modified residuei75 – 7515-hydroxylysine1 Publication
Glycosylationi75 – 751O-linked (Gal...)
Modified residuei81 – 8114-hydroxyproline1 Publication
Modified residuei93 – 9314-hydroxyproline1 Publication
Modified residuei96 – 9614-hydroxyproline1 Publication
Modified residuei99 – 9914-hydroxyproline1 Publication
Modified residuei105 – 10514-hydroxyproline1 Publication

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

PaxDbiP02747.
PeptideAtlasiP02747.
PRIDEiP02747.

Miscellaneous databases

PMAP-CutDBP02747.

Expressioni

Gene expression databases

BgeeiP02747.
CleanExiHS_C1QC.
GenevestigatoriP02747.

Organism-specific databases

HPAiCAB009828.
HPA001471.

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.

Protein-protein interaction databases

BioGridi107175. 2 interactions.
IntActiP02747. 3 interactions.
MINTiMINT-6630018.
STRINGi9606.ENSP00000363768.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi116 – 1183Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi142 – 1454Combined sources
Turni153 – 1553Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi164 – 17613Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi187 – 1948Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi201 – 21111Combined sources
Beta strandi216 – 22510Combined sources
Beta strandi236 – 2449Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PK6X-ray1.85C117-245[»]
2JG8X-ray2.05C/F115-245[»]
2JG9X-ray1.90C/F115-245[»]
2WNUX-ray2.30C/F115-245[»]
2WNVX-ray1.25C/F115-245[»]
ProteinModelPortaliP02747.
SMRiP02747. Positions 66-94, 117-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02747.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 11282Collagen-likeAdd
BLAST
Domaini115 – 245131C1qPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG115796.
GeneTreeiENSGT00760000118830.
HOGENOMiHOG000085653.
HOVERGENiHBG108220.
InParanoidiP02747.
KOiK03988.
OMAiQTANLCV.
OrthoDBiEOG70ZZPW.
PhylomeDBiP02747.
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. 2 hits.
[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.

P02747-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDVGPSSLPH LGLKLLLLLL LLPLRGQANT GCYGIPGMPG LPGAPGKDGY
60 70 80 90 100
DGLPGPKGEP GIPAIPGIRG PKGQKGEPGL PGHPGKNGPM GPPGMPGVPG
110 120 130 140 150
PMGIPGEPGE EGRYKQKFQS VFTVTRQTHQ PPAPNSLIRF NAVLTNPQGD
160 170 180 190 200
YDTSTGKFTC KVPGLYYFVY HASHTANLCV LLYRSGVKVV TFCGHTSKTN
210 220 230 240
QVNSGGVLLR LQVGEEVWLA VNDYYDMVGI QGSDSVFSGF LLFPD
Length:245
Mass (Da):25,774
Last modified:April 16, 2002 - v3
Checksum:iFA17117EB7ABFC12
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141K → R in BAB71575. (PubMed:14702039)Curated
Sequence conflicti23 – 231P → A no nucleotide entry (PubMed:1706597)Curated
Sequence conflicti26 – 272GQ → AK in AAP97191. 1 PublicationCurated
Sequence conflicti57 – 571K → P AA sequence (PubMed:486087)Curated
Sequence conflicti66 – 661P → K AA sequence (PubMed:486087)Curated
Sequence conflicti72 – 721K → P AA sequence (PubMed:486087)Curated
Sequence conflicti84 – 841P → K AA sequence (PubMed:486087)Curated
Sequence conflicti87 – 871N → D AA sequence (PubMed:486087)Curated
Sequence conflicti90 – 901M → N AA sequence (PubMed:486087)Curated
Sequence conflicti104 – 1041I → F in AAP97191. 1 PublicationCurated
Sequence conflicti149 – 1491G → E in AAP97191. 1 PublicationCurated
Sequence conflicti215 – 2151E → G in BAB71575. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341G → R in C1QD. 1 Publication
VAR_008542

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087892 mRNA. Translation: AAP97191.1.
AK057792 mRNA. Translation: BAB71575.1.
AL158086 Genomic DNA. Translation: CAI22894.1.
BC009016 mRNA. Translation: AAH09016.1.
CCDSiCCDS227.1.
PIRiS14351. C1HUQC.
RefSeqiNP_001107573.1. NM_001114101.1.
NP_758957.2. NM_172369.3.
UniGeneiHs.467753.

Genome annotation databases

EnsembliENST00000374637; ENSP00000363768; ENSG00000159189.
ENST00000374639; ENSP00000363770; ENSG00000159189.
ENST00000374640; ENSP00000363771; ENSG00000159189.
GeneIDi714.
KEGGihsa:714.
UCSCiuc001bga.4. human.

Polymorphism databases

DMDMi20178281.

Cross-referencesi

Web resourcesi

C1QGbase

C1QC mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087892 mRNA. Translation: AAP97191.1 .
AK057792 mRNA. Translation: BAB71575.1 .
AL158086 Genomic DNA. Translation: CAI22894.1 .
BC009016 mRNA. Translation: AAH09016.1 .
CCDSi CCDS227.1.
PIRi S14351. C1HUQC.
RefSeqi NP_001107573.1. NM_001114101.1.
NP_758957.2. NM_172369.3.
UniGenei Hs.467753.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PK6 X-ray 1.85 C 117-245 [» ]
2JG8 X-ray 2.05 C/F 115-245 [» ]
2JG9 X-ray 1.90 C/F 115-245 [» ]
2WNU X-ray 2.30 C/F 115-245 [» ]
2WNV X-ray 1.25 C/F 115-245 [» ]
ProteinModelPortali P02747.
SMRi P02747. Positions 66-94, 117-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107175. 2 interactions.
IntActi P02747. 3 interactions.
MINTi MINT-6630018.
STRINGi 9606.ENSP00000363768.

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.
DB00075. Muromonab.
DB00108. Natalizumab.
DB00110. Palivizumab.
DB00073. Rituximab.
DB00081. Tositumomab.
DB00072. Trastuzumab.

Polymorphism databases

DMDMi 20178281.

Proteomic databases

PaxDbi P02747.
PeptideAtlasi P02747.
PRIDEi P02747.

Protocols and materials databases

DNASUi 714.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374637 ; ENSP00000363768 ; ENSG00000159189 .
ENST00000374639 ; ENSP00000363770 ; ENSG00000159189 .
ENST00000374640 ; ENSP00000363771 ; ENSG00000159189 .
GeneIDi 714.
KEGGi hsa:714.
UCSCi uc001bga.4. human.

Organism-specific databases

CTDi 714.
GeneCardsi GC01P022970.
HGNCi HGNC:1245. C1QC.
HPAi CAB009828.
HPA001471.
MIMi 120575. gene.
613652. phenotype.
neXtProti NX_P02747.
Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBi PA25626.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG115796.
GeneTreei ENSGT00760000118830.
HOGENOMi HOG000085653.
HOVERGENi HBG108220.
InParanoidi P02747.
KOi K03988.
OMAi QTANLCV.
OrthoDBi EOG70ZZPW.
PhylomeDBi P02747.
TreeFami TF329591.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi C1QC. human.
EvolutionaryTracei P02747.
GenomeRNAii 714.
NextBioi 2902.
PMAP-CutDB P02747.
PROi P02747.
SOURCEi Search...

Gene expression databases

Bgeei P02747.
CleanExi HS_C1QC.
Genevestigatori P02747.

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. 2 hits.
[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. "Cloning and characterization of a novel human cDNA homology to murine C1q C-chain mRNA."
    Dai F.Y., Yu L., Wan Y.Z., Zhang H.L., Huang J., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Cerebellum.
  4. "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].
  5. "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: Brain.
  6. "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 29-122, HYDROXYLATION AT PRO-36; PRO-39; PRO-42; PRO-45; PRO-54; PRO-63; LYS-75; PRO-81; PRO-93; PRO-96; PRO-99 AND PRO-105.
  7. "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 117-245.
  8. "Molecular basis of hereditary C1q deficiency."
    Petry F.
    Immunobiology 199:286-294(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON C1Q DEFICIENCY.
  9. "Homozygous hereditary C1q deficiency and systemic lupus erythematosus. A new family and the molecular basis of C1q deficiency in three families."
    Slingsby J.H., Norsworthy P., Pearce G., Vaishnaw A.K., Issler H., Morley B.J., Walport M.J.
    Arthritis Rheum. 39:663-670(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT C1QD ARG-34.

Entry informationi

Entry nameiC1QC_HUMAN
AccessioniPrimary (citable) accession number: P02747
Secondary accession number(s): Q7Z502, Q96DL2, Q96H05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: November 26, 2014
This is version 159 of the entry and version 3 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