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Q14993

- COJA1_HUMAN

UniProt

Q14993 - COJA1_HUMAN

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Protein

Collagen alpha-1(XIX) chain

Gene

COL19A1

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

Functioni

May act as a cross-bridge between fibrils and other extracellular matrix molecules. Involved in skeletal myogenesis in the developing esophagus. May play a role in organization of the pericellular matrix or the sphinteric smooth muscle.1 Publication

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: UniProtKB
  2. protein binding, bridging Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. cell differentiation Source: UniProtKB-KW
  3. collagen catabolic process Source: Reactome
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: UniProtKB
  6. single organismal cell-cell adhesion Source: UniProtKB
  7. skeletal muscle tissue development Source: Ensembl
  8. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion, Differentiation, Myogenesis

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150401. Collagen degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XIX) chain
Alternative name(s):
Collagen alpha-1(Y) chain
Gene namesi
Name:COL19A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2196. COL19A1.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 11421119Collagen alpha-1(XIX) chainPRO_0000005797Add
BLAST

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PaxDbiQ14993.
PRIDEiQ14993.

PTM databases

PhosphoSiteiQ14993.

Expressioni

Tissue specificityi

Localized to vascular, neuronal, mesenchymal, and some epithelial basement membrane zones in umbilical cord.1 Publication

Gene expression databases

BgeeiQ14993.
ExpressionAtlasiQ14993. baseline.
GenevestigatoriQ14993.

Organism-specific databases

HPAiHPA042422.

Interactioni

Subunit structurei

Oligomer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi107705. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ14993.
SMRiQ14993. Positions 51-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 234185Laminin G-likeAdd
BLAST
Domaini292 – 34958Collagen-like 1Add
BLAST
Domaini350 – 39142Collagen-like 2Add
BLAST
Domaini392 – 43342Collagen-like 3Add
BLAST
Domaini474 – 51643Collagen-like 4Add
BLAST
Domaini568 – 62457Collagen-like 5Add
BLAST
Domaini626 – 67853Collagen-like 6Add
BLAST
Domaini728 – 77851Collagen-like 7Add
BLAST
Domaini779 – 81436Collagen-like 8Add
BLAST
Domaini845 – 90359Collagen-like 9Add
BLAST
Domaini904 – 94744Collagen-like 10Add
BLAST
Domaini948 – 100457Collagen-like 11Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni292 – 35160Triple-helical region 1 (COL1)Add
BLAST
Regioni370 – 42960Triple-helical region 2 (COL2)Add
BLAST
Regioni448 – 688241Triple-helical region 3 (COL3)Add
BLAST
Regioni700 – 818119Triple-helical region 4 (COL4)Add
BLAST
Regioni833 – 1012180Triple-helical region 5 (COL5)Add
BLAST
Regioni1054 – 111158Triple-helical region 6 (COL6)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi952 – 9543Cell attachment siteSequence Analysis

Domaini

The numerous interruptions in the triple helix may make this molecule either elastic or flexible.1 Publication

Sequence similaritiesi

Contains 11 collagen-like domains.Curated
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG275976.
GeneTreeiENSGT00770000120455.
HOVERGENiHBG060240.
InParanoidiQ14993.
OMAiERWFLWQ.
OrthoDBiEOG7353W7.
PhylomeDBiQ14993.
TreeFamiTF351778.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 11 hits.
[Graphical view]
SMARTiSM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q14993-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLTGPWKLW LWMSIFLLPA STSVTVRDKT EESCPILRIE GHQLTYDNIN
60 70 80 90 100
KLEVSGFDLG DSFSLRRAFC ESDKTCFKLG SALLIRDTIK IFPKGLPEEY
110 120 130 140 150
SVAAMFRVRR NAKKERWFLW QVLNQQNIPQ ISIVVDGGKK VVEFMFQATE
160 170 180 190 200
GDVLNYIFRN RELRPLFDRQ WHKLGISIQS QVISLYMDCN LIARRQTDEK
210 220 230 240 250
DTVDFHGRTV IATRASDGKP VDIELHQLKI YCSANLIAQE TCCEISDTKC
260 270 280 290 300
PEQDGFGNIA SSWVTAHASK MSSYLPAKQE LKDQCQCIPN KGEAGLPGAP
310 320 330 340 350
GSPGQKGHKG EPGENGLHGA PGFPGQKGEQ GFEGSKGETG EKGEQGEKGD
360 370 380 390 400
PALAGLNGEN GLKGDLGPHG PPGPKGEKGD TGPPGPPALP GSLGIQGPQG
410 420 430 440 450
PPGKEGQRGR RGKTGPPGKP GPPGPPGPPG IQGIHQTLGG YYNKDNKGND
460 470 480 490 500
EHEAGGLKGD KGETGLPGFP GSVGPKGQKG EPGEPFTKGE KGDRGEPGVI
510 520 530 540 550
GSQGVKGEPG DPGPPGLIGS PGLKGQQGSA GSMGPRGPPG DVGLPGEHGI
560 570 580 590 600
PGKQGIKGEK GDPGGIIGPP GLPGPKGEAG PPGKSLPGEP GLDGNPGAPG
610 620 630 640 650
PRGPKGERGL PGVHGSPGDI GPQGIGIPGR TGAQGPAGEP GIQGPRGLPG
660 670 680 690 700
LPGTPGTPGN DGVPGRDGKP GLPGPPGDPI ALPLLGDIGA LLKNFCGNCQ
710 720 730 740 750
ASVPGLKSNK GEEGGAGEPG KYDSMARKGD IGPRGPPGIP GREGPKGSKG
760 770 780 790 800
ERGYPGIPGE KGDEGLQGIP GIPGAPGPTG PPGLMGRTGH PGPTGAKGEK
810 820 830 840 850
GSDGPPGKPG PPGPPGIPFN ERNGMSSLYK IKGGVNVPSY PGPPGPPGPK
860 870 880 890 900
GDPGPVGEPG AMGLPGLEGF PGVKGDRGPA GPPGIAGMSG KPGAPGPPGV
910 920 930 940 950
PGEPGERGPV GDIGFPGPEG PSGKPGINGK DGIPGAQGIM GKPGDRGPKG
960 970 980 990 1000
ERGDQGIPGD RGSQGERGKP GLTGMKGAIG PMGPPGNKGS MGSPGHQGPP
1010 1020 1030 1040 1050
GSPGIPGIPA DAVSFEEIKK YINQEVLRIF EERMAVFLSQ LKLPAAMLAA
1060 1070 1080 1090 1100
QAYGRPGPPG KDGLPGPPGD PGPQGYRGQK GERGEPGIGL PGSPGLPGTS
1110 1120 1130 1140
ALGLPGSPGA PGPQGPPGPS GRCNPEDCLY PVSHAHQRTG GN
Length:1,142
Mass (Da):115,221
Last modified:July 5, 2005 - v3
Checksum:iF1153CE751387943
GO

Sequence cautioni

The sequence CAC12699.3 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI42319.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI42496.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891I → MY in BAA23309. (PubMed:9344653)Curated
Sequence conflicti106 – 11914FRVRR…ERWFL → ETTVPFWRFFVLET in AAA36358. (PubMed:7916703)CuratedAdd
BLAST
Sequence conflicti279 – 2791Q → L in BAA07368. (PubMed:7775380)Curated
Sequence conflicti354 – 3552AG → GC in AAA58468. (PubMed:1639419)Curated
Sequence conflicti365 – 3651D → V in BAA07368. (PubMed:7775380)Curated
Sequence conflicti365 – 3651D → V in AAA58468. (PubMed:1639419)Curated
Sequence conflicti441 – 4422YY → DD in BAA07368. (PubMed:7775380)Curated
Sequence conflicti441 – 4422YY → DD in AAA58468. (PubMed:1639419)Curated
Sequence conflicti622 – 6243PQG → QRD in AAA58468. (PubMed:1639419)Curated
Sequence conflicti816 – 8238GIPFNERN → VSCSRLKI in AAA36358. (PubMed:7916703)Curated
Sequence conflicti937 – 9371Q → E in BAA07368. (PubMed:7775380)Curated
Sequence conflicti1140 – 11401G → C in BAA23309. (PubMed:9344653)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti352 – 3521A → G.
Corresponds to variant rs2273426 [ dbSNP | Ensembl ].
VAR_024419
Natural varianti361 – 3611G → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_035746
Natural varianti406 – 4061G → E.
Corresponds to variant rs13204209 [ dbSNP | Ensembl ].
VAR_048782
Natural varianti496 – 4961E → G.
Corresponds to variant rs13204209 [ dbSNP | Ensembl ].
VAR_048783
Natural varianti1019 – 10191K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_035747

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38163 mRNA. Translation: BAA07368.1.
AB004629 Genomic DNA. Translation: BAA23309.1.
AL118519 Genomic DNA. Translation: CAB99331.2.
AL133388, AL136445, AL160262 Genomic DNA. Translation: CAI42496.2. Sequence problems.
AL133388
, AL118519, AL136445, AL359539, AL160262 Genomic DNA. Translation: CAI42497.1.
AL136445, AL133388, AL160262 Genomic DNA. Translation: CAC12699.3. Sequence problems.
AL136445
, AL118519, AL133388, AL160262, AL359539 Genomic DNA. Translation: CAI42716.1.
AL160262, AL133388, AL136445 Genomic DNA. Translation: CAI42319.2. Sequence problems.
AL160262
, AL118519, AL133388, AL136445, AL359539 Genomic DNA. Translation: CAI42322.1.
AL359539
, AL118519, AL133388, AL136445, AL160262 Genomic DNA. Translation: CAI16492.1.
BC113362 mRNA. Translation: AAI13363.1.
BC113364 mRNA. Translation: AAI13365.1.
M63597 mRNA. Translation: AAA58468.1.
L12347 mRNA. Translation: AAA36358.1.
U09279 mRNA. Translation: AAA21146.1.
AH000850 Genomic DNA. Translation: AAA21147.1.
CCDSiCCDS4970.1.
PIRiJX0369.
RefSeqiNP_001849.2. NM_001858.5.
UniGeneiHs.444842.

Genome annotation databases

EnsembliENST00000620364; ENSP00000480474; ENSG00000082293.
GeneIDi1310.
KEGGihsa:1310.
UCSCiuc003pfc.1. human.

Polymorphism databases

DMDMi68840003.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38163 mRNA. Translation: BAA07368.1 .
AB004629 Genomic DNA. Translation: BAA23309.1 .
AL118519 Genomic DNA. Translation: CAB99331.2 .
AL133388 , AL136445 , AL160262 Genomic DNA. Translation: CAI42496.2 . Sequence problems.
AL133388
, AL118519 , AL136445 , AL359539 , AL160262 Genomic DNA. Translation: CAI42497.1 .
AL136445 , AL133388 , AL160262 Genomic DNA. Translation: CAC12699.3 . Sequence problems.
AL136445
, AL118519 , AL133388 , AL160262 , AL359539 Genomic DNA. Translation: CAI42716.1 .
AL160262 , AL133388 , AL136445 Genomic DNA. Translation: CAI42319.2 . Sequence problems.
AL160262
, AL118519 , AL133388 , AL136445 , AL359539 Genomic DNA. Translation: CAI42322.1 .
AL359539
, AL118519 , AL133388 , AL136445 , AL160262 Genomic DNA. Translation: CAI16492.1 .
BC113362 mRNA. Translation: AAI13363.1 .
BC113364 mRNA. Translation: AAI13365.1 .
M63597 mRNA. Translation: AAA58468.1 .
L12347 mRNA. Translation: AAA36358.1 .
U09279 mRNA. Translation: AAA21146.1 .
AH000850 Genomic DNA. Translation: AAA21147.1 .
CCDSi CCDS4970.1.
PIRi JX0369.
RefSeqi NP_001849.2. NM_001858.5.
UniGenei Hs.444842.

3D structure databases

ProteinModelPortali Q14993.
SMRi Q14993. Positions 51-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107705. 1 interaction.

PTM databases

PhosphoSitei Q14993.

Polymorphism databases

DMDMi 68840003.

Proteomic databases

PaxDbi Q14993.
PRIDEi Q14993.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000620364 ; ENSP00000480474 ; ENSG00000082293 .
GeneIDi 1310.
KEGGi hsa:1310.
UCSCi uc003pfc.1. human.

Organism-specific databases

CTDi 1310.
GeneCardsi GC06P070633.
HGNCi HGNC:2196. COL19A1.
HPAi HPA042422.
MIMi 120165. gene.
neXtProti NX_Q14993.
PharmGKBi PA26712.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG275976.
GeneTreei ENSGT00770000120455.
HOVERGENi HBG060240.
InParanoidi Q14993.
OMAi ERWFLWQ.
OrthoDBi EOG7353W7.
PhylomeDBi Q14993.
TreeFami TF351778.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi COL19A1. human.
GeneWikii Collagen,_type_XIX,_alpha_1.
GenomeRNAii 1310.
NextBioi 5357.
PROi Q14993.
SOURCEi Search...

Gene expression databases

Bgeei Q14993.
ExpressionAtlasi Q14993. baseline.
Genevestigatori Q14993.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01391. Collagen. 11 hits.
[Graphical view ]
SMARTi SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains a long unusual 3' untranslated region and displays many unique splicing variants."
    Inoguchi K., Yoshioka H., Khaleduzzaman M., Ninomiya Y.
    J. Biochem. 117:137-146(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure of the human type XIX collagen (COL19A1) gene, which suggests it has arisen from an ancestor gene of the FACIT family."
    Khaleduzzaman M., Sumiyoshi H., Ueki Y., Inoguchi K., Ninomiya Y., Yoshioka H.
    Genomics 45:304-312(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Synteny between the loci for a novel FACIT-like collagen locus (D6S228E) and alpha 1 (IX) collagen (COL9A1) on 6q12-q14 in humans."
    Yoshioka H., Zhang H., Ramirez F., Mattei M.-G., Moradi-Ameli M., van der Rest M., Gordon M.K.
    Genomics 13:884-886(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-624.
    Tissue: Rhabdomyosarcoma.
  6. "Human cDNA clones transcribed from an unusually high-molecular-weight RNA encode a new collagen chain."
    Myers J.C., Sun M.J., D'Ippolito J.A., Jabs E.W., Neilson E.G., Dion A.S.
    Gene 123:211-217(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-1020.
  7. "The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to alpha 1(XVI)."
    Myers J.C., Yang H., D'Ippolito J.A., Presente A., Miller M.K., Dion A.S.
    J. Biol. Chem. 269:18549-18557(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 738-1142.
    Tissue: Skin.
  8. "Type XIX collagen purified from human umbilical cord is characterized by multiple sharp kinks delineating collagenous subdomains and by intermolecular aggregates via globular, disulfide-linked, and heparin-binding amino termini."
    Myers J.C., Li D., Amenta P.S., Clark C.C., Nagaswami C., Weisel J.W.
    J. Biol. Chem. 278:32047-32057(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DOMAIN.
  9. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-361 AND ASN-1019.

Entry informationi

Entry nameiCOJA1_HUMAN
AccessioniPrimary (citable) accession number: Q14993
Secondary accession number(s): Q00559
, Q05850, Q12885, Q13676, Q14DH1, Q5JUF0, Q5T424, Q9H572, Q9NPZ2, Q9NQP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: July 5, 2005
Last modified: November 26, 2014
This is version 137 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3