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Q14993

- COJA1_HUMAN

UniProt

Q14993 - COJA1_HUMAN

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
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (05 Jul 2005)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ14993.
    BgeeiQ14993.
    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.
    HOVERGENiHBG060240.
    InParanoidiQ14993.
    OMAiERWFLWQ.
    OrthoDBiEOG7353W7.
    PhylomeDBiQ14993.
    TreeFamiTF351778.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

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    MRLTGPWKLW LWMSIFLLPA STSVTVRDKT EESCPILRIE GHQLTYDNIN     50
    KLEVSGFDLG DSFSLRRAFC ESDKTCFKLG SALLIRDTIK IFPKGLPEEY 100
    SVAAMFRVRR NAKKERWFLW QVLNQQNIPQ ISIVVDGGKK VVEFMFQATE 150
    GDVLNYIFRN RELRPLFDRQ WHKLGISIQS QVISLYMDCN LIARRQTDEK 200
    DTVDFHGRTV IATRASDGKP VDIELHQLKI YCSANLIAQE TCCEISDTKC 250
    PEQDGFGNIA SSWVTAHASK MSSYLPAKQE LKDQCQCIPN KGEAGLPGAP 300
    GSPGQKGHKG EPGENGLHGA PGFPGQKGEQ GFEGSKGETG EKGEQGEKGD 350
    PALAGLNGEN GLKGDLGPHG PPGPKGEKGD TGPPGPPALP GSLGIQGPQG 400
    PPGKEGQRGR RGKTGPPGKP GPPGPPGPPG IQGIHQTLGG YYNKDNKGND 450
    EHEAGGLKGD KGETGLPGFP GSVGPKGQKG EPGEPFTKGE KGDRGEPGVI 500
    GSQGVKGEPG DPGPPGLIGS PGLKGQQGSA GSMGPRGPPG DVGLPGEHGI 550
    PGKQGIKGEK GDPGGIIGPP GLPGPKGEAG PPGKSLPGEP GLDGNPGAPG 600
    PRGPKGERGL PGVHGSPGDI GPQGIGIPGR TGAQGPAGEP GIQGPRGLPG 650
    LPGTPGTPGN DGVPGRDGKP GLPGPPGDPI ALPLLGDIGA LLKNFCGNCQ 700
    ASVPGLKSNK GEEGGAGEPG KYDSMARKGD IGPRGPPGIP GREGPKGSKG 750
    ERGYPGIPGE KGDEGLQGIP GIPGAPGPTG PPGLMGRTGH PGPTGAKGEK 800
    GSDGPPGKPG PPGPPGIPFN ERNGMSSLYK IKGGVNVPSY PGPPGPPGPK 850
    GDPGPVGEPG AMGLPGLEGF PGVKGDRGPA GPPGIAGMSG KPGAPGPPGV 900
    PGEPGERGPV GDIGFPGPEG PSGKPGINGK DGIPGAQGIM GKPGDRGPKG 950
    ERGDQGIPGD RGSQGERGKP GLTGMKGAIG PMGPPGNKGS MGSPGHQGPP 1000
    GSPGIPGIPA DAVSFEEIKK YINQEVLRIF EERMAVFLSQ LKLPAAMLAA 1050
    QAYGRPGPPG KDGLPGPPGD PGPQGYRGQK GERGEPGIGL PGSPGLPGTS 1100
    ALGLPGSPGA PGPQGPPGPS GRCNPEDCLY PVSHAHQRTG GN 1142
    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.
    The sequence CAI42319.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI42496.2 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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

    EnsembliENST00000322773; ENSP00000316030; ENSG00000082293.
    GeneIDi1310.
    KEGGihsa:1310.
    UCSCiuc003pfc.1. human.

    Polymorphism databases

    DMDMi68840003.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 ENST00000322773 ; ENSP00000316030 ; 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.
    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

    ArrayExpressi Q14993.
    Bgeei Q14993.
    Genevestigatori Q14993.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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: October 1, 2014
    This is version 135 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