Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q05707

- COEA1_HUMAN

UniProt

Q05707 - COEA1_HUMAN

Protein

Collagen alpha-1(XIV) chain

Gene

COL14A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (06 Feb 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors By similarity.By similarity

    GO - Molecular functioni

    1. collagen binding Source: UniProtKB
    2. extracellular matrix structural constituent Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding, bridging Source: UniProtKB

    GO - Biological processi

    1. collagen catabolic process Source: Reactome
    2. collagen fibril organization Source: UniProtKB
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: UniProtKB
    5. homeostasis of number of cells within a tissue Source: Ensembl
    6. regulation of cell growth involved in cardiac muscle cell development Source: Ensembl
    7. single organismal cell-cell adhesion Source: UniProtKB
    8. ventricular cardiac muscle tissue development Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(XIV) chain
    Alternative name(s):
    Undulin
    Gene namesi
    Name:COL14A1Imported
    Synonyms:UND
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:2191. COL14A1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix By similarity

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB
    2. collagen type XIV trimer Source: UniProtKB
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. extracellular space Source: BHF-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. interstitial matrix Source: Ensembl
    8. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti79501. Punctate palmoplantar keratoderma type 1.
    PharmGKBiPA26707.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 17961768Collagen alpha-1(XIV) chainPRO_0000005785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)1 Publication
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)1 Publication
    Glycosylationi1384 – 13841N-linked (GlcNAc...)1 Publication
    Glycosylationi1388 – 13881N-linked (GlcNAc...)1 Publication
    Modified residuei1467 – 146714-hydroxyproline1 Publication
    Modified residuei1470 – 147014-hydroxyproline; partial1 Publication
    Modified residuei1476 – 147615-hydroxylysine; alternate1 Publication
    Glycosylationi1476 – 14761O-linked (Gal...); alternate1 Publication
    Modified residuei1482 – 148214-hydroxyproline1 Publication
    Modified residuei1485 – 148515-hydroxylysine; partial1 Publication
    Glycosylationi1485 – 14851O-linked (Gal...); partial1 Publication
    Modified residuei1497 – 149714-hydroxyproline1 Publication
    Modified residuei1503 – 150314-hydroxyproline1 Publication
    Modified residuei1517 – 151714-hydroxyproline1 Publication
    Modified residuei1520 – 152014-hydroxyproline1 Publication
    Modified residuei1523 – 152315-hydroxylysine; partial1 Publication
    Glycosylationi1523 – 15231O-linked (Gal...); partial1 Publication
    Modified residuei1526 – 152615-hydroxylysine; partial1 Publication
    Glycosylationi1526 – 15261O-linked (Gal...); partial1 Publication
    Modified residuei1532 – 153214-hydroxyproline1 Publication
    Modified residuei1538 – 153814-hydroxyproline1 Publication
    Modified residuei1544 – 154414-hydroxyproline1 Publication
    Modified residuei1550 – 155014-hydroxyproline1 Publication
    Modified residuei1556 – 155614-hydroxyproline1 Publication
    Modified residuei1565 – 156514-hydroxyproline1 Publication
    Modified residuei1568 – 156814-hydroxyproline1 Publication
    Modified residuei1574 – 157414-hydroxyproline1 Publication
    Modified residuei1577 – 157714-hydroxyproline1 Publication
    Modified residuei1580 – 158014-hydroxyproline1 Publication
    Modified residuei1595 – 159514-hydroxyproline1 Publication
    Modified residuei1598 – 159814-hydroxyproline1 Publication
    Modified residuei1601 – 160115-hydroxylysine; alternate1 Publication
    Glycosylationi1601 – 16011O-linked (Gal...); alternate1 Publication
    Modified residuei1643 – 164314-hydroxyproline; partial1 Publication
    Modified residuei1656 – 165614-hydroxyproline1 Publication
    Modified residuei1659 – 165914-hydroxyproline1 Publication
    Modified residuei1662 – 166214-hydroxyproline1 Publication
    Modified residuei1665 – 166514-hydroxyproline1 Publication
    Modified residuei1668 – 166814-hydroxyproline1 Publication
    Modified residuei1674 – 167414-hydroxyproline1 Publication
    Modified residuei1677 – 167714-hydroxyproline1 Publication
    Modified residuei1680 – 168014-hydroxyproline1 Publication
    Modified residuei1686 – 168614-hydroxyproline1 Publication
    Modified residuei1689 – 168914-hydroxyproline1 Publication
    Modified residuei1698 – 169815-hydroxylysine; alternate1 Publication
    Glycosylationi1698 – 16981O-linked (Gal...); alternate1 Publication
    Modified residuei1701 – 170115-hydroxylysine; alternate1 Publication
    Glycosylationi1701 – 17011O-linked (Gal...); partial1 Publication
    Modified residuei1704 – 170414-hydroxyproline1 Publication
    Modified residuei1715 – 171514-hydroxyproline1 Publication
    Modified residuei1726 – 172614-hydroxyproline; partial1 Publication
    Modified residuei1729 – 172914-hydroxyproline1 Publication
    Modified residuei1732 – 173214-hydroxyproline1 Publication
    Modified residuei1735 – 173514-hydroxyproline1 Publication
    Modified residuei1741 – 174114-hydroxyproline1 Publication
    Modified residuei1747 – 174714-hydroxyproline1 Publication
    Modified residuei1756 – 175614-hydroxyproline1 Publication

    Post-translational modificationi

    Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.By similarity
    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.By similarity
    May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    MaxQBiQ05707.
    PaxDbiQ05707.
    PRIDEiQ05707.

    PTM databases

    PhosphoSiteiQ05707.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05707.
    BgeeiQ05707.
    CleanExiHS_COL14A1.
    GenevestigatoriQ05707.

    Organism-specific databases

    HPAiHPA023781.

    Interactioni

    Subunit structurei

    Homotrimer.By similarity

    Protein-protein interaction databases

    BioGridi113219. 4 interactions.
    IntActiQ05707. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05707.
    SMRiQ05707. Positions 30-113, 158-1000, 1032-1194, 1225-1436.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 12291Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini158 – 330173VWFA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 44490Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini445 – 53692Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini537 – 62690Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini627 – 71589Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini737 – 82993Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini831 – 92191Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini922 – 101089Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1032 – 1205174VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1229 – 1424196Laminin G-likeAdd
    BLAST
    Domaini1462 – 151049Collagen-like 1Add
    BLAST
    Domaini1514 – 157057Collagen-like 2Add
    BLAST
    Domaini1571 – 160939Collagen-like 3Add
    BLAST
    Domaini1653 – 170553Collagen-like 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1217 – 1458242Nonhelical region (NC4)Add
    BLAST
    Regioni1459 – 1610152Triple-helical region 1 (COL2)Add
    BLAST
    Regioni1654 – 1779126Triple-helical region 2 (COL1)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1607 – 16093Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 4 collagen-like domains.Curated
    Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 laminin G-like domain.Curated
    Contains 2 VWFA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG307460.
    HOVERGENiHBG051060.
    InParanoidiQ05707.
    KOiK08133.
    OMAiWYNRLRI.
    OrthoDBiEOG71P290.
    PhylomeDBiQ05707.
    TreeFamiTF329914.

    Family and domain databases

    Gene3Di2.60.40.10. 8 hits.
    3.40.50.410. 2 hits.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR001791. Laminin_G.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01391. Collagen. 4 hits.
    PF00041. fn3. 8 hits.
    PF00092. VWA. 2 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 8 hits.
    SM00210. TSPN. 1 hit.
    SM00327. VWA. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 6 hits.
    SSF49899. SSF49899. 1 hit.
    SSF53300. SSF53300. 2 hits.
    PROSITEiPS50853. FN3. 8 hits.
    PS50234. VWFA. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q05707-1) [UniParc]FASTAAdd to Basket

    Also known as: Undulin 11 Publication

    , Un11 Publication

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKIFQRKMRY WLLPPFLAIV YFCTIVQGQV APPTRLRYNV ISHDSIQISW     50
    KAPRGKFGGY KLLVTPTSGG KTNQLNLQNT ATKAIIQGLM PDQNYTVQII 100
    AYNKDKESKP AQGQFRIKDL EKRKDPKPRV KVVDRGNGSR PSSPEEVKFV 150
    CQTPAIADIV ILVDGSWSIG RFNFRLVRHF LENLVTAFDV GSEKTRIGLA 200
    QYSGDPRIEW HLNAFSTKDE VIEAVRNLPY KGGNTLTGLA LNYIFENSFK 250
    PEAGSRTGVS KIGILITDGK SQDDIIPPSR NLRESGVELF AIGVKNADVN 300
    ELQEIASEPD STHVYNVAEF DLMHTVVESL TRTLCSRVEE QDREIKASAH 350
    AITGPPTELI TSEVTARSFM VNWTHAPGNV EKYRVVYYPT RGGKPDEVVV 400
    DGTVSSTVLK NLMSLTEYQI AVFAIYAHTA SEGLRGTETT LALPMASDLL 450
    LYDVTENSMR VKWDAVPGAS GYLILYAPLT EGLAGDEKEM KIGETHTDIE 500
    LSGLLPNTEY TVTVYAMFGE EASDPVTGQE TTLALSPPRN LRISNVGSNS 550
    ARLTWDPTSR QINGYRIVYN NADGTEINEV EVDPITTFPL KGLTPLTEYT 600
    IAIFSIYDEG QSEPLTGVFT TEEVPAQQYL EIDEVTTDSF RVTWHPLSAD 650
    EGLHKLMWIP VYGGKTEEVV LKEEQDSHVI EGLEPGTEYE VSLLAVLDDG 700
    SESEVVTAVG TTLDSFWTEP ATTIVPTTSV TSVFQTGIRN LVVGDETTSS 750
    LRVKWDISDS DVQQFRVTYM TAQGDPEEEV IGTVMVPGSQ NNLLLKPLLP 800
    DTEYKVTVTP IYTDGEGVSV SAPGKTLPSS GPQNLRVSEE WYNRLRITWD 850
    PPSSPVKGYR IVYKPVSVPG PTLETFVGAD INTILITNLL SGMDYNVKIF 900
    ASQASGFSDA LTGMVKTLFL GVTNLQAKHV EMTSLCAHWQ VHRHATAYRV 950
    VIESLQDRQK QESTVGGGTT RHCFYGLQPD SEYKISVYTK LQEIEGPSVS 1000
    IMEKTQSLPT RPPTFPPTIP PAKEVCKAAK ADLVFMVDGS WSIGDENFNK 1050
    IISFLYSTVG ALNKIGTDGT QVAMVQFTDD PRTEFKLNAY KTKETLLDAI 1100
    KHISYKGGNT KTGKAIKYVR DTLFTAESGT RRGIPKVIVV ITDGRSQDDV 1150
    NKISREMQLD GYSIFAIGVA DADYSELVSI GSKPSARHVF FVDDFDAFKK 1200
    IEDELITFVC ETASATCPVV HKDGIDLAGF KMMEMFGLVE KDFSSVEGVS 1250
    MEPGTFNVFP CYQLHKDALV SQPTRYLHPE GLPSDYTISF LFRILPDTPQ 1300
    EPFALWEILN KNSDPLVGVI LDNGGKTLTY FNYDQSGDFQ TVTFEGPEIR 1350
    KIFYGSFHKL HIVVSETLVK VVIDCKQVGE KAMNASANIT SDGVEVLGKM 1400
    VRSRGPGGNS APFQLQMFDI VCSTSWANTD KCCELPGLRD DESCPDLPHS 1450
    CSCSETNEVA LGPAGPPGGP GLRGPKGQQG EPGPKGPDGP RGEIGLPGPQ 1500
    GPPGPQGPSG LSIQGMPGMP GEKGEKGDTG LPGPQGIPGG VGSPGRDGSP 1550
    GQRGLPGKDG SSGPPGPPGP IGIPGTPGVP GITGSMGPQG ALGPPGVPGA 1600
    KGERGERGDL QSQAMVRSVA RQVCEQLIQS HMARYTAILN QIPSHSSSIR 1650
    TVQGPPGEPG RPGSPGAPGE QGPPGTPGFP GNAGVPGTPG ERGLTGIKGE 1700
    KGNPGVGTQG PRGPPGPAGP SGESRPGSPG PPGSPGPRGP PGHLGVPGPQ 1750
    GPSGQPGYCD PSSCSAYGVR APHPDQPEFT PVQDELEAME LWGPGV 1796
    Length:1,796
    Mass (Da):193,515
    Last modified:February 6, 2007 - v3
    Checksum:i30A72F6E2CC07F70
    GO
    Isoform 21 Publication (identifier: Q05707-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1771-1796: APHPDQPEFTPVQDELEAMELWGPGV → DLIPYNDYQH

    Show »
    Length:1,780
    Mass (Da):191,903
    Checksum:iD0818CA6359B66D4
    GO
    Isoform 31 Publication (identifier: Q05707-3) [UniParc]FASTAAdd to Basket

    Also known as: Undulin 21 Publication

    , Un21 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         197-291: Missing.

    Show »
    Length:1,701
    Mass (Da):183,154
    Checksum:i351A5F24379FEDF0
    GO

    Sequence cautioni

    The sequence AAA36795.1 differs from that shown. Reason:
    The sequence AAH14640.1 differs from that shown. Reason: Frameshift at position 1047.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti616 – 6161T → I in AAA36794. (PubMed:15489334)Curated
    Sequence conflicti1025 – 10251V → G in AAA36794. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti563 – 5631N → H.
    Corresponds to variant rs4870723 [ dbSNP | Ensembl ].
    VAR_048772
    Natural varianti636 – 6361T → A.
    Corresponds to variant rs56815167 [ dbSNP | Ensembl ].
    VAR_061113
    Natural varianti855 – 8551P → L.
    Corresponds to variant rs2305606 [ dbSNP | Ensembl ].
    VAR_048773
    Natural varianti922 – 9221V → I.
    Corresponds to variant rs11774228 [ dbSNP | Ensembl ].
    VAR_048774
    Natural varianti1342 – 13421V → L.1 Publication
    Corresponds to variant rs17833992 [ dbSNP | Ensembl ].
    VAR_048775

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei197 – 29195Missing in isoform 3. 1 PublicationVSP_051653Add
    BLAST
    Alternative sequencei1771 – 179626APHPD…WGPGV → DLIPYNDYQH in isoform 2. 1 PublicationVSP_051654Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC020603 Genomic DNA. No translation available.
    AC090735 Genomic DNA. No translation available.
    AC107877 Genomic DNA. No translation available.
    BC014640 mRNA. Translation: AAH14640.1. Frameshift.
    BC083495 mRNA. Translation: AAH83495.1.
    BC140893 mRNA. Translation: AAI40894.1.
    Y11709 mRNA. Translation: CAA72401.1.
    Y11710 mRNA. Translation: CAA72402.1.
    Y11711 mRNA. Translation: CAA72403.1.
    M64108 mRNA. Translation: AAA36794.1.
    M64109 mRNA. Translation: AAA36795.1. Sequence problems.
    CCDSiCCDS34938.1. [Q05707-1]
    PIRiA40970.
    B40970.
    S37749.
    S46657.
    RefSeqiNP_066933.1. NM_021110.2. [Q05707-1]
    XP_005251116.1. XM_005251059.1. [Q05707-2]
    XP_006716714.1. XM_006716651.1. [Q05707-1]
    UniGeneiHs.409662.

    Genome annotation databases

    EnsembliENST00000247781; ENSP00000247781; ENSG00000187955. [Q05707-3]
    ENST00000297848; ENSP00000297848; ENSG00000187955. [Q05707-1]
    ENST00000309791; ENSP00000311809; ENSG00000187955. [Q05707-2]
    GeneIDi7373.
    KEGGihsa:7373.
    UCSCiuc003yox.4. human. [Q05707-1]

    Polymorphism databases

    DMDMi125987815.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC020603 Genomic DNA. No translation available.
    AC090735 Genomic DNA. No translation available.
    AC107877 Genomic DNA. No translation available.
    BC014640 mRNA. Translation: AAH14640.1 . Frameshift.
    BC083495 mRNA. Translation: AAH83495.1 .
    BC140893 mRNA. Translation: AAI40894.1 .
    Y11709 mRNA. Translation: CAA72401.1 .
    Y11710 mRNA. Translation: CAA72402.1 .
    Y11711 mRNA. Translation: CAA72403.1 .
    M64108 mRNA. Translation: AAA36794.1 .
    M64109 mRNA. Translation: AAA36795.1 . Sequence problems.
    CCDSi CCDS34938.1. [Q05707-1 ]
    PIRi A40970.
    B40970.
    S37749.
    S46657.
    RefSeqi NP_066933.1. NM_021110.2. [Q05707-1 ]
    XP_005251116.1. XM_005251059.1. [Q05707-2 ]
    XP_006716714.1. XM_006716651.1. [Q05707-1 ]
    UniGenei Hs.409662.

    3D structure databases

    ProteinModelPortali Q05707.
    SMRi Q05707. Positions 30-113, 158-1000, 1032-1194, 1225-1436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113219. 4 interactions.
    IntActi Q05707. 2 interactions.

    PTM databases

    PhosphoSitei Q05707.

    Polymorphism databases

    DMDMi 125987815.

    Proteomic databases

    MaxQBi Q05707.
    PaxDbi Q05707.
    PRIDEi Q05707.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000247781 ; ENSP00000247781 ; ENSG00000187955 . [Q05707-3 ]
    ENST00000297848 ; ENSP00000297848 ; ENSG00000187955 . [Q05707-1 ]
    ENST00000309791 ; ENSP00000311809 ; ENSG00000187955 . [Q05707-2 ]
    GeneIDi 7373.
    KEGGi hsa:7373.
    UCSCi uc003yox.4. human. [Q05707-1 ]

    Organism-specific databases

    CTDi 7373.
    GeneCardsi GC08P121093.
    H-InvDB HIX0007753.
    HGNCi HGNC:2191. COL14A1.
    HPAi HPA023781.
    MIMi 120324. gene.
    neXtProti NX_Q05707.
    Orphaneti 79501. Punctate palmoplantar keratoderma type 1.
    PharmGKBi PA26707.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307460.
    HOVERGENi HBG051060.
    InParanoidi Q05707.
    KOi K08133.
    OMAi WYNRLRI.
    OrthoDBi EOG71P290.
    PhylomeDBi Q05707.
    TreeFami TF329914.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi COL14A1. human.
    GeneWikii Collagen,_type_XIV,_alpha_1.
    GenomeRNAii 7373.
    NextBioi 28870.
    PROi Q05707.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05707.
    Bgeei Q05707.
    CleanExi HS_COL14A1.
    Genevestigatori Q05707.

    Family and domain databases

    Gene3Di 2.60.40.10. 8 hits.
    3.40.50.410. 2 hits.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR001791. Laminin_G.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01391. Collagen. 4 hits.
    PF00041. fn3. 8 hits.
    PF00092. VWA. 2 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 8 hits.
    SM00210. TSPN. 1 hit.
    SM00327. VWA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 6 hits.
    SSF49899. SSF49899. 1 hit.
    SSF53300. SSF53300. 2 hits.
    PROSITEi PS50853. FN3. 8 hits.
    PS50234. VWFA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1), VARIANT LEU-1342.
      Tissue: Brain, MuscleImported and PNSImported.
    3. "Complete primary structure of human collagen type XIV (undulin)."
      Bauer M., Dieterich W., Ehnis T., Schuppan D.
      Biochim. Biophys. Acta 1354:183-188(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165, NUCLEOTIDE SEQUENCE [MRNA] OF 1026-1796 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1760-1796 (ISOFORM 2).
    4. "Undulin is a novel member of the fibronectin-tenascin family of extracellular matrix glycoproteins."
      Just M., Herbst H., Hummel M., Duerkop H., Tripier D., Stein H., Schuppan D.
      J. Biol. Chem. 266:17326-17332(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-582 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 188-1030 (ISOFORM 1).
    5. "Structure and stability of the triple-helical domains of human collagen XIV."
      Brown J.C., Golbik R., Mann K., Timpl R.
      Matrix Biol. 14:287-295(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1459-1635 AND 1640-1767, HYDROXYLATION AT PRO-1467; PRO-1470; LYS-1476; PRO-1482; LYS-1485; PRO-1497; PRO-1503; PRO-1517; PRO-1520; LYS-1523; LYS-1526; PRO-1532; PRO-1538; PRO-1544; PRO-1550; PRO-1556; PRO-1565; PRO-1568; PRO-1574; PRO-1577; PRO-1580; PRO-1595; PRO-1598; LYS-1601; PRO-1643; PRO-1656; PRO-1659; PRO-1662; PRO-1665; PRO-1668; PRO-1674; PRO-1677; PRO-1680; PRO-1686; PRO-1689; LYS-1698; LYS-1701; PRO-1704; PRO-1715; PRO-1726; PRO-1729; PRO-1732; PRO-1735; PRO-1741; PRO-1747 AND PRO-1756, GLYCOSYLATION AT LYS-1476; LYS-1485; LYS-1523; LYS-1526; LYS-1601; LYS-1698 AND LYS-1701.
      Tissue: Placenta.
    6. "Undulin, an extracellular matrix glycoprotein associated with collagen fibrils."
      Schuppan D., Cantaluppi M., Becker J., Veit A., Bunte T., Troyer D., Schuppan F., Schmid M., Ackermann R., Hahn E.
      J. Biol. Chem. 265:8823-8832(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "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-94; ASN-372; ASN-1384 AND ASN-1388.
      Tissue: Liver.

    Entry informationi

    Entry nameiCOEA1_HUMAN
    AccessioniPrimary (citable) accession number: Q05707
    Secondary accession number(s): B2RU07
    , O00260, O00261, O00262, Q05708, Q5XJ18, Q96C67, Q9UDF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 118 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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