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Q05707

- COEA1_HUMAN

UniProt

Q05707 - COEA1_HUMAN

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Protein

Collagen alpha-1(XIV) chain

Gene
COL14A1, UND
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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
Complete GO annotation...

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:COL14A1
Synonyms:UND
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:2191. COL14A1.

Subcellular locationi

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
Complete GO annotation...

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 – 2828 Reviewed predictionAdd
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...) Reviewed prediction
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.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.By similarity
May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding By similarity.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.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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12291Fibronectin type-III 1Add
BLAST
Domaini158 – 330173VWFA 1Add
BLAST
Domaini355 – 44490Fibronectin type-III 2Add
BLAST
Domaini445 – 53692Fibronectin type-III 3Add
BLAST
Domaini537 – 62690Fibronectin type-III 4Add
BLAST
Domaini627 – 71589Fibronectin type-III 5Add
BLAST
Domaini737 – 82993Fibronectin type-III 6Add
BLAST
Domaini831 – 92191Fibronectin type-III 7Add
BLAST
Domaini922 – 101089Fibronectin type-III 8Add
BLAST
Domaini1032 – 1205174VWFA 2Add
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 site Reviewed prediction

Sequence similaritiesi

Contains 2 VWFA domains.

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 1, Un1

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 2, Un2

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161T → I in AAA36794. 1 Publication
Sequence conflicti1025 – 10251V → G in AAA36794. 1 Publication

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

« Hide 'large scale' publications
  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, Muscle and PNS.
  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: September 3, 2014
This is version 117 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

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