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Q05707 (COEA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XIV) chain
Alternative name(s):
Undulin
Gene names
Name:COL14A1
Synonyms:UND
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1796 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

Homotrimer By similarity. UniProtKB P32018

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Post-translational modification

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates By similarity. UniProtKB P32018

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains By similarity. UniProtKB P32018

May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding By similarity. UniProtKB P32018

Sequence similarities

Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.

Contains 4 collagen-like domains.

Contains 8 fibronectin type-III domains.

Contains 1 laminin G-like domain.

Contains 2 VWFA domains.

Sequence caution

The sequence AAA36795.1 differs from that shown. Reason:

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCollagen
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Non-traceable author statement Ref.6. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Non-traceable author statement Ref.3. Source: UniProtKB

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

regulation of cell growth involved in cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Non-traceable author statement Ref.3. Source: UniProtKB

ventricular cardiac muscle tissue development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcollagen trimer

Non-traceable author statement Ref.3. Source: UniProtKB

collagen type XIV trimer

Non-traceable author statement Ref.3. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

interstitial matrix

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Non-traceable author statement Ref.6. Source: UniProtKB

   Molecular_functioncollagen binding

Non-traceable author statement Ref.6. Source: UniProtKB

extracellular matrix structural constituent

Non-traceable author statement Ref.6Ref.3. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding, bridging

Non-traceable author statement Ref.3. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.3 (identifier: Q05707-1)

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.
Isoform 2 Ref.3 (identifier: Q05707-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1771-1796: APHPDQPEFTPVQDELEAMELWGPGV → DLIPYNDYQH
Isoform 3 Ref.4 (identifier: Q05707-3)

Also known as: Undulin 2; Un2;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 17961768Collagen alpha-1(XIV) chain
PRO_0000005785

Regions

Domain32 – 12291Fibronectin type-III 1
Domain158 – 330173VWFA 1
Domain355 – 44490Fibronectin type-III 2
Domain445 – 53692Fibronectin type-III 3
Domain537 – 62690Fibronectin type-III 4
Domain627 – 71589Fibronectin type-III 5
Domain737 – 82993Fibronectin type-III 6
Domain831 – 92191Fibronectin type-III 7
Domain922 – 101089Fibronectin type-III 8
Domain1032 – 1205174VWFA 2
Domain1229 – 1424196Laminin G-like
Domain1462 – 151049Collagen-like 1
Domain1514 – 157057Collagen-like 2
Domain1571 – 160939Collagen-like 3
Domain1653 – 170553Collagen-like 4
Region1217 – 1458242Nonhelical region (NC4)
Region1459 – 1610152Triple-helical region 1 (COL2)
Region1654 – 1779126Triple-helical region 2 (COL1)
Motif1607 – 16093Cell attachment site Potential

Amino acid modifications

Modified residue146714-hydroxyproline Ref.5
Modified residue147014-hydroxyproline; partial Ref.5
Modified residue147615-hydroxylysine; alternate Ref.5
Modified residue148214-hydroxyproline Ref.5
Modified residue148515-hydroxylysine; partial Ref.5
Modified residue149714-hydroxyproline Ref.5
Modified residue150314-hydroxyproline Ref.5
Modified residue151714-hydroxyproline Ref.5
Modified residue152014-hydroxyproline Ref.5
Modified residue152315-hydroxylysine; partial Ref.5
Modified residue152615-hydroxylysine; partial Ref.5
Modified residue153214-hydroxyproline Ref.5
Modified residue153814-hydroxyproline Ref.5
Modified residue154414-hydroxyproline Ref.5
Modified residue155014-hydroxyproline Ref.5
Modified residue155614-hydroxyproline Ref.5
Modified residue156514-hydroxyproline Ref.5
Modified residue156814-hydroxyproline Ref.5
Modified residue157414-hydroxyproline Ref.5
Modified residue157714-hydroxyproline Ref.5
Modified residue158014-hydroxyproline Ref.5
Modified residue159514-hydroxyproline Ref.5
Modified residue159814-hydroxyproline Ref.5
Modified residue160115-hydroxylysine; alternate Ref.5
Modified residue164314-hydroxyproline; partial Ref.5
Modified residue165614-hydroxyproline Ref.5
Modified residue165914-hydroxyproline Ref.5
Modified residue166214-hydroxyproline Ref.5
Modified residue166514-hydroxyproline Ref.5
Modified residue166814-hydroxyproline Ref.5
Modified residue167414-hydroxyproline Ref.5
Modified residue167714-hydroxyproline Ref.5
Modified residue168014-hydroxyproline Ref.5
Modified residue168614-hydroxyproline Ref.5
Modified residue168914-hydroxyproline Ref.5
Modified residue169815-hydroxylysine; alternate Ref.5
Modified residue170115-hydroxylysine; alternate Ref.5
Modified residue170414-hydroxyproline Ref.5
Modified residue171514-hydroxyproline Ref.5
Modified residue172614-hydroxyproline; partial Ref.5
Modified residue172914-hydroxyproline Ref.5
Modified residue173214-hydroxyproline Ref.5
Modified residue173514-hydroxyproline Ref.5
Modified residue174114-hydroxyproline Ref.5
Modified residue174714-hydroxyproline Ref.5
Modified residue175614-hydroxyproline Ref.5
Glycosylation941N-linked (GlcNAc...) Ref.7
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Ref.7
Glycosylation13841N-linked (GlcNAc...) Ref.7
Glycosylation13881N-linked (GlcNAc...) Ref.7
Glycosylation14761O-linked (Gal...); alternate Ref.5
Glycosylation14851O-linked (Gal...); partial Ref.5
Glycosylation15231O-linked (Gal...); partial Ref.5
Glycosylation15261O-linked (Gal...); partial Ref.5
Glycosylation16011O-linked (Gal...); alternate Ref.5
Glycosylation16981O-linked (Gal...); alternate Ref.5
Glycosylation17011O-linked (Gal...); partial Ref.5

Natural variations

Alternative sequence197 – 29195Missing in isoform 3. Ref.4
VSP_051653
Alternative sequence1771 – 179626APHPD…WGPGV → DLIPYNDYQH in isoform 2. Ref.3
VSP_051654
Natural variant5631N → H.
Corresponds to variant rs4870723 [ dbSNP | Ensembl ].
VAR_048772
Natural variant6361T → A.
Corresponds to variant rs56815167 [ dbSNP | Ensembl ].
VAR_061113
Natural variant8551P → L.
Corresponds to variant rs2305606 [ dbSNP | Ensembl ].
VAR_048773
Natural variant9221V → I.
Corresponds to variant rs11774228 [ dbSNP | Ensembl ].
VAR_048774
Natural variant13421V → L. Ref.2
Corresponds to variant rs17833992 [ dbSNP | Ensembl ].
VAR_048775

Experimental info

Sequence conflict6161T → I in AAA36794. Ref.2
Sequence conflict10251V → G in AAA36794. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Undulin 1) (Un1) [UniParc].

Last modified February 6, 2007. Version 3.
Checksum: 30A72F6E2CC07F70

FASTA1,796193,515
        10         20         30         40         50         60 
MKIFQRKMRY WLLPPFLAIV YFCTIVQGQV APPTRLRYNV ISHDSIQISW KAPRGKFGGY 

        70         80         90        100        110        120 
KLLVTPTSGG KTNQLNLQNT ATKAIIQGLM PDQNYTVQII AYNKDKESKP AQGQFRIKDL 

       130        140        150        160        170        180 
EKRKDPKPRV KVVDRGNGSR PSSPEEVKFV CQTPAIADIV ILVDGSWSIG RFNFRLVRHF 

       190        200        210        220        230        240 
LENLVTAFDV GSEKTRIGLA QYSGDPRIEW HLNAFSTKDE VIEAVRNLPY KGGNTLTGLA 

       250        260        270        280        290        300 
LNYIFENSFK PEAGSRTGVS KIGILITDGK SQDDIIPPSR NLRESGVELF AIGVKNADVN 

       310        320        330        340        350        360 
ELQEIASEPD STHVYNVAEF DLMHTVVESL TRTLCSRVEE QDREIKASAH AITGPPTELI 

       370        380        390        400        410        420 
TSEVTARSFM VNWTHAPGNV EKYRVVYYPT RGGKPDEVVV DGTVSSTVLK NLMSLTEYQI 

       430        440        450        460        470        480 
AVFAIYAHTA SEGLRGTETT LALPMASDLL LYDVTENSMR VKWDAVPGAS GYLILYAPLT 

       490        500        510        520        530        540 
EGLAGDEKEM KIGETHTDIE LSGLLPNTEY TVTVYAMFGE EASDPVTGQE TTLALSPPRN 

       550        560        570        580        590        600 
LRISNVGSNS ARLTWDPTSR QINGYRIVYN NADGTEINEV EVDPITTFPL KGLTPLTEYT 

       610        620        630        640        650        660 
IAIFSIYDEG QSEPLTGVFT TEEVPAQQYL EIDEVTTDSF RVTWHPLSAD EGLHKLMWIP 

       670        680        690        700        710        720 
VYGGKTEEVV LKEEQDSHVI EGLEPGTEYE VSLLAVLDDG SESEVVTAVG TTLDSFWTEP 

       730        740        750        760        770        780 
ATTIVPTTSV TSVFQTGIRN LVVGDETTSS LRVKWDISDS DVQQFRVTYM TAQGDPEEEV 

       790        800        810        820        830        840 
IGTVMVPGSQ NNLLLKPLLP DTEYKVTVTP IYTDGEGVSV SAPGKTLPSS GPQNLRVSEE 

       850        860        870        880        890        900 
WYNRLRITWD PPSSPVKGYR IVYKPVSVPG PTLETFVGAD INTILITNLL SGMDYNVKIF 

       910        920        930        940        950        960 
ASQASGFSDA LTGMVKTLFL GVTNLQAKHV EMTSLCAHWQ VHRHATAYRV VIESLQDRQK 

       970        980        990       1000       1010       1020 
QESTVGGGTT RHCFYGLQPD SEYKISVYTK LQEIEGPSVS IMEKTQSLPT RPPTFPPTIP 

      1030       1040       1050       1060       1070       1080 
PAKEVCKAAK ADLVFMVDGS WSIGDENFNK IISFLYSTVG ALNKIGTDGT QVAMVQFTDD 

      1090       1100       1110       1120       1130       1140 
PRTEFKLNAY KTKETLLDAI KHISYKGGNT KTGKAIKYVR DTLFTAESGT RRGIPKVIVV 

      1150       1160       1170       1180       1190       1200 
ITDGRSQDDV NKISREMQLD GYSIFAIGVA DADYSELVSI GSKPSARHVF FVDDFDAFKK 

      1210       1220       1230       1240       1250       1260 
IEDELITFVC ETASATCPVV HKDGIDLAGF KMMEMFGLVE KDFSSVEGVS MEPGTFNVFP 

      1270       1280       1290       1300       1310       1320 
CYQLHKDALV SQPTRYLHPE GLPSDYTISF LFRILPDTPQ EPFALWEILN KNSDPLVGVI 

      1330       1340       1350       1360       1370       1380 
LDNGGKTLTY FNYDQSGDFQ TVTFEGPEIR KIFYGSFHKL HIVVSETLVK VVIDCKQVGE 

      1390       1400       1410       1420       1430       1440 
KAMNASANIT SDGVEVLGKM VRSRGPGGNS APFQLQMFDI VCSTSWANTD KCCELPGLRD 

      1450       1460       1470       1480       1490       1500 
DESCPDLPHS CSCSETNEVA LGPAGPPGGP GLRGPKGQQG EPGPKGPDGP RGEIGLPGPQ 

      1510       1520       1530       1540       1550       1560 
GPPGPQGPSG LSIQGMPGMP GEKGEKGDTG LPGPQGIPGG VGSPGRDGSP GQRGLPGKDG 

      1570       1580       1590       1600       1610       1620 
SSGPPGPPGP IGIPGTPGVP GITGSMGPQG ALGPPGVPGA KGERGERGDL QSQAMVRSVA 

      1630       1640       1650       1660       1670       1680 
RQVCEQLIQS HMARYTAILN QIPSHSSSIR TVQGPPGEPG RPGSPGAPGE QGPPGTPGFP 

      1690       1700       1710       1720       1730       1740 
GNAGVPGTPG ERGLTGIKGE KGNPGVGTQG PRGPPGPAGP SGESRPGSPG PPGSPGPRGP 

      1750       1760       1770       1780       1790 
PGHLGVPGPQ GPSGQPGYCD PSSCSAYGVR APHPDQPEFT PVQDELEAME LWGPGV 

« Hide

Isoform 2 [UniParc].

Checksum: D0818CA6359B66D4
Show »

FASTA1,780191,903
Isoform 3 (Undulin 2) (Un2) [UniParc].

Checksum: 351A5F24379FEDF0
Show »

FASTA1,701183,154

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34938.1. [Q05707-1]
PIRA40970.
B40970.
S37749.
S46657.
RefSeqNP_066933.1. NM_021110.2. [Q05707-1]
XP_005251116.1. XM_005251059.1. [Q05707-2]
XP_006716714.1. XM_006716651.1. [Q05707-1]
UniGeneHs.409662.

3D structure databases

ProteinModelPortalQ05707.
SMRQ05707. Positions 30-113, 158-1000, 1032-1194, 1225-1436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113219. 4 interactions.
IntActQ05707. 2 interactions.

PTM databases

PhosphoSiteQ05707.

Polymorphism databases

DMDM125987815.

Proteomic databases

MaxQBQ05707.
PaxDbQ05707.
PRIDEQ05707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247781; ENSP00000247781; ENSG00000187955. [Q05707-3]
ENST00000297848; ENSP00000297848; ENSG00000187955. [Q05707-1]
ENST00000309791; ENSP00000311809; ENSG00000187955. [Q05707-2]
GeneID7373.
KEGGhsa:7373.
UCSCuc003yox.4. human. [Q05707-1]

Organism-specific databases

CTD7373.
GeneCardsGC08P121093.
H-InvDBHIX0007753.
HGNCHGNC:2191. COL14A1.
HPAHPA023781.
MIM120324. gene.
neXtProtNX_Q05707.
Orphanet79501. Punctate palmoplantar keratoderma type 1.
PharmGKBPA26707.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307460.
HOVERGENHBG051060.
InParanoidQ05707.
KOK08133.
OMAWYNRLRI.
OrthoDBEOG71P290.
PhylomeDBQ05707.
TreeFamTF329914.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ05707.
BgeeQ05707.
CleanExHS_COL14A1.
GenevestigatorQ05707.

Family and domain databases

Gene3D2.60.40.10. 8 hits.
3.40.50.410. 2 hits.
InterProIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view]
PfamPF01391. Collagen. 4 hits.
PF00041. fn3. 8 hits.
PF00092. VWA. 2 hits.
[Graphical view]
SMARTSM00060. FN3. 8 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 6 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 2 hits.
PROSITEPS50853. FN3. 8 hits.
PS50234. VWFA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL14A1. human.
GeneWikiCollagen,_type_XIV,_alpha_1.
GenomeRNAi7373.
NextBio28870.
PROQ05707.
SOURCESearch...

Entry information

Entry nameCOEA1_HUMAN
AccessionPrimary (citable) accession number: Q05707
Secondary accession number(s): B2RU07 expand/collapse secondary AC list , O00260, O00261, O00262, Q05708, Q5XJ18, Q96C67, Q9UDF6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM