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Q05707

- COEA1_HUMAN

UniProt

Q05707 - COEA1_HUMAN

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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

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
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: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
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 – 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

BgeeiQ05707.
CleanExiHS_COL14A1.
ExpressionAtlasiQ05707. baseline and differential.
GenevestigatoriQ05707.

Organism-specific databases

HPAiHPA023781.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

BioGridi113219. 16 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.
GeneTreeiENSGT00760000119000.
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.
IPR013320. ConA-like_dom.
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

        10         20         30         40         50
MKIFQRKMRY WLLPPFLAIV YFCTIVQGQV APPTRLRYNV ISHDSIQISW
60 70 80 90 100
KAPRGKFGGY KLLVTPTSGG KTNQLNLQNT ATKAIIQGLM PDQNYTVQII
110 120 130 140 150
AYNKDKESKP AQGQFRIKDL EKRKDPKPRV KVVDRGNGSR PSSPEEVKFV
160 170 180 190 200
CQTPAIADIV ILVDGSWSIG RFNFRLVRHF LENLVTAFDV GSEKTRIGLA
210 220 230 240 250
QYSGDPRIEW HLNAFSTKDE VIEAVRNLPY KGGNTLTGLA LNYIFENSFK
260 270 280 290 300
PEAGSRTGVS KIGILITDGK SQDDIIPPSR NLRESGVELF AIGVKNADVN
310 320 330 340 350
ELQEIASEPD STHVYNVAEF DLMHTVVESL TRTLCSRVEE QDREIKASAH
360 370 380 390 400
AITGPPTELI TSEVTARSFM VNWTHAPGNV EKYRVVYYPT RGGKPDEVVV
410 420 430 440 450
DGTVSSTVLK NLMSLTEYQI AVFAIYAHTA SEGLRGTETT LALPMASDLL
460 470 480 490 500
LYDVTENSMR VKWDAVPGAS GYLILYAPLT EGLAGDEKEM KIGETHTDIE
510 520 530 540 550
LSGLLPNTEY TVTVYAMFGE EASDPVTGQE TTLALSPPRN LRISNVGSNS
560 570 580 590 600
ARLTWDPTSR QINGYRIVYN NADGTEINEV EVDPITTFPL KGLTPLTEYT
610 620 630 640 650
IAIFSIYDEG QSEPLTGVFT TEEVPAQQYL EIDEVTTDSF RVTWHPLSAD
660 670 680 690 700
EGLHKLMWIP VYGGKTEEVV LKEEQDSHVI EGLEPGTEYE VSLLAVLDDG
710 720 730 740 750
SESEVVTAVG TTLDSFWTEP ATTIVPTTSV TSVFQTGIRN LVVGDETTSS
760 770 780 790 800
LRVKWDISDS DVQQFRVTYM TAQGDPEEEV IGTVMVPGSQ NNLLLKPLLP
810 820 830 840 850
DTEYKVTVTP IYTDGEGVSV SAPGKTLPSS GPQNLRVSEE WYNRLRITWD
860 870 880 890 900
PPSSPVKGYR IVYKPVSVPG PTLETFVGAD INTILITNLL SGMDYNVKIF
910 920 930 940 950
ASQASGFSDA LTGMVKTLFL GVTNLQAKHV EMTSLCAHWQ VHRHATAYRV
960 970 980 990 1000
VIESLQDRQK QESTVGGGTT RHCFYGLQPD SEYKISVYTK LQEIEGPSVS
1010 1020 1030 1040 1050
IMEKTQSLPT RPPTFPPTIP PAKEVCKAAK ADLVFMVDGS WSIGDENFNK
1060 1070 1080 1090 1100
IISFLYSTVG ALNKIGTDGT QVAMVQFTDD PRTEFKLNAY KTKETLLDAI
1110 1120 1130 1140 1150
KHISYKGGNT KTGKAIKYVR DTLFTAESGT RRGIPKVIVV ITDGRSQDDV
1160 1170 1180 1190 1200
NKISREMQLD GYSIFAIGVA DADYSELVSI GSKPSARHVF FVDDFDAFKK
1210 1220 1230 1240 1250
IEDELITFVC ETASATCPVV HKDGIDLAGF KMMEMFGLVE KDFSSVEGVS
1260 1270 1280 1290 1300
MEPGTFNVFP CYQLHKDALV SQPTRYLHPE GLPSDYTISF LFRILPDTPQ
1310 1320 1330 1340 1350
EPFALWEILN KNSDPLVGVI LDNGGKTLTY FNYDQSGDFQ TVTFEGPEIR
1360 1370 1380 1390 1400
KIFYGSFHKL HIVVSETLVK VVIDCKQVGE KAMNASANIT SDGVEVLGKM
1410 1420 1430 1440 1450
VRSRGPGGNS APFQLQMFDI VCSTSWANTD KCCELPGLRD DESCPDLPHS
1460 1470 1480 1490 1500
CSCSETNEVA LGPAGPPGGP GLRGPKGQQG EPGPKGPDGP RGEIGLPGPQ
1510 1520 1530 1540 1550
GPPGPQGPSG LSIQGMPGMP GEKGEKGDTG LPGPQGIPGG VGSPGRDGSP
1560 1570 1580 1590 1600
GQRGLPGKDG SSGPPGPPGP IGIPGTPGVP GITGSMGPQG ALGPPGVPGA
1610 1620 1630 1640 1650
KGERGERGDL QSQAMVRSVA RQVCEQLIQS HMARYTAILN QIPSHSSSIR
1660 1670 1680 1690 1700
TVQGPPGEPG RPGSPGAPGE QGPPGTPGFP GNAGVPGTPG ERGLTGIKGE
1710 1720 1730 1740 1750
KGNPGVGTQG PRGPPGPAGP SGESRPGSPG PPGSPGPRGP PGHLGVPGPQ
1760 1770 1780 1790
GPSGQPGYCD PSSCSAYGVR APHPDQPEFT PVQDELEAME LWGPGV
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: Curated
The sequence AAH14640.1 differs from that shown. Reason: Frameshift at position 1047. Curated

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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000297848; 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:
EMBLi
GenBanki
DDBJi
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. 16 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 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.
GeneTreei ENSGT00760000119000.
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

Bgeei Q05707.
CleanExi HS_COL14A1.
ExpressionAtlasi Q05707. baseline and differential.
Genevestigatori Q05707.

Family and domain databases

Gene3Di 2.60.40.10. 8 hits.
3.40.50.410. 2 hits.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
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, 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 29, 2014
This is version 119 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