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Q07092

- COGA1_HUMAN

UniProt

Q07092 - COGA1_HUMAN

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Protein

Collagen alpha-1(XVI) chain

Gene

COL16A1

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

Functioni

Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.1 Publication

GO - Molecular functioni

  1. integrin binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. cellular response to amino acid stimulus Source: Ensembl
  3. collagen catabolic process Source: Reactome
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. female pregnancy Source: ProtInc
  7. integrin-mediated signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150401. Collagen degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XVI) chain
Gene namesi
Name:COL16A1
ORF Names:FP1572
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2193. COL16A1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

  1. collagen type XVI trimer Source: ProtInc
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular region Source: Reactome
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26709.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21212 PublicationsAdd
BLAST
Chaini22 – 16041583Collagen alpha-1(XVI) chainPRO_0000005792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Glycosylated.2 Publications

Keywords - PTMi

Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ07092.
PaxDbiQ07092.
PRIDEiQ07092.

PTM databases

PhosphoSiteiQ07092.

Expressioni

Tissue specificityi

In papillary dermis, is a component of specialized fibrillin-1-containing microfibrils, whereas in territorial cartilage matrix, it is localized to a discrete population of thin, weakly banded collagen fibrils in association with other collagens (at protein level). In the placenta, where it is found in the amnion, a membranous tissue lining the amniotic cavity. Within the amnion, it is found in an acellular, relatively dense layer of a complex network of reticular fibers. Also located to a fibroblast layer beneath this dense layer. Exists in tissues in association with other types of collagen.1 Publication

Developmental stagei

Transiently elevated expression during gestation, and decrease at term.

Gene expression databases

BgeeiQ07092.
CleanExiHS_COL16A1.
ExpressionAtlasiQ07092. baseline and differential.
GenevestigatoriQ07092.

Organism-specific databases

HPAiHPA027235.
HPA027237.

Interactioni

Subunit structurei

Homotrimer. Interacts with FBN1, fibronectin and integrins ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique site within COL16A1 located close to its C-terminal end between collagenous domains COL1-COL3.4 Publications

Protein-protein interaction databases

BioGridi107703. 1 interaction.
IntActiQ07092. 3 interactions.
MINTiMINT-6743139.
STRINGi9606.ENSP00000362776.

Structurei

3D structure databases

ProteinModelPortaliQ07092.
SMRiQ07092. Positions 47-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 231182Laminin G-likeAdd
BLAST
Domaini375 – 42349Collagen-like 1Add
BLAST
Domaini573 – 63361Collagen-like 2Add
BLAST
Domaini667 – 72155Collagen-like 3Add
BLAST
Domaini788 – 84053Collagen-like 4Add
BLAST
Domaini888 – 93851Collagen-like 5Add
BLAST
Domaini1018 – 107558Collagen-like 6Add
BLAST
Domaini1472 – 152453Collagen-like 7Add
BLAST
Domaini1528 – 157649Collagen-like 8Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni232 – 374143Nonhelical region 10 (NC10)Add
BLAST
Regioni375 – 506132Triple-helical region 9 (COL9) with 3 imperfectionsAdd
BLAST
Regioni507 – 52115Nonhelical region 9 (NC9)Add
BLAST
Regioni522 – 55534Triple-helical region 8 (COL8) with 1 imperfectionAdd
BLAST
Regioni556 – 57217Nonhelical region 8 (NC8)Add
BLAST
Regioni573 – 63159Triple-helical region 7 (COL7) with 1 imperfectionAdd
BLAST
Regioni632 – 65221Nonhelical region 7 (NC7)Add
BLAST
Regioni653 – 72371Triple-helical region 6 (COL6) with 1 imperfectionAdd
BLAST
Regioni724 – 73815Nonhelical region 6 (NC6)Add
BLAST
Regioni739 – 876138Triple-helical region 5 (COL5) with 3 imperfectionsAdd
BLAST
Regioni877 – 88711Nonhelical region 5 (NC5)Add
BLAST
Regioni888 – 93952Triple-helical region 4 (COL4) with 2 imperfectionsAdd
BLAST
Regioni940 – 97334Nonhelical region 4 (NC4)Add
BLAST
Regioni974 – 98815Triple-helical region 3 (COL3)Add
BLAST
Regioni989 – 101123Nonhelical region 3 (NC3)Add
BLAST
Regioni1012 – 1433422Triple-helical region 2 (COL2) with 2 imperfectionsAdd
BLAST
Regioni1434 – 147239Nonhelical region 2 (NC2)Add
BLAST
Regioni1473 – 1578106Triple-helical region 1 (COL1) with 2 imperfectionsAdd
BLAST
Regioni1579 – 160426Nonhelical region 1 (NC1)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi540 – 5423Cell attachment siteSequence Analysis
Motifi1006 – 10083Cell attachment siteSequence Analysis
Motifi1227 – 12293Cell attachment siteSequence Analysis

Domaini

This sequence defines eighteen different domains, nine triple-helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10 to NC1). The numerous interruptions in the triple helix may make this molecule either elastic or flexible.

Sequence similaritiesi

Contains 8 collagen-like domains.Curated
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118927.
HOGENOMiHOG000085653.
HOVERGENiHBG071631.
InParanoidiQ07092.
OMAiSTWYLFQ.
OrthoDBiEOG779NXQ.
PhylomeDBiQ07092.
TreeFamiTF332900.

Family and domain databases

InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 8 hits.
[Graphical view]
SMARTiSM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q07092-1) [UniParc]FASTAAdd to Basket

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
MWVSWAPGLW LLGLWATFGH GANTGAQCPP SQQEGLKLEH SSSLPANVTG
60 70 80 90 100
FNLIHRLSLM KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF
110 120 130 140 150
ALVLTLLLKK HTHQKTWYLF QVTDANGYPQ ISLEVNSQER SLELRAQGQD
160 170 180 190 200
GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA SVHVDCSSAS SQPLGPRRPM
210 220 230 240 250
RPVGHVFLGL DAEQGKPVSF DLQQVHIYCD PELVLEEGCC EILPAGCPPE
260 270 280 290 300
TSKARRDTQS NELIEINPQS EGKVYTRCFC LEEPQNSEVD AQLTGRISQK
310 320 330 340 350
AERGAKVHQE TAADECPPCV HGARDSNVTL APSGPKGGKG ERGLPGPPGS
360 370 380 390 400
KGEKGARGND CVRISPDAPL QCAEGPKGEK GESGALGPSG LPGSTGEKGQ
410 420 430 440 450
KGEKGDGGIK GVPGKPGRDG RPGEICVIGP KGQKGDPGFV GPEGLAGEPG
460 470 480 490 500
PPGLPGPPGI GLPGTPGDPG GPPGPKGDKG SSGIPGKEGP GGKPGKPGVK
510 520 530 540 550
GEKGDPCEVC PTLPEGFQNF VGLPGKPGPK GEPGDPVPAR GDPGIQGIKG
560 570 580 590 600
EKGEPCLSCS SVVGAQHLVS STGASGDVGS PGFGLPGLPG RAGVPGLKGE
610 620 630 640 650
KGNFGEAGPA GSPGPPGPVG PAGIKGAKGE PCEPCPALSN LQDGDVRVVA
660 670 680 690 700
LPGPSGEKGE PGPPGFGLPG KQGKAGERGL KGQKGDAGNP GDPGTPGTTG
710 720 730 740 750
RPGLSGEPGV QGPAGPKGEK GDGCTACPSL QGTVTDMAGR PGQPGPKGEQ
760 770 780 790 800
GPEGVGRPGK PGQPGLPGVQ GPPGLKGVQG EPGPPGRGVQ GPQGEPGAPG
810 820 830 840 850
LPGIQGLPGP RGPPGPTGEK GAQGSPGVKG ATGPVGPPGA SVSGPPGRDG
860 870 880 890 900
QQGQTGLRGT PGEKGPRGEK GEPGECSCPS QGDLIFSGMP GAPGLWMGSS
910 920 930 940 950
WQPGPQGPPG IPGPPGPPGV PGLQGVPGNN GLPGQPGLTA ELGSLPIEQH
960 970 980 990 1000
LLKSICGDCV QGQRAHPGYL VEKGEKGDQG IPGVPGLDNC AQCFLSLERP
1010 1020 1030 1040 1050
RAEEARGDNS EGDPGCVGSP GLPGPPGLPG QRGEEGPPGM RGSPGPPGPI
1060 1070 1080 1090 1100
GPPGFPGAVG SPGLPGLQGE RGLTGLTGDK GEPGPPGQPG YPGATGPPGL
1110 1120 1130 1140 1150
PGIKGERGYT GSAGEKGEPG PPGSEGLPGP PGPAGPRGER GPQGNSGEKG
1160 1170 1180 1190 1200
DQGFQGQPGF PGPPGPPGFP GKVGSPGPPG PQAEKGSEGI RGPSGLPGSP
1210 1220 1230 1240 1250
GPPGPPGIQG PAGLDGLDGK DGKPGLRGDP GPAGPPGLMG PPGFKGKTGH
1260 1270 1280 1290 1300
PGLPGPKGDC GKPGPPGSTG RPGAEGEPGA MGPQGRPGPP GHVGPPGPPG
1310 1320 1330 1340 1350
QPGPAGISAV GLKGDRGATG ERGLAGLPGQ PGPPGHPGPP GEPGTDGAAG
1360 1370 1380 1390 1400
KEGPPGKQGF YGPPGPKGDP GAAGQKGQAG EKGRAGMPGG PGKSGSMGPV
1410 1420 1430 1440 1450
GPPGPAGERG HPGAPGPSGS PGLPGVPGSM GDMVNYDEIK RFIRQEIIKM
1460 1470 1480 1490 1500
FDERMAYYTS RMQFPMEMAA APGRPGPPGK DGAPGRPGAP GSPGLPGQIG
1510 1520 1530 1540 1550
REGRQGLPGV RGLPGTKGEK GDIGIGIAGE NGLPGPPGPQ GPPGYGKMGA
1560 1570 1580 1590 1600
TGPMGQQGIP GIPGPPGPMG QPGKAGHCNP SDCFGAMPME QQYPPMKTMK

GPFG
Length:1,604
Mass (Da):157,751
Last modified:April 3, 2007 - v2
Checksum:i5FAA1950DFC6CA3C
GO
Isoform 2 (identifier: Q07092-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1052-1052: Missing.
     1161-1161: Missing.

Note: No experimental confirmation available.

Show »
Length:1,602
Mass (Da):157,557
Checksum:iC0F8388B57BBA080
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4191D → G in AAB25797. (PubMed:1284248)Curated
Sequence conflicti420 – 4212GR → A in AAA58427. (PubMed:1631157)Curated
Sequence conflicti538 – 5381P → R in AAA58427. (PubMed:1631157)Curated
Sequence conflicti848 – 8492RD → VM in CAA33142. 1 PublicationCurated
Sequence conflicti848 – 8492RD → VM in CAA33085. 1 PublicationCurated
Sequence conflicti1161 – 11611P → T in AAA58427. (PubMed:1631157)Curated
Sequence conflicti1164 – 11641P → T in AAA58427. (PubMed:1631157)Curated
Sequence conflicti1166 – 11661P → S in AAA58427. (PubMed:1631157)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271Q → H.
Corresponds to variant rs2229802 [ dbSNP | Ensembl ].
VAR_048777
Natural varianti62 – 621T → K.1 Publication
Corresponds to variant rs2228552 [ dbSNP | Ensembl ].
VAR_031440
Natural varianti418 – 4181R → Q.
Corresponds to variant rs6699645 [ dbSNP | Ensembl ].
VAR_048778
Natural varianti745 – 7451G → S.
Corresponds to variant rs34770879 [ dbSNP | Ensembl ].
VAR_048779
Natural varianti909 – 9091P → L.
Corresponds to variant rs2229804 [ dbSNP | Ensembl ].
VAR_048780

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1052 – 10521Missing in isoform 2. 1 PublicationVSP_024259
Alternative sequencei1161 – 11611Missing in isoform 2. 1 PublicationVSP_024260

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M92642 mRNA. Translation: AAA58427.1.
AC114488 Genomic DNA. No translation available.
AB209571 mRNA. Translation: BAD92808.1.
X14963 mRNA. Translation: CAA33085.1.
X15038 mRNA. Translation: CAA33142.1.
S57132 mRNA. Translation: AAB25797.1.
AF370368 mRNA. Translation: AAQ15204.1.
CCDSiCCDS41297.1. [Q07092-1]
PIRiS23810.
RefSeqiNP_001847.3. NM_001856.3. [Q07092-1]
UniGeneiHs.368921.

Genome annotation databases

EnsembliENST00000373672; ENSP00000362776; ENSG00000084636. [Q07092-1]
GeneIDi1307.
KEGGihsa:1307.
UCSCiuc001btj.1. human. [Q07092-2]
uc001btk.1. human. [Q07092-1]

Polymorphism databases

DMDMi143811380.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M92642 mRNA. Translation: AAA58427.1 .
AC114488 Genomic DNA. No translation available.
AB209571 mRNA. Translation: BAD92808.1 .
X14963 mRNA. Translation: CAA33085.1 .
X15038 mRNA. Translation: CAA33142.1 .
S57132 mRNA. Translation: AAB25797.1 .
AF370368 mRNA. Translation: AAQ15204.1 .
CCDSi CCDS41297.1. [Q07092-1 ]
PIRi S23810.
RefSeqi NP_001847.3. NM_001856.3. [Q07092-1 ]
UniGenei Hs.368921.

3D structure databases

ProteinModelPortali Q07092.
SMRi Q07092. Positions 47-242.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107703. 1 interaction.
IntActi Q07092. 3 interactions.
MINTi MINT-6743139.
STRINGi 9606.ENSP00000362776.

PTM databases

PhosphoSitei Q07092.

Polymorphism databases

DMDMi 143811380.

Proteomic databases

MaxQBi Q07092.
PaxDbi Q07092.
PRIDEi Q07092.

Protocols and materials databases

DNASUi 1307.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373672 ; ENSP00000362776 ; ENSG00000084636 . [Q07092-1 ]
GeneIDi 1307.
KEGGi hsa:1307.
UCSCi uc001btj.1. human. [Q07092-2 ]
uc001btk.1. human. [Q07092-1 ]

Organism-specific databases

CTDi 1307.
GeneCardsi GC01M032117.
H-InvDB HIX0028602.
HGNCi HGNC:2193. COL16A1.
HPAi HPA027235.
HPA027237.
MIMi 120326. gene.
neXtProti NX_Q07092.
PharmGKBi PA26709.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118927.
HOGENOMi HOG000085653.
HOVERGENi HBG071631.
InParanoidi Q07092.
OMAi STWYLFQ.
OrthoDBi EOG779NXQ.
PhylomeDBi Q07092.
TreeFami TF332900.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150401. Collagen degradation.

Miscellaneous databases

GeneWikii Collagen,_type_XVI,_alpha_1.
GenomeRNAii 1307.
NextBioi 5349.
PROi Q07092.
SOURCEi Search...

Gene expression databases

Bgeei Q07092.
CleanExi HS_COL16A1.
ExpressionAtlasi Q07092. baseline and differential.
Genevestigatori Q07092.

Family and domain databases

InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01391. Collagen. 8 hits.
[Graphical view ]
SMARTi SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal location of human alpha 1(XVI) collagen."
    Pan T.-C., Zhang R.-Z., Mattei M.-G., Timpl R., Chu M.-L.
    Proc. Natl. Acad. Sci. U.S.A. 89:6565-6569(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-62.
    Tissue: Fibroblast.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Recombinant analysis of human alpha 1 (XVI) collagen. Evidence for processing of the N-terminal globular domain."
    Tillet E., Mann K., Nischt R., Pan T.-C., Chu M.-L., Timpl R.
    Eur. J. Biochem. 228:160-168(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-33, SUBUNIT, GLYCOSYLATION.
  4. "Molecular structure and interaction of recombinant human type XVI collagen."
    Kassner A., Tiedemann K., Notbohm H., Ludwig T., Morgelin M., Reinhardt D.P., Chu M.-L., Bruckner P., Grassel S.
    J. Mol. Biol. 339:835-853(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-30; 257-265 AND 941-950, SUBUNIT, INTERACTION WITH FBN1 AND FN1, GLYCOSYLATION.
  5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-1604 (ISOFORM 2).
    Tissue: Spleen.
  6. Kimura S.
    Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 403-849.
    Tissue: Placenta.
  7. "Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing non-collagenous segments."
    Yamaguchi N., Kimura S., McBride O.W., Hori H., Yamada Y., Kanamori T., Yamakoshi H., Nagai Y.
    J. Biochem. 112:856-863(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 418-1604 (ISOFORM 1).
    Tissue: Placenta.
  8. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1387-1604.
  9. "Biosynthesis and processing of type XVI collagen in human fibroblasts and smooth muscle cells."
    Grassel S., Timpl R., Tan E.M.L., Chu M.-L.
    Eur. J. Biochem. 242:576-584(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  10. "Discrete integration of collagen XVI into tissue-specific collagen fibrils or beaded microfibrils."
    Kassner A., Hansen U., Miosge N., Reinhardt D.P., Aigner T., Bruckner-Tuderman L., Bruckner P., Grassel S.
    Matrix Biol. 22:131-143(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Collagen XVI harbors an integrin alpha1 beta1 recognition site in its C-terminal domains."
    Eble J.A., Kassner A., Niland S., Morgelin M., Grifka J., Grassel S.
    J. Biol. Chem. 281:25745-25756(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH INTEGRIN ALPHA-1/BETA-1 AND INTEGRIN ALPHA-2/BETA-1.

Entry informationi

Entry nameiCOGA1_HUMAN
AccessioniPrimary (citable) accession number: Q07092
Secondary accession number(s): Q16593, Q59F89, Q71RG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 137 of the entry and version 2 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 1
    Human chromosome 1: 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