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Entry version 168 (08 May 2019)
Sequence version 2 (29 Aug 2001)
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Protein

Collagen alpha-2(I) chain

Gene

Col1a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1187CalciumBy similarity1
Metal bindingi1189CalciumBy similarity1
Metal bindingi1190Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1192Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1195CalciumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-114604 GPVI-mediated activation cascade
R-MMU-1442490 Collagen degradation
R-MMU-1474244 Extracellular matrix organization
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-216083 Integrin cell surface interactions
R-MMU-2214320 Anchoring fibril formation
R-MMU-2243919 Crosslinking of collagen fibrils
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-430116 GP1b-IX-V activation signalling
R-MMU-75892 Platelet Adhesion to exposed collagen
R-MMU-76009 Platelet Aggregation (Plug Formation)
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8948216 Collagen chain trimerization

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Col1a2
Synonyms:Cola2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88468 Col1a2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 22By similarityAdd BLAST22
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000580723 – 85N-terminal propeptideBy similarityAdd BLAST63
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000580886 – 1125Collagen alpha-2(I) chainAdd BLAST1040
PropeptideiPRO_00000058091126 – 1372C-terminal propeptideBy similarityAdd BLAST247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei23Pyrrolidone carboxylic acidBy similarity1
Modified residuei90AllysineBy similarity1
Modified residuei1835-hydroxylysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi183O-linked (Gal...) hydroxylysine; alternateBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi1169 ↔ 1201PROSITE-ProRule annotation
Disulfide bondi1209 ↔ 1370PROSITE-ProRule annotation
Glycosylationi1273N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1278 ↔ 1323PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q01149

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q01149

PeptideAtlas

More...
PeptideAtlasi
Q01149

PRoteomics IDEntifications database

More...
PRIDEi
Q01149

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01149

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q01149

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000029661 Expressed in 292 organ(s), highest expression level in vault of skull

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q01149 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q01149 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198832, 1 interactor

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2956 Collagen type I trimer

Protein interaction database and analysis system

More...
IntActi
Q01149, 1 interactor

Molecular INTeraction database

More...
MINTi
Q01149

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000031668

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q01149

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1139 – 1372Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3544 Eukaryota
ENOG410XNMM LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155639

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000085654

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01149

KEGG Orthology (KO)

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KOi
K06236

Identification of Orthologs from Complete Genome Data

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OMAi
PTGKHGN

Database of Orthologous Groups

More...
OrthoDBi
1406711at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q01149

TreeFam database of animal gene trees

More...
TreeFami
TF344135

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 6 hits

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00038 COLFI, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51461 NC1_FIB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q01149-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSFVDTRTL LLLAVTSCLA TCQYLQSGSV RKGPTGDRGP RGQRGPAGPR
60 70 80 90 100
GRDGVDGPMG PPGPPGSPGP PGSPAPPGLT GNFAAQYSDK GVSSGPGPMG
110 120 130 140 150
LMGPRGPPGA VGAPGPQGFQ GPAGEPGEPG QTGPAGPRGP AGSPGKAGED
160 170 180 190 200
GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP GFKGVKGHSG MDGLKGQPGA
210 220 230 240 250
QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR GSDGSVGPVG
260 270 280 290 300
PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE VGLPGLSGPV
310 320 330 340 350
GPPGNPGTNG LTGAKGATGL PGVAGAPGLP GPRGIPGPAG AAGATGARGL
360 370 380 390 400
VGEPGPAGSK GESGNKGEPG SVGAQGPPGP SGEEGKRGSP GEAGSAGPAG
410 420 430 440 450
PPGLRGSPGS RGLPGADGRA GVMGPPGNRG STGPAGIRGP NGDAGRPGEP
460 470 480 490 500
GLMGPRGLPG SPGNVGPSGK EGPVGLPGID GRPGPIGPAG PRGEAGNIGF
510 520 530 540 550
PGPKGPSGDP GKPGERGHPG LAGARGAPGP DGNNGAQGPP GPQGVQGGKG
560 570 580 590 600
EQGPAGPPGF QGLPGPSGTT GEVGKPGERG LPGEFGLPGP AGPRGERGTP
610 620 630 640 650
GESGAAGPSG PIGSRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE
660 670 680 690 700
RGAAGIPGGK GEKGETGLRG DTGNTGRDGA RGIPGAVGAP GPAGASGDRG
710 720 730 740 750
EAGAAGPSGP AGPRGSPGER GEVGPAGPNG FAGPAGAAGQ PGAKGEKGTK
760 770 780 790 800
GPKGENGIVG PTGSVGAAGP SGPNGPPGPV GSRGDGGPPG MTGFPGAAGR
810 820 830 840 850
TGPPGPSGIA GPPGPPGAAG KEGIRGPRGD QGPVGRTGET GASGPPGFVG
860 870 880 890 900
EKGPSGEPGT AGAPGTAGPQ GLLGAPGILG LPGSRGERGL PGIAGALGEP
910 920 930 940 950
GPLGISGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH
960 970 980 990 1000
KGERGYPGSI GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG
1010 1020 1030 1040 1050
PRGPSGPQGI RGDKGEPGDK GHRGLPGLKG YSGLQGLPGL AGLHGDQGAP
1060 1070 1080 1090 1100
GPVGPAGPRG PAGPSGPVGK DGRSGQPGPV GPAGVRGSQG SQGPAGPPGP
1110 1120 1130 1140 1150
PGPPGPPGVS GGGYDFGFEG DFYRADQPRS QPSLRPKDYE VDATLKSLNN
1160 1170 1180 1190 1200
QIETLLTPEG SRKNPARTCR DLRLSHPEWN SDYYWIDPNQ GCTMDAIKVY
1210 1220 1230 1240 1250
CDFSTGETCI QAQPVNTPAK NSYSRAQANK HVWLGETING GSQFEYNVEG
1260 1270 1280 1290 1300
VSSKEMATQL AFMRLLANRA SQNITYHCKN SIAYLDEETG SLNKAVLLQG
1310 1320 1330 1340 1350
SNDVELVAEG NSRFTYSVLV DGCSKKTNEW GKTIIEYKTN KPSRLPFLDI
1360 1370
APLDIGGADQ EFRVEVGPVC FK
Length:1,372
Mass (Da):129,557
Last modified:August 29, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0D17DF5D6C1452D1
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E0CXI2E0CXI2_MOUSE
Collagen alpha-2(I) chain
Col1a2
177Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti15V → A in AAA37331 (PubMed:3039494).Curated1
Sequence conflicti1167R → TT in CAA41205 (PubMed:1505972).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X58251 mRNA Translation: CAA41205.1
BC007158 mRNA Translation: AAH07158.1
BC042503 mRNA Translation: AAH42503.2
K01832 Genomic DNA Translation: AAA37331.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS39420.1

Protein sequence database of the Protein Information Resource

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PIRi
A43291

NCBI Reference Sequences

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RefSeqi
NP_031769.2, NM_007743.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000031668; ENSMUSP00000031668; ENSMUSG00000029661

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
12843

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12843

UCSC genome browser

More...
UCSCi
uc009avm.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58251 mRNA Translation: CAA41205.1
BC007158 mRNA Translation: AAH07158.1
BC042503 mRNA Translation: AAH42503.2
K01832 Genomic DNA Translation: AAA37331.1
CCDSiCCDS39420.1
PIRiA43291
RefSeqiNP_031769.2, NM_007743.3

3D structure databases

SMRiQ01149
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198832, 1 interactor
ComplexPortaliCPX-2956 Collagen type I trimer
IntActiQ01149, 1 interactor
MINTiQ01149
STRINGi10090.ENSMUSP00000031668

PTM databases

iPTMnetiQ01149
PhosphoSitePlusiQ01149

Proteomic databases

jPOSTiQ01149
PaxDbiQ01149
PeptideAtlasiQ01149
PRIDEiQ01149

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031668; ENSMUSP00000031668; ENSMUSG00000029661
GeneIDi12843
KEGGimmu:12843
UCSCiuc009avm.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1278
MGIiMGI:88468 Col1a2

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00940000155639
HOGENOMiHOG000085654
InParanoidiQ01149
KOiK06236
OMAiPTGKHGN
OrthoDBi1406711at2759
PhylomeDBiQ01149
TreeFamiTF344135

Enzyme and pathway databases

ReactomeiR-MMU-114604 GPVI-mediated activation cascade
R-MMU-1442490 Collagen degradation
R-MMU-1474244 Extracellular matrix organization
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-202733 Cell surface interactions at the vascular wall
R-MMU-216083 Integrin cell surface interactions
R-MMU-2214320 Anchoring fibril formation
R-MMU-2243919 Crosslinking of collagen fibrils
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-3000178 ECM proteoglycans
R-MMU-430116 GP1b-IX-V activation signalling
R-MMU-75892 Platelet Adhesion to exposed collagen
R-MMU-76009 Platelet Aggregation (Plug Formation)
R-MMU-8874081 MET activates PTK2 signaling
R-MMU-8948216 Collagen chain trimerization

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Col1a2 mouse

Protein Ontology

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PROi
PR:Q01149

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000029661 Expressed in 292 organ(s), highest expression level in vault of skull
ExpressionAtlasiQ01149 baseline and differential
GenevisibleiQ01149 MM

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 6 hits
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO1A2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01149
Secondary accession number(s): Q8CGA5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: August 29, 2001
Last modified: May 8, 2019
This is version 168 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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