C0HLJ3 · CO1A1_NOTSH

Function

function

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

Miscellaneous

These protein fragments were extracted from ancient femur bone collected at Rampart Cave in Arizona.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular space
Molecular Functionextracellular matrix structural constituent conferring tensile strength
Biological Processextracellular matrix organization

Names & Taxonomy

Protein names

  • Recommended name
    Collagen alpha-1(I) chain
  • Alternative names
    • Alpha-1 type I collagen

Organism names

Accessions

  • Primary accession
    C0HLJ3

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

Type
IDPosition(s)Description
ChainPRO_00004484701-998Collagen alpha-1(I) chain
Modified residue254-hydroxyproline
Modified residue284-hydroxyproline
Modified residue304-hydroxyproline
Modified residue394-hydroxyproline
Modified residue424-hydroxyproline
Modified residue454-hydroxyproline
Modified residue594-hydroxyproline
Modified residue744-hydroxyproline
Modified residue804-hydroxyproline
Modified residue894-hydroxyproline
Modified residue954-hydroxyproline
Modified residue985-hydroxylysine; alternate
Glycosylation98O-linked (Gal...) hydroxylysine; alternate
Modified residue104Phosphoserine
Modified residue1224-hydroxyproline
Modified residue1254-hydroxyproline
Modified residue1314-hydroxyproline
Modified residue1404-hydroxyproline
Modified residue1464-hydroxyproline
Modified residue1674-hydroxyproline
Modified residue1764-hydroxyproline
Modified residue1794-hydroxyproline
Modified residue2064-hydroxyproline
Modified residue2094-hydroxyproline
Modified residue2214-hydroxyproline
Modified residue2274-hydroxyproline
Modified residue2364-hydroxyproline
Modified residue2424-hydroxyproline
Modified residue2454-hydroxyproline
Modified residue2604-hydroxyproline
Modified residue2635-hydroxylysine
Modified residue2694-hydroxyproline
Modified residue2724-hydroxyproline
Modified residue2844-hydroxyproline
Modified residue2934-hydroxyproline
Modified residue3084-hydroxyproline
Modified residue3144-hydroxyproline
Modified residue3234-hydroxyproline
Modified residue3294-hydroxyproline
Modified residue3385-hydroxylysine
Modified residue3474-hydroxyproline
Modified residue3564-hydroxyproline
Modified residue3624-hydroxyproline
Modified residue3684-hydroxyproline
Modified residue3774-hydroxyproline
Modified residue3804-hydroxyproline
Modified residue3894-hydroxyproline
Modified residue3984-hydroxyproline
Modified residue4044-hydroxyproline
Modified residue4164-hydroxyproline
Modified residue4254-hydroxyproline
Modified residue4344-hydroxyproline
Modified residue4374-hydroxyproline
Modified residue4554-hydroxyproline
Modified residue4724-hydroxyproline
Modified residue4784-hydroxyproline
Modified residue4844-hydroxyproline
Modified residue4904-hydroxyproline
Modified residue4964-hydroxyproline
Modified residue5024-hydroxyproline
Modified residue5144-hydroxyproline
Modified residue5234-hydroxyproline
Modified residue5374-hydroxyproline
Modified residue5434-hydroxyproline
Modified residue5524-hydroxyproline
Modified residue5645-hydroxylysine
Modified residue5704-hydroxyproline
Modified residue5854-hydroxyproline
Modified residue5914-hydroxyproline
Modified residue600Phosphoserine
Modified residue6124-hydroxyproline
Modified residue6184-hydroxyproline
Modified residue6214-hydroxyproline
Modified residue6304-hydroxyproline
Modified residue6364-hydroxyproline
Modified residue6544-hydroxyproline
Modified residue6634-hydroxyproline
Modified residue6724-hydroxyproline
Modified residue6755-hydroxylysine
Modified residue6844-hydroxyproline
Modified residue6904-hydroxyproline
Modified residue6983-hydroxyproline
Modified residue6994-hydroxyproline
Modified residue7084-hydroxyproline
Modified residue7114-hydroxyproline
Modified residue7324-hydroxyproline
Modified residue7414-hydroxyproline
Modified residue7494-hydroxyproline
Modified residue7584-hydroxyproline
Modified residue7764-hydroxyproline
Modified residue7854-hydroxyproline
Modified residue7884-hydroxyproline
Modified residue7944-hydroxyproline
Modified residue8094-hydroxyproline
Modified residue8154-hydroxyproline
Modified residue8214-hydroxyproline
Modified residue8304-hydroxyproline
Modified residue8364-hydroxyproline
Modified residue8455-hydroxylysine
Modified residue8564-hydroxyproline
Modified residue8594-hydroxyproline
Modified residue8624-hydroxyproline
Modified residue9075-hydroxylysine
Modified residue9195-hydroxylysine; alternate
Glycosylation919O-linked (Gal...) hydroxylysine; alternate
Modified residue9344-hydroxyproline
Modified residue9374-hydroxyproline
Modified residue9554-hydroxyproline
Modified residue9704-hydroxyproline
Modified residue9753-hydroxyproline
Modified residue9764-hydroxyproline
Modified residue9903-hydroxyproline
Modified residue9914-hydroxyproline
Modified residue9933-hydroxyproline
Modified residue9944-hydroxyproline
Modified residue9963-hydroxyproline
Modified residue9974-hydroxyproline

Post-translational modification

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.

Keywords

Expression

Tissue specificity

Expressed in bones.

Interaction

Subunit

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

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-998Disordered
Compositional bias18-59Pro residues
Compositional bias252-266Pro residues
Compositional bias382-405Pro residues
Compositional bias655-669Pro residues
Compositional bias701-715Pro residues
Compositional bias733-747Pro residues

Sequence similarities

Belongs to the fibrillar collagen family.

Family and domain databases

Sequence

  • Sequence status
    Fragments
  • Length
    998
  • Mass (Da)
    89,146
  • Last updated
    2019-11-13 v1
  • Checksum
    64842BD4699508CB
SYGYDEKGGVSVPGPMGPSGPRGLPGPPGPGPQGFQGPPGEPGEPGSGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGASGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGARGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGPPGPKGNSGEPGAPGSKGDTGAKGEPGPTGIQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGNGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPTGPPGPIGNVGAPGPKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPVGKEGGKGPRGETGPAGRPGEVGPPGPPGPGEKGSPGADGPAGAPGTPGPQGISGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGSSGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGPKGDRGETGPGPPGAPGAPGAPGPVGPAGKNGDRGETGPAGPAGPAGPAGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPAGPPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDAGPVGPPGPPGPPG

Features

Showing features for non-terminal residue, non-adjacent residues, compositional bias, sequence uncertainty.

Type
IDPosition(s)Description
Non-terminal residue1
Non-adjacent residues7-8
Compositional bias18-59Pro residues
Sequence uncertainty24L or I
Non-adjacent residues29-30
Non-adjacent residues46-47
Sequence uncertainty88L or I
Sequence uncertainty94L or I
Sequence uncertainty106L or I
Sequence uncertainty139L or I
Sequence uncertainty238I or L
Compositional bias252-266Pro residues
Sequence uncertainty289I or L
Sequence uncertainty313L or I
Sequence uncertainty367L or I
Sequence uncertainty373L or I
Compositional bias382-405Pro residues
Non-adjacent residues471-472
Sequence uncertainty477L or I
Sequence uncertainty499L or I
Non-adjacent residues530-531
Non-adjacent residues532-533
Sequence uncertainty539L or I
Sequence uncertainty551L or I
Sequence uncertainty578L or I
Sequence uncertainty582I or L
Compositional bias655-669Pro residues
Sequence uncertainty666I or L
Compositional bias701-715Pro residues
Compositional bias733-747Pro residues
Non-adjacent residues743-744
Sequence uncertainty766I or L
Sequence uncertainty775L or I
Sequence uncertainty787L or I
Sequence uncertainty817L or I
Non-adjacent residues853-854
Sequence uncertainty918I or L
Sequence uncertainty927L or I
Sequence uncertainty966L or I
Sequence uncertainty969L or I
Sequence uncertainty973I or L
Non-terminal residue998

Keywords

Similar Proteins

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