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P11087

- CO1A1_MOUSE

UniProt

P11087 - CO1A1_MOUSE

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Protein

Collagen alpha-1(I) chain

Gene

Col1a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1266 – 12661CalciumBy similarity
Metal bindingi1268 – 12681CalciumBy similarity
Metal bindingi1269 – 12691Calcium; via carbonyl oxygenBy similarity
Metal bindingi1271 – 12711Calcium; via carbonyl oxygenBy similarity
Metal bindingi1274 – 12741CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: MGI
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood vessel development Source: MGI
  2. bone trabecula formation Source: MGI
  3. cartilage development involved in endochondral bone morphogenesis Source: MGI
  4. cellular response to amino acid stimulus Source: MGI
  5. cellular response to mechanical stimulus Source: UniProtKB
  6. cellular response to retinoic acid Source: Ensembl
  7. cellular response to transforming growth factor beta stimulus Source: Ensembl
  8. collagen biosynthetic process Source: Ensembl
  9. collagen fibril organization Source: Ensembl
  10. embryonic skeletal system development Source: Ensembl
  11. endochondral ossification Source: MGI
  12. face morphogenesis Source: MGI
  13. intramembranous ossification Source: MGI
  14. negative regulation of cell-substrate adhesion Source: MGI
  15. osteoblast differentiation Source: BHF-UCL
  16. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  17. positive regulation of cell migration Source: Ensembl
  18. positive regulation of epithelial to mesenchymal transition Source: Ensembl
  19. positive regulation of transcription, DNA-templated Source: Ensembl
  20. protein heterotrimerization Source: MGI
  21. protein localization to nucleus Source: Ensembl
  22. protein transport Source: MGI
  23. response to cAMP Source: Ensembl
  24. response to corticosteroid Source: Ensembl
  25. response to estradiol Source: Ensembl
  26. response to hydrogen peroxide Source: Ensembl
  27. response to nutrient Source: Ensembl
  28. response to peptide hormone Source: Ensembl
  29. sensory perception of sound Source: Ensembl
  30. skeletal system development Source: MGI
  31. skeletal system morphogenesis Source: MGI
  32. skin development Source: MGI
  33. skin morphogenesis Source: Ensembl
  34. tooth mineralization Source: Ensembl
  35. visual perception Source: Ensembl
  36. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196515. Crosslinking of collagen fibrils.
REACT_196581. Scavenging by Class A Receptors.
REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene namesi
Name:Col1a1
Synonyms:Cola1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:88467. Col1a1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen trimer Source: MGI
  2. collagen type I trimer Source: MGI
  3. cytoplasm Source: MGI
  4. extracellular matrix Source: UniProtKB
  5. extracellular space Source: Ensembl
  6. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Add
BLAST
Propeptidei23 – 151129N-terminal propeptidePRO_0000005722Add
BLAST
Chaini152 – 12071056Collagen alpha-1(I) chainPRO_0000005723Add
BLAST
Propeptidei1208 – 1453246C-terminal propeptidePRO_0000005724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
Modified residuei152 – 1521Pyrrolidone carboxylic acidBy similarity
Modified residuei160 – 1601AllysineBy similarity
Modified residuei254 – 25415-hydroxylysine; alternateBy similarity
Glycosylationi254 – 2541O-linked (Gal...); alternateBy similarity
Modified residuei1153 – 115313-hydroxyprolineBy similarity
Disulfide bondi1248 ↔ 1280PROSITE-ProRule annotation
Disulfide bondi1254 – 1254Interchain (with C-1271)PROSITE-ProRule annotation
Disulfide bondi1271 – 1271Interchain (with C-1254)PROSITE-ProRule annotation
Disulfide bondi1288 ↔ 1451PROSITE-ProRule annotation
Glycosylationi1354 – 13541N-linked (GlcNAc...)1 Publication
Disulfide bondi1359 ↔ 1404PROSITE-ProRule annotation

Post-translational modificationi

Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP11087.
PaxDbiP11087.
PRIDEiP11087.

PTM databases

PhosphoSiteiP11087.

Miscellaneous databases

PMAP-CutDBP11087.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP11087.
CleanExiMM_COL1A1.
ExpressionAtlasiP11087. baseline and differential.
GenevestigatoriP11087.

Interactioni

Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198831. 7 interactions.
IntActiP11087. 2 interactions.
MINTiMINT-4091294.
STRINGi10090.ENSMUSP00000001547.

Structurei

3D structure databases

ProteinModelPortaliP11087.
SMRiP11087. Positions 30-89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 8759VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1218 – 1453236Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 16716Nonhelical region (N-terminal)Add
BLAST
Regioni168 – 11811014Triple-helical regionAdd
BLAST
Regioni1182 – 120726Nonhelical region (C-terminal)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi734 – 7363Cell attachment siteSequence Analysis
Motifi1082 – 10843Cell attachment siteSequence Analysis

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00770000120467.
HOVERGENiHBG004933.
InParanoidiP11087.
KOiK06236.
OMAiKEKRHVW.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP11087.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

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: P11087-1) [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
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPEVCL
60 70 80 90 100
ICICHNGTAV CDDVQCNEEL DCPNPQRREG ECCAFCPEEY VSPNSEDVGV
110 120 130 140 150
EGPKGDPGPQ GPRGPVGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA
160 170 180 190 200
SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG PPGAPGPQGF QGPPGEPGEP
210 220 230 240 250
GGSGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG ARGLPGTAGL
260 270 280 290 300
PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
310 320 330 340 350
RPGPPGTAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAVGA KGEAGPQGAR
360 370 380 390 400
GSEGPQGVRG EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF
410 420 430 440 450
PGARGPSGPQ GPSGPPGPKG NSGEPGAPGN KGDTGAKGEP GATGVQGPPG
460 470 480 490 500
PAGEEGKRGA RGEPGPSGLP GPPGERGGPG SRGFPGADGV AGPKGPSGER
510 520 530 540 550
GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG KTGPPGPAGQ
560 570 580 590 600
DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGLP GPPGAVGPAG
610 620 630 640 650
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ
660 670 680 690 700
GVPGDLGAPG PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD
710 720 730 740 750
TGAPGAPGSQ GAPGLQGMPG ERGAAGLPGP KGDRGDAGPK GADGSPGKDG
760 770 780 790 800
ARGLTGPIGP PGPAGAPGDK GEAGPSGPPG PTGARGAPGD RGEAGPPGPA
810 820 830 840 850
GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG PIGNVGAPGP
860 870 880 890 900
KGPRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG
910 920 930 940 950
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV
960 970 980 990 1000
GLPGQRGERG FPGLPGPSGE PGKQGPSGSS GERGPPGPMG PPGLAGPPGE
1010 1020 1030 1040 1050
SGREGSPGAE GSPGRDGAPG AKGDRGETGP AGPPGAPGAP GAPGPVGPAG
1060 1070 1080 1090 1100
KNGDRGETGP AGPAGPIGPA GARGPAGPQG PRGDKGETGE QGDRGIKGHR
1110 1120 1130 1140 1150
GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG KDGLNGLPGP
1160 1170 1180 1190 1200
IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD
1210 1220 1230 1240 1250
GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD
1260 1270 1280 1290 1300
LKMCHSDWKS GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN
1310 1320 1330 1340 1350
WYISPNPKEK KHVWFGESMT DGFPFEYGSE GSDPADVAIQ LTFLRLMSTE
1360 1370 1380 1390 1400
ASQNITYHCK NSVAYMDQQT GNLKKALLLQ GSNEIELRGE GNSRFTYSTL
1410 1420 1430 1440 1450
VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD QEFGLDIGPA

CFV
Length:1,453
Mass (Da):138,032
Last modified:December 6, 2005 - v4
Checksum:i0B7F06BBB9A1D5EA
GO
Isoform 2 (identifier: P11087-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     803-1030: Missing.

Note: No experimental confirmation available.

Show »
Length:1,225
Mass (Da):117,820
Checksum:i5EBF34F79AD32E86
GO

Sequence cautioni

The sequence CAA38657.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811E → G in AAA88912. (PubMed:8535610)Curated
Sequence conflicti106 – 1061D → G in AAA88912. (PubMed:8535610)Curated
Sequence conflicti136 – 1361P → H in AAH59281. (PubMed:15489334)Curated
Sequence conflicti1202 – 12021G → D in AAA88912. (PubMed:8535610)Curated
Sequence conflicti1219 – 12191E → A in AAA88912. (PubMed:8535610)Curated
Sequence conflicti1222 – 12221T → A in AAA88912. (PubMed:8535610)Curated
Sequence conflicti1335 – 13351A → T in AAA88912. (PubMed:8535610)Curated
Sequence conflicti1399 – 14002TL → RV in AAA88912. (PubMed:8535610)Curated
Sequence conflicti1450 – 14501A → V in CAA29927. (PubMed:3340560)Curated
Sequence conflicti1450 – 14501A → V in CAA33904. (PubMed:3340560)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei803 – 1030228Missing in isoform 2. 1 PublicationVSP_016548Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08020 mRNA. Translation: AAA88912.1.
AL662790, AL606480 Genomic DNA. Translation: CAI25880.1.
AL606480, AL662790 Genomic DNA. Translation: CAI23970.1.
BC050014 mRNA. Translation: AAH50014.1.
BC059281 mRNA. Translation: AAH59281.1.
K01688 Genomic DNA. Translation: AAA37330.1.
S67530 Genomic DNA. Translation: AAB29424.1.
S67482 Genomic DNA. No translation available.
X54876 Genomic DNA. Translation: CAA38657.1. Sequence problems.
M14423 mRNA. Translation: AAA37333.1.
M17491 Genomic DNA. Translation: AAA37334.1.
K03036
, K03029, K03030, K03031, K03032, K03033, K03034, K03035 Genomic DNA. Translation: AAA37332.1.
X06753 Genomic DNA. Translation: CAA29927.1.
X15896 Genomic DNA. Translation: CAA33904.1.
X57981 Genomic DNA. Translation: CAA41046.1.
CCDSiCCDS25265.1. [P11087-1]
PIRiI49558.
S57243. S21626.
RefSeqiNP_031768.2. NM_007742.3. [P11087-1]
UniGeneiMm.277735.
Mm.458212.

Genome annotation databases

EnsembliENSMUST00000001547; ENSMUSP00000001547; ENSMUSG00000001506. [P11087-1]
GeneIDi12842.
KEGGimmu:12842.
UCSCiuc007kzn.1. mouse. [P11087-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08020 mRNA. Translation: AAA88912.1 .
AL662790 , AL606480 Genomic DNA. Translation: CAI25880.1 .
AL606480 , AL662790 Genomic DNA. Translation: CAI23970.1 .
BC050014 mRNA. Translation: AAH50014.1 .
BC059281 mRNA. Translation: AAH59281.1 .
K01688 Genomic DNA. Translation: AAA37330.1 .
S67530 Genomic DNA. Translation: AAB29424.1 .
S67482 Genomic DNA. No translation available.
X54876 Genomic DNA. Translation: CAA38657.1 . Sequence problems.
M14423 mRNA. Translation: AAA37333.1 .
M17491 Genomic DNA. Translation: AAA37334.1 .
K03036
, K03029 , K03030 , K03031 , K03032 , K03033 , K03034 , K03035 Genomic DNA. Translation: AAA37332.1 .
X06753 Genomic DNA. Translation: CAA29927.1 .
X15896 Genomic DNA. Translation: CAA33904.1 .
X57981 Genomic DNA. Translation: CAA41046.1 .
CCDSi CCDS25265.1. [P11087-1 ]
PIRi I49558.
S57243. S21626.
RefSeqi NP_031768.2. NM_007742.3. [P11087-1 ]
UniGenei Mm.277735.
Mm.458212.

3D structure databases

ProteinModelPortali P11087.
SMRi P11087. Positions 30-89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198831. 7 interactions.
IntActi P11087. 2 interactions.
MINTi MINT-4091294.
STRINGi 10090.ENSMUSP00000001547.

PTM databases

PhosphoSitei P11087.

Proteomic databases

MaxQBi P11087.
PaxDbi P11087.
PRIDEi P11087.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001547 ; ENSMUSP00000001547 ; ENSMUSG00000001506 . [P11087-1 ]
GeneIDi 12842.
KEGGi mmu:12842.
UCSCi uc007kzn.1. mouse. [P11087-1 ]

Organism-specific databases

CTDi 1277.
MGIi MGI:88467. Col1a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120467.
HOVERGENi HBG004933.
InParanoidi P11087.
KOi K06236.
OMAi KEKRHVW.
OrthoDBi EOG7TJ3HH.
PhylomeDBi P11087.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_196515. Crosslinking of collagen fibrils.
REACT_196581. Scavenging by Class A Receptors.
REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_196644. Syndecan interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_220092. GPVI-mediated activation cascade.
REACT_225107. Platelet Adhesion to exposed collagen.
REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

ChiTaRSi Col1a1. mouse.
NextBioi 282376.
PMAP-CutDB P11087.
PROi P11087.
SOURCEi Search...

Gene expression databases

Bgeei P11087.
CleanExi MM_COL1A1.
ExpressionAtlasi P11087. baseline and differential.
Genevestigatori P11087.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete cDNA coding sequence for the mouse pro alpha 1(I) chain of type I procollagen."
    Li S.W., Khillan J., Prockop D.J.
    Matrix Biol. 14:593-595(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: FVB/N.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORMS 1 AND 2).
    Strain: FVB/N.
    Tissue: Colon.
  4. "Insertion of retrovirus into the first intron of alpha1(I) collagen gene leads to embryonic lethal mutation in mice."
    Harbers K., Kuehn M., Delius H., Jaenisch R.
    Proc. Natl. Acad. Sci. U.S.A. 81:1504-1508(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
  5. "Genomic sequence of mouse COL1A1 encoding the collagen propeptides."
    Fenton S.P., Lamande S.R., Hannagan M., Stacey A., Jaenisch R., Bateman J.F.
    Biochim. Biophys. Acta 1216:469-474(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 AND 1030-1453.
  6. "DNA methylation represses the murine alpha 1(I) collagen promoter by an indirect mechanism."
    Rhodes K., Rippe R.A., Umezawa A., Nehls M., Brenner D.A., Breindl M.
    Mol. Cell. Biol. 14:5950-5960(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-942.
    Strain: C57BL/6.
    Tissue: Liver.
  7. "Nucleotide sequence of a cDNA clone for mouse pro alpha 1(I) collagen protein."
    French B.T., Lee W.-H., Maul G.G.
    Gene 39:311-312(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 518-1128 (ISOFORM 1).
  8. "DNA sequence analysis of a mouse pro alpha 1 (I) procollagen gene: evidence for a mouse B1 element within the gene."
    Monson J.M., Friedman J., McCarthy B.J.
    Mol. Cell. Biol. 2:1362-1371(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 735-1130.
  9. "Identification of a Balb/c mouse pro alpha 1(I) procollagen gene: evidence for insertions or deletions in gene coding sequences."
    Monson J.M., McCarthy B.J.
    DNA 1:59-69(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 735-878 AND 1005-1058.
  10. "Two mRNAs of mouse pro alpha 1(I) collagen gene differ in the size of the 3'-untranslated region."
    Mooslehner K., Harbers K.
    Nucleic Acids Res. 16:773-773(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1442-1453.
  11. "Specific hybridization probes for mouse type I, II, III and IX collagen mRNAs."
    Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.
    Biochim. Biophys. Acta 1089:241-243(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1442-1453.
  12. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1354.
    Strain: C57BL/6.
    Tissue: Plasma.

Entry informationi

Entry nameiCO1A1_MOUSE
AccessioniPrimary (citable) accession number: P11087
Secondary accession number(s): Q53WT0
, Q60635, Q61367, Q61427, Q63919, Q6PCL3, Q810J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 6, 2005
Last modified: November 26, 2014
This is version 152 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

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