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Q16610

- ECM1_HUMAN

UniProt

Q16610 - ECM1_HUMAN

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Protein

Extracellular matrix protein 1

Gene
ECM1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity.3 Publications

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. laminin binding Source: UniProtKB
  3. protease binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein C-terminus binding Source: UniProtKB
  6. signal transducer activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. biomineral tissue development Source: UniProtKB-KW
  3. inflammatory response Source: Ensembl
  4. negative regulation of bone mineralization Source: UniProtKB
  5. negative regulation of cytokine-mediated signaling pathway Source: Ensembl
  6. negative regulation of peptidase activity Source: UniProtKB
  7. ossification Source: UniProtKB-KW
  8. positive regulation of angiogenesis Source: UniProtKB
  9. positive regulation of endothelial cell proliferation Source: UniProtKB
  10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  11. regulation of T cell migration Source: Ensembl
  12. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  13. regulation of type 2 immune response Source: Ensembl
  14. signal transduction Source: GOC
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Biomineralization, Mineral balance, Osteogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular matrix protein 1
Alternative name(s):
Secretory component p85
Gene namesi
Name:ECM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3153. ECM1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: UniProtKB
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: UniProt
  4. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Lipoid proteinosis (LiP) [MIM:247100]: Rare autosomal recessive disorder characterized by generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness. Histologically, there is widespread deposition of hyaline material and disruption/reduplication of basement membrane.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671F → I in LiP. 1 Publication
VAR_018691

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi247100. phenotype.
Orphaneti530. Lipoid proteinosis.
PharmGKBiPA27598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarityAdd
BLAST
Chaini20 – 540521Extracellular matrix protein 1PRO_0000021146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi444 – 4441N-linked (GlcNAc...) (complex)2 Publications
Glycosylationi530 – 5301N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ16610.
PaxDbiQ16610.
PRIDEiQ16610.

PTM databases

PhosphoSiteiQ16610.

Expressioni

Tissue specificityi

Expressed in breast cancer tissues. Little or no expression observed in normal breast tissues. Expressed in skin; wide expression is observed throughout the dermis with minimal expression in the epidermis.2 Publications

Gene expression databases

ArrayExpressiQ16610.
BgeeiQ16610.
CleanExiHS_ECM1.
GenevestigatoriQ16610.

Organism-specific databases

HPAiHPA027241.

Interactioni

Subunit structurei

Interacts (via C-terminus) with HSPG2 (via C-terminus). Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9.3 Publications

Protein-protein interaction databases

BioGridi108222. 8 interactions.
IntActiQ16610. 10 interactions.
MINTiMINT-2858262.

Structurei

3D structure databases

ProteinModelPortaliQ16610.
SMRiQ16610. Positions 194-279, 334-361, 442-500.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati150 – 2791301Add
BLAST
Repeati283 – 4051232Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 4052562 X approximate repeatsAdd
BLAST

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG45869.
HOVERGENiHBG005561.
OMAiCCHYPPS.
OrthoDBiEOG7KWSHX.
PhylomeDBiQ16610.
TreeFamiTF330786.

Family and domain databases

InterProiIPR008605. ECM1.
IPR020858. Serum_albumin-like.
[Graphical view]
PfamiPF05782. ECM1. 1 hit.
[Graphical view]
SUPFAMiSSF48552. SSF48552. 2 hits.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16610-1) [UniParc]FASTAAdd to Basket

Also known as: 1a

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

MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP    50
LSRSLPMDHP DSSQHGPPFE GQSQVQPPPS QEATPLQQEK LLPAQLPAEK 100
EVGPPLPQEA VPLQKELPSL QHPNEQKEGT PAPFGDQSHP EPESWNAAQH 150
CQQDRSQGGW GHRLDGFPPG RPSPDNLNQI CLPNRQHVVY GPWNLPQSSY 200
SHLTRQGETL NFLEIGYSRC CHCRSHTNRL ECAKLVWEEA MSRFCEAEFS 250
VKTRPHWCCT RQGEARFSCF QEEAPQPHYQ LRACPSHQPD ISSGLELPFP 300
PGVPTLDNIK NICHLRRFRS VPRNLPATDP LQRELLALIQ LEREFQRCCR 350
QGNNHTCTWK AWEDTLDKYC DREYAVKTHH HLCCRHPPSP TRDECFARRA 400
PYPNYDRDIL TIDIGRVTPN LMGHLCGNQR VLTKHKHIPG LIHNMTARCC 450
DLPFPEQACC AEEEKLTFIN DLCGPRRNIW RDPALCCYLS PGDEQVNCFN 500
INYLRNVALV SGDTENAKGQ GEQGSTGGTN ISSTSEPKEE 540
Length:540
Mass (Da):60,674
Last modified:June 7, 2004 - v2
Checksum:iEA575895CDE068BE
GO
Isoform 2 (identifier: Q16610-2) [UniParc]FASTAAdd to Basket

Also known as: 1b

The sequence of this isoform differs from the canonical sequence as follows:
     237-361: Missing.

Show »
Length:415
Mass (Da):46,099
Checksum:iE6878AE9DEF1D5AC
GO
Isoform 3 (identifier: Q16610-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.
     72-81: QSQVQPPPSQ → MALPLRDRVK
     237-241: WEEAM → VRLGS
     242-540: Missing.

Show »
Length:170
Mass (Da):19,069
Checksum:i4C3B05692F1D1C8C
GO
Isoform 4 (identifier: Q16610-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: Q → GKEGRGPRPHSQPWLGERVGCSHIPPSI

Note: May be due to intron retention.

Show »
Length:567
Mass (Da):63,563
Checksum:iFBCFB0E51CE13735
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti130 – 1301T → M.3 Publications
Corresponds to variant rs3737240 [ dbSNP | Ensembl ].
VAR_018690
Natural varianti167 – 1671F → I in LiP. 1 Publication
VAR_018691
Natural varianti415 – 4151G → S.4 Publications
Corresponds to variant rs13294 [ dbSNP | Ensembl ].
VAR_014761
Natural varianti528 – 5281G → R.
Corresponds to variant rs1050901 [ dbSNP | Ensembl ].
VAR_014762
Natural varianti535 – 5351S → F.
Corresponds to variant rs1050904 [ dbSNP | Ensembl ].
VAR_014763

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171Missing in isoform 3. VSP_036411Add
BLAST
Alternative sequencei72 – 8110QSQVQPPPSQ → MALPLRDRVK in isoform 3. VSP_036412
Alternative sequencei74 – 741Q → GKEGRGPRPHSQPWLGERVG CSHIPPSI in isoform 4. VSP_036413
Alternative sequencei237 – 361125Missing in isoform 2. VSP_036414Add
BLAST
Alternative sequencei237 – 2415WEEAM → VRLGS in isoform 3. VSP_036415
Alternative sequencei242 – 540299Missing in isoform 3. VSP_036416Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 847Missing in BAG63622. 1 Publication
Sequence conflicti520 – 5201Q → R in BAF85124. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U68186 mRNA. Translation: AAB88081.1.
U68187 mRNA. Translation: AAB88082.1.
U65932 mRNA. Translation: AAB05933.1.
U65938
, U65933, U65934, U65935, U65936, U65937 Genomic DNA. Translation: AAB05934.1.
AK097046 mRNA. Translation: BAG53412.1.
AK292435 mRNA. Translation: BAF85124.1.
AK301369 mRNA. Translation: BAG62911.1.
AK302279 mRNA. Translation: BAG63622.1.
AL356356 Genomic DNA. Translation: CAI15491.1.
AL356356 Genomic DNA. Translation: CAI15492.1.
AL356356 Genomic DNA. Translation: CAI15493.1.
CH471121 Genomic DNA. Translation: EAW53544.1.
CH471121 Genomic DNA. Translation: EAW53545.1.
CH471121 Genomic DNA. Translation: EAW53546.1.
BC023505 mRNA. Translation: AAH23505.1.
CCDSiCCDS55632.1. [Q16610-4]
CCDS953.1. [Q16610-1]
CCDS954.1. [Q16610-2]
RefSeqiNP_001189787.1. NM_001202858.1. [Q16610-4]
NP_004416.2. NM_004425.3. [Q16610-1]
NP_073155.2. NM_022664.2. [Q16610-2]
UniGeneiHs.81071.

Genome annotation databases

EnsembliENST00000346569; ENSP00000271630; ENSG00000143369. [Q16610-2]
ENST00000369047; ENSP00000358043; ENSG00000143369. [Q16610-1]
ENST00000369049; ENSP00000358045; ENSG00000143369. [Q16610-4]
GeneIDi1893.
KEGGihsa:1893.
UCSCiuc001eus.3. human. [Q16610-1]
uc001eut.3. human. [Q16610-2]
uc001euv.3. human. [Q16610-4]
uc010pce.2. human. [Q16610-3]

Polymorphism databases

DMDMi48429255.

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
U68186 mRNA. Translation: AAB88081.1 .
U68187 mRNA. Translation: AAB88082.1 .
U65932 mRNA. Translation: AAB05933.1 .
U65938
, U65933 , U65934 , U65935 , U65936 , U65937 Genomic DNA. Translation: AAB05934.1 .
AK097046 mRNA. Translation: BAG53412.1 .
AK292435 mRNA. Translation: BAF85124.1 .
AK301369 mRNA. Translation: BAG62911.1 .
AK302279 mRNA. Translation: BAG63622.1 .
AL356356 Genomic DNA. Translation: CAI15491.1 .
AL356356 Genomic DNA. Translation: CAI15492.1 .
AL356356 Genomic DNA. Translation: CAI15493.1 .
CH471121 Genomic DNA. Translation: EAW53544.1 .
CH471121 Genomic DNA. Translation: EAW53545.1 .
CH471121 Genomic DNA. Translation: EAW53546.1 .
BC023505 mRNA. Translation: AAH23505.1 .
CCDSi CCDS55632.1. [Q16610-4 ]
CCDS953.1. [Q16610-1 ]
CCDS954.1. [Q16610-2 ]
RefSeqi NP_001189787.1. NM_001202858.1. [Q16610-4 ]
NP_004416.2. NM_004425.3. [Q16610-1 ]
NP_073155.2. NM_022664.2. [Q16610-2 ]
UniGenei Hs.81071.

3D structure databases

ProteinModelPortali Q16610.
SMRi Q16610. Positions 194-279, 334-361, 442-500.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108222. 8 interactions.
IntActi Q16610. 10 interactions.
MINTi MINT-2858262.

PTM databases

PhosphoSitei Q16610.

Polymorphism databases

DMDMi 48429255.

Proteomic databases

MaxQBi Q16610.
PaxDbi Q16610.
PRIDEi Q16610.

Protocols and materials databases

DNASUi 1893.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000346569 ; ENSP00000271630 ; ENSG00000143369 . [Q16610-2 ]
ENST00000369047 ; ENSP00000358043 ; ENSG00000143369 . [Q16610-1 ]
ENST00000369049 ; ENSP00000358045 ; ENSG00000143369 . [Q16610-4 ]
GeneIDi 1893.
KEGGi hsa:1893.
UCSCi uc001eus.3. human. [Q16610-1 ]
uc001eut.3. human. [Q16610-2 ]
uc001euv.3. human. [Q16610-4 ]
uc010pce.2. human. [Q16610-3 ]

Organism-specific databases

CTDi 1893.
GeneCardsi GC01P150480.
HGNCi HGNC:3153. ECM1.
HPAi HPA027241.
MIMi 247100. phenotype.
602201. gene.
neXtProti NX_Q16610.
Orphaneti 530. Lipoid proteinosis.
PharmGKBi PA27598.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45869.
HOVERGENi HBG005561.
OMAi CCHYPPS.
OrthoDBi EOG7KWSHX.
PhylomeDBi Q16610.
TreeFami TF330786.

Miscellaneous databases

ChiTaRSi ECM1. human.
GeneWikii ECM1.
GenomeRNAii 1893.
NextBioi 7719.
PROi Q16610.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16610.
Bgeei Q16610.
CleanExi HS_ECM1.
Genevestigatori Q16610.

Family and domain databases

InterProi IPR008605. ECM1.
IPR020858. Serum_albumin-like.
[Graphical view ]
Pfami PF05782. ECM1. 1 hit.
[Graphical view ]
SUPFAMi SSF48552. SSF48552. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human extracellular matrix gene 1 (ECM1): genomic structure, cDNA cloning, expression pattern, and chromosomal localization."
    Smits P., Ni J., Feng P., Wauters J., van Hul W., Boutaibi M.E., Dillon P.J., Merregaert J.
    Genomics 45:487-495(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT SER-415.
  2. "Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21."
    Johnson M.R., Wilkin D.J., Vos H.L., Ortiz de Luna R.I., Dehejia A.M., Polymeropoulos M.H., Francomano C.A.
    Matrix Biol. 16:289-292(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), VARIANTS MET-130 AND SER-415.
    Tissue: Synovial cell and Testis.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANTS MET-130 AND SER-415.
    Tissue: Skin.
  7. "Recombinant human extracellular matrix protein 1 inhibits alkaline phosphatase activity and mineralization of mouse embryonic metatarsals in vitro."
    Deckers M.M.L., Smits P., Karperien M., Ni J., Tylzanowski P., Feng P., Parmelee D., Zhang J., Bouffard E., Gentz R., Loewik C.W.G.M., Merregaert J.
    Bone 28:14-20(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BONE FORMATION.
  8. "Extracellular matrix protein 1 (ECM1) has angiogenic properties and is expressed by breast tumor cells."
    Han Z., Ni J., Smits P., Underhill C.B., Xie B., Chen Y., Liu N., Tylzanowski P., Parmelee D., Feng P., Ding I., Gao F., Gentz R., Huylebroeck D., Merregaert J., Zhang L.
    FASEB J. 15:988-994(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS, TISSUE SPECIFICITY.
  9. Cited for: INVOLVEMENT IN LIPOID PROTEINOSIS.
  10. "Perlecan protein core interacts with extracellular matrix protein 1 (ECM1), a glycoprotein involved in bone formation and angiogenesis."
    Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V.
    J. Biol. Chem. 278:17491-17499(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPG2, TISSUE SPECIFICITY.
  11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-444.
    Tissue: Plasma.
  12. "Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high-affinity protein/protein interactions."
    Fujimoto N., Terlizzi J., Aho S., Brittingham R., Fertala A., Oyama N., McGrath J.A., Uitto J.
    Exp. Dermatol. 15:300-307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MMP9, FUNCTION.
  13. "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
    Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
    Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EFEMP1 AND LAMB3.
  14. Cited for: GLYCOSYLATION AT ASN-444.
  15. Cited for: VARIANT LIP ILE-167, VARIANTS MET-130 AND SER-415.

Entry informationi

Entry nameiECM1_HUMAN
AccessioniPrimary (citable) accession number: Q16610
Secondary accession number(s): A8K8S0
, B4DW49, B4DY60, O43266, Q5T5G4, Q5T5G5, Q5T5G6, Q8IZ60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 123 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, 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

External Data

Dasty 3

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