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Q16610 (ECM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular matrix protein 1
Alternative name(s):
Secretory component p85
Gene names
Name:ECM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity. Ref.7 Ref.8 Ref.12

Subunit structure

Interacts (via C-terminus) with HSPG2 (via C-terminus). Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9. Ref.10 Ref.12 Ref.13

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

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. Ref.8 Ref.10

Involvement in disease

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.

Ontologies

Keywords
   Biological processAngiogenesis
Biomineralization
Mineral balance
Osteogenesis
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

biomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone mineralization

Inferred from direct assay Ref.7. Source: UniProtKB

negative regulation of cytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidase activity

Inferred from direct assay Ref.12. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of angiogenesis

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of T cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of type 2 immune response

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from mutant phenotype PubMed 12761501. Source: GOC

   Cellular_componentextracellular matrix

Inferred from direct assay PubMed 20870722. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

proteinaceous extracellular matrix

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 20870722. Source: UniProtKB

laminin binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protease binding

Inferred from physical interaction Ref.12. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.10. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16610-1)

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.
Isoform 2 (identifier: Q16610-2)

Also known as: 1b;

The sequence of this isoform differs from the canonical sequence as follows:
     237-361: Missing.
Isoform 3 (identifier: Q16610-3)

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.
Isoform 4 (identifier: Q16610-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: Q → GKEGRGPRPHSQPWLGERVGCSHIPPSI
Note: May be due to intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 540521Extracellular matrix protein 1
PRO_0000021146

Regions

Repeat150 – 2791301
Repeat283 – 4051232
Region150 – 4052562 X approximate repeats

Amino acid modifications

Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) (complex) Ref.11 Ref.14
Glycosylation5301N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 7171Missing in isoform 3.
VSP_036411
Alternative sequence72 – 8110QSQVQPPPSQ → MALPLRDRVK in isoform 3.
VSP_036412
Alternative sequence741Q → GKEGRGPRPHSQPWLGERVG CSHIPPSI in isoform 4.
VSP_036413
Alternative sequence237 – 361125Missing in isoform 2.
VSP_036414
Alternative sequence237 – 2415WEEAM → VRLGS in isoform 3.
VSP_036415
Alternative sequence242 – 540299Missing in isoform 3.
VSP_036416
Natural variant1301T → M. Ref.3 Ref.6 Ref.15
Corresponds to variant rs3737240 [ dbSNP | Ensembl ].
VAR_018690
Natural variant1671F → I in LiP. Ref.15
VAR_018691
Natural variant4151G → S. Ref.1 Ref.3 Ref.6 Ref.15
Corresponds to variant rs13294 [ dbSNP | Ensembl ].
VAR_014761
Natural variant5281G → R.
Corresponds to variant rs1050901 [ dbSNP | Ensembl ].
VAR_014762
Natural variant5351S → F.
Corresponds to variant rs1050904 [ dbSNP | Ensembl ].
VAR_014763

Experimental info

Sequence conflict78 – 847Missing in BAG63622. Ref.3
Sequence conflict5201Q → R in BAF85124. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (1a) [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: EA575895CDE068BE

FASTA54060,674
        10         20         30         40         50         60 
MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP LSRSLPMDHP 

        70         80         90        100        110        120 
DSSQHGPPFE GQSQVQPPPS QEATPLQQEK LLPAQLPAEK EVGPPLPQEA VPLQKELPSL 

       130        140        150        160        170        180 
QHPNEQKEGT PAPFGDQSHP EPESWNAAQH CQQDRSQGGW GHRLDGFPPG RPSPDNLNQI 

       190        200        210        220        230        240 
CLPNRQHVVY GPWNLPQSSY SHLTRQGETL NFLEIGYSRC CHCRSHTNRL ECAKLVWEEA 

       250        260        270        280        290        300 
MSRFCEAEFS VKTRPHWCCT RQGEARFSCF QEEAPQPHYQ LRACPSHQPD ISSGLELPFP 

       310        320        330        340        350        360 
PGVPTLDNIK NICHLRRFRS VPRNLPATDP LQRELLALIQ LEREFQRCCR QGNNHTCTWK 

       370        380        390        400        410        420 
AWEDTLDKYC DREYAVKTHH HLCCRHPPSP TRDECFARRA PYPNYDRDIL TIDIGRVTPN 

       430        440        450        460        470        480 
LMGHLCGNQR VLTKHKHIPG LIHNMTARCC DLPFPEQACC AEEEKLTFIN DLCGPRRNIW 

       490        500        510        520        530        540 
RDPALCCYLS PGDEQVNCFN INYLRNVALV SGDTENAKGQ GEQGSTGGTN ISSTSEPKEE 

« Hide

Isoform 2 (1b) [UniParc].

Checksum: E6878AE9DEF1D5AC
Show »

FASTA41546,099
Isoform 3 [UniParc].

Checksum: 4C3B05692F1D1C8C
Show »

FASTA17019,069
Isoform 4 [UniParc].

Checksum: FBCFB0E51CE13735
Show »

FASTA56763,563

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Lipoid proteinosis maps to 1q21 and is caused by mutations in the extracellular matrix protein 1 gene (ECM1)."
Hamada T., McLean W.H.I., Ramsay M., Ashton G.H.S., Nanda A., Jenkins T., Edelstein I., South A.P., Bleck O., Wessagowit V., Mallipeddi R., Orchard G.E., Wan H., Dopping-Hepenstal P.J.C., Mellerio J.E., Whittock N.V., Munro C.S., van Steensel M.A.M. expand/collapse author list , Steijlen P.M., Ni J., Zhang L., Hashimoto T., Eady R.A.E., McGrath J.A.
Hum. Mol. Genet. 11:833-840(2002) [PubMed] [Europe PMC] [Abstract]
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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-444.
[15]"Extracellular matrix protein 1 gene (ECM1) mutations in lipoid proteinosis and genotype-phenotype correlation."
Hamada T., Wessagowit V., South A.P., Ashton G.H.S., Chan I., Oyama N., Siriwattana A., Jewhasuchin P., Charuwichitratana S., Thappa D.M., Lenane P., Krafchik B., Kulthanan K., Shimizu H., Kaya T.I., Erdal M.E., Paradisi M., Paller A.S. expand/collapse author list , Seishima M., Hashimoto T., McGrath J.A.
J. Invest. Dermatol. 120:345-350(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LIP ILE-167, VARIANTS MET-130 AND SER-415.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U68186 mRNA. Translation: AAB88081.1.
U68187 mRNA. Translation: AAB88082.1.
U65932 mRNA. Translation: AAB05933.1.
U65938 expand/collapse EMBL AC list , 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.
RefSeqNP_001189787.1. NM_001202858.1.
NP_004416.2. NM_004425.3.
NP_073155.2. NM_022664.2.
UniGeneHs.81071.

3D structure databases

ProteinModelPortalQ16610.
SMRQ16610. Positions 194-279, 334-361, 442-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108222. 8 interactions.
IntActQ16610. 10 interactions.
MINTMINT-2858262.

PTM databases

PhosphoSiteQ16610.

Polymorphism databases

DMDM48429255.

Proteomic databases

PaxDbQ16610.
PRIDEQ16610.

Protocols and materials databases

DNASU1893.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346569; ENSP00000271630; ENSG00000143369. [Q16610-2]
ENST00000369047; ENSP00000358043; ENSG00000143369. [Q16610-1]
ENST00000369049; ENSP00000358045; ENSG00000143369. [Q16610-4]
GeneID1893.
KEGGhsa:1893.
UCSCuc001eus.3. human. [Q16610-1]
uc001eut.3. human. [Q16610-2]
uc001euv.3. human. [Q16610-4]
uc010pce.2. human. [Q16610-3]

Organism-specific databases

CTD1893.
GeneCardsGC01P150480.
HGNCHGNC:3153. ECM1.
HPAHPA027241.
MIM247100. phenotype.
602201. gene.
neXtProtNX_Q16610.
Orphanet530. Lipoid proteinosis.
PharmGKBPA27598.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45869.
HOVERGENHBG005561.
OMACCHYPPS.
OrthoDBEOG7KWSHX.
PhylomeDBQ16610.
TreeFamTF330786.

Gene expression databases

ArrayExpressQ16610.
BgeeQ16610.
CleanExHS_ECM1.
GenevestigatorQ16610.

Family and domain databases

InterProIPR008605. ECM1.
IPR020858. Serum_albumin-like.
[Graphical view]
PfamPF05782. ECM1. 1 hit.
[Graphical view]
SUPFAMSSF48552. SSF48552. 2 hits.
ProtoNetSearch...

Other

ChiTaRSECM1. human.
GeneWikiECM1.
GenomeRNAi1893.
NextBio7719.
PROQ16610.
SOURCESearch...

Entry information

Entry nameECM1_HUMAN
AccessionPrimary (citable) accession number: Q16610
Secondary accession number(s): A8K8S0 expand/collapse secondary AC list , B4DW49, B4DY60, O43266, Q5T5G4, Q5T5G5, Q5T5G6, Q8IZ60
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM