Q16610 (ECM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Extracellular matrix protein 1

Alternative name(s):
Secretory component p85

Gene names

Name:

ECM1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	540 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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 process	Angiogenesis Biomineralization Mineral balance Osteogenesis
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat Signal
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW biomineral tissue development Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: Compara 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: Compara 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 cascade 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: Compara regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara regulation of type 2 immune response Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	By similarity
	Chain	20 – 540	521	Extracellular matrix protein 1		PRO_0000021146
Regions
	Repeat	150 – 279	130	1
	Repeat	283 – 405	123	2
	Region	150 – 405	256	2 X approximate repeats
Amino acid modifications
	Glycosylation	354	1	N-linked (GlcNAc...) Potential
	Glycosylation	444	1	N-linked (GlcNAc...) Ref.11
	Glycosylation	530	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1 – 71	71	Missing in isoform 3.		VSP_036411
	Alternative sequence	72 – 81	10	QSQVQPPPSQ → MALPLRDRVK in isoform 3.		VSP_036412
	Alternative sequence	74	1	Q → GKEGRGPRPHSQPWLGERVG CSHIPPSI in isoform 4.		VSP_036413
	Alternative sequence	237 – 361	125	Missing in isoform 2.		VSP_036414
	Alternative sequence	237 – 241	5	WEEAM → VRLGS in isoform 3.		VSP_036415
	Alternative sequence	242 – 540	299	Missing in isoform 3.		VSP_036416
	Natural variant	130	1	T → M. Ref.3 Ref.6 Ref.14 Corresponds to variant rs3737240 [ dbSNP | Ensembl ].		VAR_018690
	Natural variant	167	1	F → I in LiP. Ref.14		VAR_018691
	Natural variant	415	1	G → S. Ref.1 Ref.3 Ref.6 Ref.14 Corresponds to variant rs13294 [ dbSNP | Ensembl ].		VAR_014761
	Natural variant	528	1	G → R. Corresponds to variant rs1050901 [ dbSNP | Ensembl ].		VAR_014762
	Natural variant	535	1	S → F. Corresponds to variant rs1050904 [ dbSNP | Ensembl ].		VAR_014763
Experimental info
	Sequence conflict	78 – 84	7	Missing in BAG63622. Ref.3
	Sequence conflict	520	1	Q → R in BAF85124. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (1a) [UniParc]. Last modified June 7, 2004. Version 2. Checksum: EA575895CDE068BE	FASTA	540	60,674
	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
	Isoform 2 (1b) [UniParc]. Checksum: E6878AE9DEF1D5AC	FASTA	415	46,099
	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 ECAKLVWEDT 250 260 270 280 290 300 LDKYCDREYA VKTHHHLCCR HPPSPTRDEC FARRAPYPNY DRDILTIDIG RVTPNLMGHL 310 320 330 340 350 360 CGNQRVLTKH KHIPGLIHNM TARCCDLPFP EQACCAEEEK LTFINDLCGP RRNIWRDPAL 370 380 390 400 410 CCYLSPGDEQ VNCFNINYLR NVALVSGDTE NAKGQGEQGS TGGTNISSTS EPKEE
	Isoform 3 [UniParc]. Checksum: 4C3B05692F1D1C8C	FASTA	170	19,069
	10 20 30 40 50 60 MALPLRDRVK EATPLQQEKL LPAQLPAEKE VGPPLPQEAV PLQKELPSLQ HPNEQKEGTP 70 80 90 100 110 120 APFGDQSHPE PESWNAAQHC QQDRSQGGWG HRLDGFPPGR PSPDNLNQIC LPNRQHVVYG 130 140 150 160 170 PWNLPQSSYS HLTRQGETLN FLEIGYSRCC HCRSHTNRLE CAKLVVRLGS
	Isoform 4 [UniParc]. Checksum: FBCFB0E51CE13735	FASTA	567	63,563
	10 20 30 40 50 60 MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP LSRSLPMDHP 70 80 90 100 110 120 DSSQHGPPFE GQSGKEGRGP RPHSQPWLGE RVGCSHIPPS IVQPPPSQEA TPLQQEKLLP 130 140 150 160 170 180 AQLPAEKEVG PPLPQEAVPL QKELPSLQHP NEQKEGTPAP FGDQSHPEPE SWNAAQHCQQ 190 200 210 220 230 240 DRSQGGWGHR LDGFPPGRPS PDNLNQICLP NRQHVVYGPW NLPQSSYSHL TRQGETLNFL 250 260 270 280 290 300 EIGYSRCCHC RSHTNRLECA KLVWEEAMSR FCEAEFSVKT RPHWCCTRQG EARFSCFQEE 310 320 330 340 350 360 APQPHYQLRA CPSHQPDISS GLELPFPPGV PTLDNIKNIC HLRRFRSVPR NLPATDPLQR 370 380 390 400 410 420 ELLALIQLER EFQRCCRQGN NHTCTWKAWE DTLDKYCDRE YAVKTHHHLC CRHPPSPTRD 430 440 450 460 470 480 ECFARRAPYP NYDRDILTID IGRVTPNLMG HLCGNQRVLT KHKHIPGLIH NMTARCCDLP 490 500 510 520 530 540 FPEQACCAEE EKLTFINDLC GPRRNIWRDP ALCCYLSPGD EQVNCFNINY LRNVALVSGD 550 560 TENAKGQGEQ GSTGGTNISS TSEPKEE

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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. , 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, MASS SPECTROMETRY. 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]	"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. , 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 , 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.
IPI	IPI00003351. IPI00006969. IPI00645849. IPI00909747.
RefSeq	NP_001189787.1. NM_001202858.1. NP_004416.2. NM_004425.3. NP_073155.2. NM_022664.2.
UniGene	Hs.81071.
3D structure databases
ProteinModelPortal	Q16610.
SMR	Q16610. Positions 343-400.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16610. 9 interactions.
MINT	MINT-2858262.
PTM databases
PhosphoSite	Q16610.
Polymorphism databases
DMDM	48429255.
Proteomic databases
PaxDb	Q16610.
PRIDE	Q16610.
Protocols and materials databases
DNASU	1893.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000346569; ENSP00000271630; ENSG00000143369. ENST00000369047; ENSP00000358043; ENSG00000143369. ENST00000369049; ENSP00000358045; ENSG00000143369.
GeneID	1893.
KEGG	hsa:1893.
UCSC	uc001eus.3. human. uc001eut.3. human. uc001euv.3. human. uc010pce.2. human.
Organism-specific databases
CTD	1893.
GeneCards	GC01P150480.
HGNC	HGNC:3153. ECM1.
HPA	HPA027241.
MIM	247100. phenotype. 602201. gene.
neXtProt	NX_Q16610.
Orphanet	530. Lipoid proteinosis.
PharmGKB	PA27598.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG45869.
HOVERGEN	HBG005561.
OMA	CCHYPPS.
PhylomeDB	Q16610.
Gene expression databases
ArrayExpress	Q16610.
Bgee	Q16610.
CleanEx	HS_ECM1.
Genevestigator	Q16610.
GermOnline	ENSG00000143369. Homo sapiens.
Family and domain databases
InterPro	IPR008605. ECM1. [Graphical view]
Pfam	PF05782. ECM1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ECM1. human.
GenomeRNAi	1893.
NextBio	7719.
SOURCE	Search...

Entry information

Entry name

ECM1_HUMAN

Accession

Primary (citable) accession number: Q16610
Secondary accession number(s): A8K8S0 , 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:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.