UniProt Accession

 ST14_HUMAN; Q9Y5Y6; Q9BS01; Q9H3S0; Q9HB36; Q9HCA3 

Genbank Protein ID

 AF118224; AF133086; AB030036; AF057145; BC005826; BC030532; AF283256 

Genbank Nucleotide ID

 AAD42765.2; AAF00109.1; BAB20376.1; AAG15395.1; AAH05826.2; AAH30532.1; AAG13949.1 

Protein Name

 Suppressor of tumorigenicity 14 protein 

Protein Synonyms/Alias

 Matriptase; Membrane-type serine protease 1; MT-SP1; Prostamin; Serine protease 14; Serine protease TADG-15; Tumor-associated differentially-expressed gene 15 protein 

Gene Name

 ST14 

Gene Synonyms/Alias

 PRSS14; SNC19; TADG15 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
21	KDFGAGLKYNSRHEK	ubiquitination	[1, 2]
28	KYNSRHEKVNGLEEG	ubiquitination	[1, 2]
45	FLPVNNVKKVEKHGP	ubiquitination	[1, 2]
189	PPRARSLKSFVVTSV	ubiquitination	[2]
204	VAFPTDSKTVQRTQD	ubiquitination	[1, 2, 3]
424	VVTSNSNKITVRFHS	ubiquitination	[3]
497	AGHQFTCKNKFCKPL	ubiquitination	[3]
540	SNGKCLSKSQQCNGK	ubiquitination	[3]
561	SDEASCPKVNVVTCT	ubiquitination	[3]
582	LNGLCLSKGNPECDG	ubiquitination	[3]
590	GNPECDGKEDCSDGS	ubiquitination	[3]
600	CSDGSDEKDCDCGLR	ubiquitination	[3]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional Description

 Degrades extracellular matrix. Proposed to play a role in breast cancer invasion and metastasis. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site. 

Sequence Annotation

 DOMAIN 214 334 CUB 1.
 DOMAIN 340 447 CUB 2.
 DOMAIN 452 487 LDL-receptor class A 1.
 DOMAIN 487 524 LDL-receptor class A 2.
 DOMAIN 524 560 LDL-receptor class A 3.
 DOMAIN 566 603 LDL-receptor class A 4.
 DOMAIN 615 854 Peptidase S1.
 ACT_SITE 656 656 Charge relay system.
 ACT_SITE 711 711 Charge relay system.
 ACT_SITE 805 805 Charge relay system.
 CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
 CARBOHYD 302 302 N-linked (GlcNAc...) (Potential).
 CARBOHYD 485 485 N-linked (GlcNAc...) (Potential).
 CARBOHYD 772 772 N-linked (GlcNAc...) (Potential).
 DISULFID 214 244 By similarity.
 DISULFID 340 366 By similarity.
 DISULFID 397 410 By similarity.
 DISULFID 453 464 By similarity.
 DISULFID 459 477 By similarity.
 DISULFID 471 486 By similarity.
 DISULFID 488 501 By similarity.
 DISULFID 496 514 By similarity.
 DISULFID 508 523 By similarity.
 DISULFID 525 537 By similarity.
 DISULFID 532 550 By similarity.
 DISULFID 544 559 By similarity.
 DISULFID 567 579 By similarity.
 DISULFID 574 593 By similarity.
 DISULFID 587 602 By similarity.
 DISULFID 641 657
 DISULFID 776 790
 DISULFID 801 830  

Keyword

 3D-structure; Complete proteome; Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Hypotrichosis; Ichthyosis; Membrane; Polymorphism; Protease; Reference proteome; Repeat; Serine protease; Signal-anchor; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 855 AA 

Protein Sequence

Gene Ontology

 GO:0005576; C:extracellular region; IEA:Compara.
 GO:0019897; C:extrinsic to plasma membrane; IEA:Compara.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
 GO:0006508; P:proteolysis; IDA:UniProtKB. 

Interpro

 IPR000859; CUB_dom.
 IPR023415; LDLR_class-A_CS.
 IPR002172; LDrepeatLR_classA_rpt.
 IPR001254; Peptidase_S1.
 IPR018114; Peptidase_S1_AS.
 IPR017051; Peptidase_S1A_matripase.
 IPR000082; SEA_dom.
 IPR009003; Trypsin-like_Pept_dom. 

Pfam

 PF00431; CUB
 PF00057; Ldl_recept_a
 PF01390; SEA
 PF00089; Trypsin 

SMART

 SM00042; CUB
 SM00192; LDLa
 SM00020; Tryp_SPc 

PROSITE

 PS01180; CUB
 PS01209; LDLRA_1
 PS50068; LDLRA_2
 PS50240; TRYPSIN_DOM
 PS00134; TRYPSIN_HIS
 PS00135; TRYPSIN_SER 

PRINTS