SEPR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SEPR_HUMAN
• UniProt AC: Q12884
• Protein Name: Prolyl endopeptidase FAP {ECO:0000305}
• Gene Name: FAP {ECO:0000312|HGNC:HGNC:3590}
• Organism: Homo sapiens (Human).
• Sequence Length: 760
• Subcellular Localization: Prolyl endopeptidase FAP: Cell surface . Cell membrane ; Single-pass type II membrane protein . Cell projection, lamellipodium membrane ; Single-pass type II membrane protein . Cell projection, invadopodium membrane ; Single-pass type II membrane protein
• Protein Description: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. [PubMed: 14751930]
• Protein Sequence: MKTWVKIVFGVATSAVLALLVMCIVLRPSRVHNSEENTMRALTLKDILNGTFSYKTFFPNWISGQEYLHQSADNNIVLYNIETGQSYTILSNRTMKSVNASNYGLSPDRQFVYLESDYSKLWRYSYTATYYIYDLSNGEFVRGNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPGDPPFQITFNGRENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTDIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDTTYPAYVGPQEVPVPAMIASSDYYFSWLTWVTDERVCLQWLKRVQNVSVLSICDFREDWQTWDCPKTQEHIEESRTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEEYPGRRNIYRISIGSYPPSKKCVTCHLRKERCQYYTASFSDYAKYYALVCYGPGIPISTLHDGRTDQEIKILEENKELENALKNIQLPKEEIKKLEVDEITLWYKMILPPQFDRSKKYPLLIQVYGGPCSQSVRSVFAVNWISYLASKEGMVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASVYTERFMGLPTKDDNLEHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTNHLYTHMTHFLKQCFSLSD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Phosphorylation	MCIVLRPSRVHNSEE HHHHHCHHHCCCCCC	40.27	24719451
49	N-linked_Glycosylation	LTLKDILNGTFSYKT ECHHHHHCCCCEECC	48.03	15809306
92	N-linked_Glycosylation	QSYTILSNRTMKSVN CEEEEEECCEECCCC	39.74	15809306
99	N-linked_Glycosylation	NRTMKSVNASNYGLS CCEECCCCHHHCCCC	44.75	16335952
227	N-linked_Glycosylation	FLAYAEFNDTDIPVI EEEEEEECCCCCCEE	42.66	16335952
254	Acetylation	TINIPYPKAGAKNPV EEECCCCCCCCCCCE	54.32	7409397
254	Ubiquitination	TINIPYPKAGAKNPV EEECCCCCCCCCCCE	54.32	-
314	N-linked_Glycosylation	QWLKRVQNVSVLSIC HHHHHCCCEEEEEEE	25.77	15809306
379	Phosphorylation	DGYKHIHYIKDTVEN CCCEEEEEEHHHHHC	14.73	23879269
383	Phosphorylation	HIHYIKDTVENAIQI EEEEEHHHHHCCEEH	25.39	23879269
431	Phosphorylation	IYRISIGSYPPSKKC EEEEECCCCCCCCCE	32.56	23403867
432	Phosphorylation	YRISIGSYPPSKKCV EEEECCCCCCCCCEE	17.60	23403867
551	Phosphorylation	PCSQSVRSVFAVNWI CCCHHHHHHHHHHHH	21.30	-
595	Phosphorylation	VYRKLGVYEVEDQIT HHHHHCCEEEHHHHH	16.68	-
602	Phosphorylation	YEVEDQITAVRKFIE EEEHHHHHHHHHHHH	17.29	-
677	Phosphorylation	KDDNLEHYKNSTVMA CCCCHHHHCCCCHHH	11.50	21214269
679	N-linked_Glycosylation	DNLEHYKNSTVMARA CCHHHHCCCCHHHHH	35.43	UniProtKB CARBOHYD
680	Phosphorylation	NLEHYKNSTVMARAE CHHHHCCCCHHHHHH	20.44	21214269
681	Phosphorylation	LEHYKNSTVMARAEY HHHHCCCCHHHHHHH	24.56	21214269

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SEPR_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SEPR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SEPR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3K1_HUMAN	SH3KBP1	physical	22939629
COR1C_HUMAN	CORO1C	physical	26344197
ADA_HUMAN	ADA	physical	26209915
CAV1_HUMAN	CAV1	physical	26209915
DPP4_HUMAN	DPP4	physical	26209915
ERLN2_HUMAN	ERLIN2	physical	26209915
STOM_HUMAN	STOM	physical	26209915
PHB_HUMAN	PHB	physical	26209915
PHB2_HUMAN	PHB2	physical	26209915
MSRB1_HUMAN	MSRB1	physical	26209915
RBM4_HUMAN	RBM4	physical	26209915
THY1_HUMAN	THY1	physical	26209915
TM109_HUMAN	TMEM109	physical	26209915

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structural and kinetic analysis of the substrate specificity of humanfibroblast activation protein alpha.";
Aertgeerts K., Levin I., Shi L., Snell G.P., Jennings A., Prasad G.S.,Zhang Y., Kraus M.L., Salakian S., Sridhar V., Wijnands R.,Tennant M.G.;
J. Biol. Chem. 280:19441-19444(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 39-757, SUBUNIT, DISULFIDEBONDS, ACTIVE SITE, AND GLYCOSYLATION AT ASN-49; ASN-92; ASN-227 ANDASN-314.
PubMed: 15809306

"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99 AND ASN-227, AND MASSSPECTROMETRY.
PubMed: 16335952