KAIN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KAIN_HUMAN
• UniProt AC: P29622
• Protein Name: Kallistatin
• Gene Name: SERPINA4
• Organism: Homo sapiens (Human).
• Sequence Length: 427
• Subcellular Localization: Secreted.
• Protein Description: Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein..
• Protein Sequence: MHLIDYLLLLLVGLLALSHGQLHVEHDGESCSNSSHQQILETGEGSPSLKIAPANADFAFRFYYLIASETPGKNIFFSPLSISAAYAMLSLGACSHSRSQILEGLGFNLTELSESDVHRGFQHLLHTLNLPGHGLETRVGSALFLSHNLKFLAKFLNDTMAVYEAKLFHTNFYDTVGTIQLINDHVKKETRGKIVDLVSELKKDVLMVLVNYIYFKALWEKPFISSRTTPKDFYVDENTTVRVPMMLQDQEHHWYLHDRYLPCSVLRMDYKGDATVFFILPNQGKMREIEEVLTPEMLMRWNNLLRKRNFYKKLELHLPKFSISGSYVLDQILPRLGFTDLFSKWADLSGITKQQKLEASKSFHKATLDVDEAGTEAAAATSFAIKFFSAQTNRHILRFNRPFLVVIFSTSTQSVLFLGKVVDPTKP

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
30	Phosphorylation	HVEHDGESCSNSSHQ EECCCCCCCCCCCCH	28.51	27130503
32	Phosphorylation	EHDGESCSNSSHQQI CCCCCCCCCCCCHHH	49.37	27130503
33	N-linked_Glycosylation	HDGESCSNSSHQQIL CCCCCCCCCCCHHHH	52.43	UniProtKB CARBOHYD
34	Phosphorylation	DGESCSNSSHQQILE CCCCCCCCCCHHHHH	16.95	27130503
35	Phosphorylation	GESCSNSSHQQILET CCCCCCCCCHHHHHC	29.57	27130503
63	Phosphorylation	ADFAFRFYYLIASET CCEEEEEHHHHHCCC	7.97	-
64	Phosphorylation	DFAFRFYYLIASETP CEEEEEHHHHHCCCC	6.74	-
68	Phosphorylation	RFYYLIASETPGKNI EEHHHHHCCCCCCCC	34.70	-
108	N-linked_Glycosylation	ILEGLGFNLTELSES HHHHCCCCCCCCCHH	44.23	16335952
145	N-linked_Glycosylation	RVGSALFLSHNLKFL CCCHHHHHHHCHHHH	5.46	16335952
145	N-linked_Glycosylation	RVGSALFLSHNLKFL CCCHHHHHHHCHHHH	5.46	16335952
157	N-linked_Glycosylation	KFLAKFLNDTMAVYE HHHHHHHHHHHHHHH	45.93	12754519
194	N-linked_Glycosylation	KKETRGKIVDLVSEL CHHHHCCHHHHHHHH	3.03	12754519
194	N-linked_Glycosylation	KKETRGKIVDLVSEL CHHHHCCHHHHHHHH	3.03	12754519
225	Phosphorylation	LWEKPFISSRTTPKD HHCCCCCCCCCCCCC	17.72	29083192
226	Phosphorylation	WEKPFISSRTTPKDF HCCCCCCCCCCCCCE	28.91	29083192
228	Phosphorylation	KPFISSRTTPKDFYV CCCCCCCCCCCCEEE	49.77	29083192
229	Phosphorylation	PFISSRTTPKDFYVD CCCCCCCCCCCEEEC	27.51	29083192
238	N-linked_Glycosylation	KDFYVDENTTVRVPM CCEEECCCCEEEEEE	36.26	19139490
275	N-linked_Glycosylation	MDYKGDATVFFILPN EEECCCEEEEEECCC	23.68	16335952
275	N-linked_Glycosylation	MDYKGDATVFFILPN EEECCCEEEEEECCC	23.68	16335952
326	Phosphorylation	PKFSISGSYVLDQIL CCCEEECHHHHHHHH	12.79	-
343	Phosphorylation	LGFTDLFSKWADLSG CCCHHHHHHHHCCCC	34.29	24719451
360	Phosphorylation	KQQKLEASKSFHKAT HHHHHHHCHHHHHHE	21.32	26437602

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KAIN_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 KAIN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FKB14_HUMAN	FKBP14	physical	26186194
FDFT_HUMAN	FDFT1	physical	26186194
FKB14_HUMAN	FKBP14	physical	28514442

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

"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-108; ASN-157 AND ASN-238,AND MASS SPECTROMETRY.
PubMed: 16335952

"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-157.
PubMed: 12754519