SPIT1_HUMAN - dbPTM
SPIT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPIT1_HUMAN
UniProt AC O43278
Protein Name Kunitz-type protease inhibitor 1
Gene Name SPINT1
Organism Homo sapiens (Human).
Sequence Length 529
Subcellular Localization Secreted.
Protein Description Inhibitor of HGF activator. Also acts as an inhibitor of matriptase (ST14)..
Protein Sequence MAPARTMARARLAPAGIPAVALWLLCTLGLQGTQAGPPPAPPGLPAGADCLNSFTAGVPGFVLDTNASVSNGATFLESPTVRRGWDCVRACCTTQNCNLALVELQPDRGEDAIAACFLINCLYEQNFVCKFAPREGFINYLTREVYRSYRQLRTQGFGGSGIPKAWAGIDLKVQPQEPLVLKDVENTDWRLLRGDTDVRVERKDPNQVELWGLKEGTYLFQLTVTSSDHPEDTANVTVTVLSTKQTEDYCLASNKVGRCRGSFPRWYYDPTEQICKSFVYGGCLGNKNNYLREEECILACRGVQGGPLRGSSGAQATFPQGPSMERRHPVCSGTCQPTQFRCSNGCCIDSFLECDDTPNCPDASDEAACEKYTSGFDELQRIHFPSDKGHCVDLPDTGLCKESIPRWYYNPFSEHCARFTYGGCYGNKNNFEEEQQCLESCRGISKKDVFGLRREIPIPSTGSVEMAVAVFLVICIVVVVAILGYCFFKNQRKDFHGHHHHPPPTPASSTVSTTEDTEHLVYNHTTRPL
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 Orthologous
Protein Cluster
66N-linked_GlycosylationPGFVLDTNASVSNGA
CCEEEECCCCCCCCC
29.86UniProtKB CARBOHYD
154PhosphorylationRSYRQLRTQGFGGSG
HHHHHHHHCCCCCCC
41.4522210691
160PhosphorylationRTQGFGGSGIPKAWA
HHCCCCCCCCCCCCC
33.6524719451
172 (in isoform 2)Ubiquitination-34.7721906983
172 (in isoform 1)Ubiquitination-34.7721906983
172UbiquitinationAWAGIDLKVQPQEPL
CCCCCCCEECCCCCE
34.7722817900
235N-linked_GlycosylationDHPEDTANVTVTVLS
CCCCCCCEEEEEEEE
31.89UniProtKB CARBOHYD
277PhosphorylationPTEQICKSFVYGGCL
CHHHHHHHHHHHCCC
18.6118669648
311PhosphorylationQGGPLRGSSGAQATF
CCCCCCCCCCCCCCC
21.1122210691
312PhosphorylationGGPLRGSSGAQATFP
CCCCCCCCCCCCCCC
40.7622210691
317O-linked_GlycosylationGSSGAQATFPQGPSM
CCCCCCCCCCCCCCC
24.62OGP
334O-linked_GlycosylationRHPVCSGTCQPTQFR
CCCCCCCCCCCCEEE
7.53OGP
373O-linked_GlycosylationEAACEKYTSGFDELQ
HHHHHHHHCCCHHHH
33.18OGP
403PhosphorylationDTGLCKESIPRWYYN
CCCCCCCCCCHHHCC
24.3224719451
505PhosphorylationHHHHPPPTPASSTVS
CCCCCCCCCCCCCCC
36.94-
508PhosphorylationHPPPTPASSTVSTTE
CCCCCCCCCCCCCCC
27.96-
510PhosphorylationPPTPASSTVSTTEDT
CCCCCCCCCCCCCCC
18.91-
512PhosphorylationTPASSTVSTTEDTEH
CCCCCCCCCCCCCCE
29.69-
514PhosphorylationASSTVSTTEDTEHLV
CCCCCCCCCCCCEEE
25.10-
522PhosphorylationEDTEHLVYNHTTRPL
CCCCEEEECCCCCCC
13.9527259358
523N-linked_GlycosylationDTEHLVYNHTTRPL-
CCCEEEECCCCCCC-
20.67UniProtKB CARBOHYD
526PhosphorylationHLVYNHTTRPL----
EEEECCCCCCC----
23.80-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SPIT1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPIT1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SPIT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SPIT1_HUMAN !!

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.
Regulatory Network of SPIT1_HUMAN

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Related Literatures of Post-Translational Modification

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