PPIP2_HUMAN - dbPTM
PPIP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPIP2_HUMAN
UniProt AC Q9H939
Protein Name Proline-serine-threonine phosphatase-interacting protein 2
Gene Name PSTPIP2
Organism Homo sapiens (Human).
Sequence Length 334
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein.
Protein Description Binds to F-actin. May be involved in regulation of the actin cytoskeleton (By similarity)..
Protein Sequence MTRSLFKGNFWSADILSTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQLAQSLREEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRKSLEMCSIQRDIEYFVNQRKTGQIPPAPIMYENFYSSQKNAVPAGKATGPNLARRGPLPIPKSSPDDPNYSLVDDYSLLYQ
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
4Phosphorylation----MTRSLFKGNFW
----CCCCCCCCCCC
29.0524719451
36UbiquitinationNNGRKNCKEFEDFLK
HHCCCCHHHHHHHHH
74.88-
68PhosphorylationRKKPCGQSEINTLKR
CCCCCCHHHHHHHHH
26.2322210691
117AcetylationEKQKLQRKKTELIMD
HHHHHHHHHHHHHHH
51.607976115
118AcetylationKQKLQRKKTELIMDA
HHHHHHHHHHHHHHH
49.797976127
119O-linked_GlycosylationQKLQRKKTELIMDAI
HHHHHHHHHHHHHHH
38.7730379171
128AcetylationLIMDAIHKQKSLQFK
HHHHHHHHHHCHHHH
53.997976139
136AcetylationQKSLQFKKTMDAKKN
HHCHHHHHHHHHHHH
50.827966179
137PhosphorylationKSLQFKKTMDAKKNY
HCHHHHHHHHHHHHH
22.37-
141AcetylationFKKTMDAKKNYEQKC
HHHHHHHHHHHHHHH
36.9715614425
176UbiquitinationQQEKLFVKLATSKTA
HHHHHHHHHHCCCCC
25.68-
181 (in isoform 2)Ubiquitination-35.8321906983
181 (in isoform 1)Ubiquitination-35.8321906983
181UbiquitinationFVKLATSKTAVEDSD
HHHHHCCCCCCCCCC
35.832190698
267PhosphorylationSIQRDIEYFVNQRKT
HCHHHHHHHHHCCCC
17.1121552520
274PhosphorylationYFVNQRKTGQIPPAP
HHHHCCCCCCCCCCC
36.1929759185
288PhosphorylationPIMYENFYSSQKNAV
CCCCCCCCCCCCCCC
20.9927642862
289PhosphorylationIMYENFYSSQKNAVP
CCCCCCCCCCCCCCC
23.3518077418
290PhosphorylationMYENFYSSQKNAVPA
CCCCCCCCCCCCCCC
33.5229759185
292AcetylationENFYSSQKNAVPAGK
CCCCCCCCCCCCCCC
49.157661935
299UbiquitinationKNAVPAGKATGPNLA
CCCCCCCCCCCCCHH
44.90-
299AcetylationKNAVPAGKATGPNLA
CCCCCCCCCCCCCHH
44.907661943
301PhosphorylationAVPAGKATGPNLARR
CCCCCCCCCCCHHHC
57.5718785766
311 (in isoform 2)Phosphorylation-7.18-
316PhosphorylationGPLPIPKSSPDDPNY
CCCCCCCCCCCCCCC
41.5728450419
317PhosphorylationPLPIPKSSPDDPNYS
CCCCCCCCCCCCCCC
38.1728450419
323PhosphorylationSSPDDPNYSLVDDYS
CCCCCCCCCCCCCCH
14.5828450419
324PhosphorylationSPDDPNYSLVDDYSL
CCCCCCCCCCCCCHH
28.6728450419
329PhosphorylationNYSLVDDYSLLYQ--
CCCCCCCCHHHCC--
9.21-
333PhosphorylationVDDYSLLYQ------
CCCCHHHCC------
19.9229978859

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 PPIP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPIP2_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 PPIP2_HUMAN !!

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

Oops, there are no PPI records of PPIP2_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 PPIP2_HUMAN

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Related Literatures of Post-Translational Modification

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