SAPC2_HUMAN - dbPTM
SAPC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAPC2_HUMAN
UniProt AC Q86UD0
Protein Name Suppressor APC domain-containing protein 2 {ECO:0000305}
Gene Name SAPCD2 {ECO:0000312|HGNC:HGNC:28055}
Organism Homo sapiens (Human).
Sequence Length 394
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cell cortex . Apical cell membrane . Cell junction, tight junction . Localized at the apical cortical region during the M phase. In horizontally retinal progenitor dividing cells, localized at the pole cortical region
Protein Description Plays a role in planar mitotic spindle orientation in retinal progenitor cells (RPCs) and promotes the production of symmetric terminal divisions (By similarity). Negatively regulates the mitotic apical cortex localization of GPSM2. [PubMed: 26766442 Involved also in positive regulation of cell proliferation and tumor cell growth]
Protein Sequence MAGAAMAERGRVPPPAPAPSTEGLPRAFLQSLRTLFDILDDRRRGCVHLREIESRWQGTDARELPRGVLEGLRQVAPASGYLTFERFVAGLRTSLLSADGGPRDPTRAPARPGDQPPPPPQRLVFAPADEPRTVLERKPLPLGVRAPLAGPSAAARSPEQLCAPAEAAPCPAEPERSQSAALEPSSSADAGAVACRALEADSGDARRAPRARGERRRHTIASGVDCGLLKQMKELEQEKEVLLQGLEMMARGRDWYQQQLQRVQERQRRLGQSRASADFGAAGSPRPLGRLLPKVQEVARCLGELLAAACASRALPPSSSGPPCPALTSTSPPVWQQQTILMLKEQNRLLTQEVTEKSERITQLEQEKSALIKQLFEARALSQQDGGPLDSTFI
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
79PhosphorylationLRQVAPASGYLTFER
HHHHCCCCCEEEHHH
27.2328152594
81PhosphorylationQVAPASGYLTFERFV
HHCCCCCEEEHHHHH
10.4825884760
83PhosphorylationAPASGYLTFERFVAG
CCCCCEEEHHHHHHH
18.2428152594
152PhosphorylationRAPLAGPSAAARSPE
CCCCCCCCHHHCCHH
29.6224719451
157PhosphorylationGPSAAARSPEQLCAP
CCCHHHCCHHHHCCC
28.2325159151
179PhosphorylationAEPERSQSAALEPSS
CCCCHHHCCCCCCCC
19.4328348404
219PhosphorylationRGERRRHTIASGVDC
HCHHHHHHHHHCCCH
19.2122617229
222PhosphorylationRRRHTIASGVDCGLL
HHHHHHHHCCCHHHH
35.1830576142
230UbiquitinationGVDCGLLKQMKELEQ
CCCHHHHHHHHHHHH
54.0832015554
256PhosphorylationMARGRDWYQQQLQRV
HHHCHHHHHHHHHHH
10.7527174698
273PhosphorylationRQRRLGQSRASADFG
HHHHHHCHHHHHCCC
28.1928102081
276PhosphorylationRLGQSRASADFGAAG
HHHCHHHHHCCCCCC
27.5329496963
284PhosphorylationADFGAAGSPRPLGRL
HCCCCCCCCCCHHHH
17.0125159151
328PhosphorylationGPPCPALTSTSPPVW
CCCCCCCCCCCCCHH
31.8728348404
329PhosphorylationPPCPALTSTSPPVWQ
CCCCCCCCCCCCHHH
27.9528348404
330PhosphorylationPCPALTSTSPPVWQQ
CCCCCCCCCCCHHHH
39.7628348404
331PhosphorylationCPALTSTSPPVWQQQ
CCCCCCCCCCHHHHH
27.2928348404
362PhosphorylationTEKSERITQLEQEKS
HHHHHHHHHHHHHHH
33.0728842319
369PhosphorylationTQLEQEKSALIKQLF
HHHHHHHHHHHHHHH
27.7928842319

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 SAPC2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAPC2_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 SAPC2_HUMAN !!

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

Oops, there are no PPI records of SAPC2_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 SAPC2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP