TP4A2_HUMAN - dbPTM
TP4A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TP4A2_HUMAN
UniProt AC Q12974
Protein Name Protein tyrosine phosphatase type IVA 2
Gene Name PTP4A2
Organism Homo sapiens (Human).
Sequence Length 167
Subcellular Localization Cell membrane. Early endosome. Cytoplasm.
Protein Description Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Promotes tumors. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB..
Protein Sequence MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ
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
11PhosphorylationPAPVEISYENMRFLI
CCCEEEEECCEEEEE		19.58-
23PhosphorylationFLITHNPTNATLNKF
EEEECCCCCCHHHHH		42.6823186163
26PhosphorylationTHNPTNATLNKFTEE
ECCCCCCHHHHHHHH		32.6923186163
29 (in isoform 2)Ubiquitination-57.6921890473
29 (in isoform 1)Ubiquitination-57.6921890473
29UbiquitinationPTNATLNKFTEELKK
CCCCHHHHHHHHHHH		57.6923000965
29MalonylationPTNATLNKFTEELKK
CCCCHHHHHHHHHHH		57.6926320211
35UbiquitinationNKFTEELKKYGVTTL
HHHHHHHHHCCCEEE		47.4223000965
36UbiquitinationKFTEELKKYGVTTLV
HHHHHHHHCCCEEEE		60.9223000965
36 (in isoform 2)Ubiquitination-60.9221890473
36 (in isoform 1)Ubiquitination-60.9221890473
49PhosphorylationLVRVCDATYDKAPVE
EEEECCCCCCCCCCC		20.9928796482
50PhosphorylationVRVCDATYDKAPVEK
EEECCCCCCCCCCCC		19.7128796482
52AcetylationVCDATYDKAPVEKEG
ECCCCCCCCCCCCCC		44.1427452117
57UbiquitinationYDKAPVEKEGIHVLD
CCCCCCCCCCEEEEE		62.5729967540
110UbiquitinationAGLGRAPVLVALALI
CCCCHHHHHHHHHHH		7.0121890473
110UbiquitinationAGLGRAPVLVALALI
CCCCHHHHHHHHHHH		7.0123000965
116UbiquitinationPVLVALALIECGMKY
HHHHHHHHHHCCCCH		3.3523000965
117UbiquitinationVLVALALIECGMKYE
HHHHHHHHHCCCCHH		3.2421890473
117UbiquitinationVLVALALIECGMKYE
HHHHHHHHHCCCCHH		3.2421890473
121UbiquitinationLALIECGMKYEDAVQ
HHHHHCCCCHHHHHH		6.7223000965
123UbiquitinationLIECGMKYEDAVQFI
HHHCCCCHHHHHHHH		15.3421890473
127UbiquitinationGMKYEDAVQFIRQKR
CCCHHHHHHHHHHHH		8.0523000965
140PhosphorylationKRRGAFNSKQLLYLE
HHCCCCCHHHHHHHH		18.4819835603
141AcetylationRRGAFNSKQLLYLEK
HCCCCCHHHHHHHHH		46.1726051181
141 (in isoform 1)Ubiquitination-46.1721890473
141UbiquitinationRRGAFNSKQLLYLEK
HCCCCCHHHHHHHHH		46.1723000965
145PhosphorylationFNSKQLLYLEKYRPK
CCHHHHHHHHHHCCC		22.7722817900
148UbiquitinationKQLLYLEKYRPKMRL
HHHHHHHHHCCCCEE		43.9221890473
152UbiquitinationYLEKYRPKMRLRFRD
HHHHHCCCCEEEEEC		27.8823000965
164FarnesylationFRDTNGHCCVQ----
EECCCCCCCCC----		2.299018080
164MethylationFRDTNGHCCVQ----
EECCCCCCCCC----		2.29-
164FarnesylationFRDTNGHCCVQ----
EECCCCCCCCC----		2.299018080
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 TP4A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TP4A2_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 TP4A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNNM3_HUMANCNNM3physical
17353931
CNNM4_HUMANCNNM4physical
17353931
FNTA_HUMANFNTAphysical
17353931
FNTB_HUMANFNTBphysical
17353931
TP4A1_HUMANPTP4A1physical
17353931
PGTB2_HUMANRABGGTBphysical
11447212
CNNM4_HUMANCNNM4physical
27880917
GBB4_HUMANGNB4physical
27880917
SPTN1_HUMANSPTAN1physical
27880917
SPTB2_HUMANSPTBN1physical
27880917
TP4A1_HUMANPTP4A1physical
28514442
CNNM1_HUMANCNNM1physical
28514442
EFL1_HUMANEFTUD1physical
28514442
CNNM4_HUMANCNNM4physical
28514442
CNNM2_HUMANCNNM2physical
28514442
FMN2_HUMANFMN2physical
28514442
TP4A3_HUMANPTP4A3physical
28514442
TP4A2_HUMANPTP4A2physical
27432908
TP4A3_HUMANPTP4A3physical
27432908
CNNM3_HUMANCNNM3physical
27432908
CNNM2_HUMANCNNM2physical
27432908
CNNM4_HUMANCNNM4physical
27432908
FHL3_HUMANFHL3physical
27432908
A7L3B_HUMANATXN7L3Bphysical
27432908
TRBP2_HUMANTARBP2physical
27432908
PRDX4_HUMANPRDX4physical
27432908
G45IP_HUMANGADD45GIP1physical
27432908
PRDX3_HUMANPRDX3physical
27432908
AROS_HUMANRPS19BP1physical
27432908
RL22L_HUMANRPL22L1physical
27432908
RL18A_HUMANRPL18Aphysical
27432908
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 TP4A2_HUMAN

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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase,with the beta-subunit of geranylgeranyltransferase II.";
Si X., Zeng Q., Ng C.H., Hong W., Pallen C.J.;
J. Biol. Chem. 276:32875-32882(2001).
Cited for: INTERACTION WITH RABGGTB, ISOPRENYLATION AT CYS-164, SUBCELLULARLOCATION, AND MUTAGENESIS OF 164-CYS--GLN-167 AND CYS-165.
"Prenylation of oncogenic human PTP(CAAX) protein tyrosinephosphatases.";
Cates C.A., Michael R.L., Stayrook K.R., Harvey K.A., Burke Y.D.,Randall S.K., Crowell P.L., Crowell D.N.;
Cancer Lett. 110:49-55(1996).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-164, ANDENZYME REGULATION.

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