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Protein Page:
PTPN23 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PTPN23 May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis. Belongs to the protein-tyrosine phosphatase family. Non-receptor class subfamily. Note: This description may include information from UniProtKB.
Protein type: EC 3.1.3.48; Motility/polarity/chemotaxis; Protein phosphatase, tyrosine (non-receptor)
Cellular Component: cytoplasmic membrane-bound vesicle; early endosome; cytoplasm; nucleolus; nucleus; endosome
Molecular Function: protein binding; protein tyrosine phosphatase activity
Biological Process: protein transport; ubiquitin-dependent protein catabolic process via the multivesicular body pathway; regulation of cell migration
Reference #:  Q9H3S7 (UniProtKB)
Alt. Names/Synonyms: DKFZp564F0923; HD-PTP; HDPTP; His domain-containing protein tyrosine phosphatase; His-domain protein tyrosine phosphatase; KIAA1471; Protein tyrosine phosphatase TD14; protein tyrosine phosphatase, non-receptor type 23; PTN23; PTP-TD14; PTPN23; Tyrosine-protein phosphatase non-receptor type 23
Gene Symbols: PTPN23
Molecular weight: 178,974 Da
Basal Isoelectric point: 6.45  Predict pI for various phosphorylation states
Select Structure to View Below

PTPN23

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 K32-u AVKKFVLkNYGENPE
0 1 K46-u EAYNEELkKLELLRQ
0 3 Y213-p ISAQVVDyYKEACRA
0 8 K279-u YFQSALDkLNEAIkL
0 3 K285-u DkLNEAIkLAkGQPD
0 2 K288-u NEAIkLAkGQPDTVQ
0 2 K340-u VKGAPLVkPLPVNPT
0 7 K472-u EDELLEQkFQEAVGQ
0 1 K500 EVRREWAKYMEVHEK
0 1 K600 TDHSEMKKLFEEQLK
0 1 K608-m2 LFEEQLKkYDQLkVY
0 1 K613-m2 LKkYDQLkVYLEQNL
0 1 Y679-p SQEGRDFyADLESKV
0 1 S733-p LLPRREEsEAVEAGD
0 2 P741 EAVEAGDPPEELRSL
0 1 R950-m1 PAGFPAPrIGPQPQP
0 3 S1122-p AAADLLSssPEsQHG
0 6 S1123-p AADLLSssPEsQHGG
0 2 S1126-p LLSssPEsQHGGtQs
0 1 T1131-p PEsQHGGtQsPGGGQ
0 4 S1133-p sQHGGtQsPGGGQPL
0 64 Y1165-p RLIERDPyEHPERLR
0 56 Y1229-p RHQDVMPyDSNRVVL
0 1 R1595-m1 FSLDSSLrGKQRMSK
0 1 R1615-m1 AHNGQGLrATrPSDD
0 1 R1618-m1 GQGLrATrPSDDPLS
0 5 K1635-u DPLWTLNkT______
  mouse

 
K32-u AVKKFVLkNYGENPE
K46 EAYNEELKKLELLRQ
Y213 ISAQVVDYYKEACRA
K279-u YFQSALDkLNEAIkL
K285-u DkLNEAIkLAkGQPD
K288-u NEAIkLAkGQPDTVQ
K340-u VKGAPLVkPLPVNPT
K472 EDELQEQKLQETLGQ
K502-u EVRREWAkYMEVHEK
K602-u TDHSEMKkLFEEQLK
K610 LFEEQLKKYDQLKVY
K615 LKKYDQLKVYLEQNL
Y681 SQEGKDFYADLESKV
G736 LLSRREEGEAVEAGD
T744-p EAVEAGDtPEELRSL
R974 PTGFPVPRTGPQAQA
S1178-p AAADLLSssPEsQHG
S1179-p AADLLSssPEsQHGG
S1182-p LLSssPEsQHGGtQP
T1187-p PEsQHGGtQPPGGGQ
P1189 sQHGGtQPPGGGQPL
Y1221 RLIEQDPYEHPERLQ
Y1285 RHQDVMPYDSNRVVL
R1651 FSLDSSLRGKQRMSK
R1671 AHNGQGLRAAQPTDD
Q1674 GQGLRAAQPTDDPLS
K1691-u DPLWTLNkT______
  rat

 
- gap
- gap
Y38 ISAQVVDYYKEACRA
K104 YFQSALDKLNEAIKL
K110 DKLNEAIKLAKGQPD
K113 NEAIKLAKGQPDTVQ
K165 VKGAPLVKPLPVNPT
K297 EDELQEQKLQETLGQ
K327 EVRREWAKYTEVHEK
K427 TDHSEMKKLFEEQLK
K435 LFEEQLKKYDQLKVY
K440 LKKYDQLKVYLEQNL
Y506 SQEGKDFYADLESKV
G561 LLSRREEGEAAEAGD
Q569 EAAEAGDQPEELRSL
R785 PTSFPAPRIGPQPPP
S985 AAADLLSSsPESQHG
S986-p AADLLSSsPESQHGG
S989 LLSSsPESQHGGTQP
T994 PESQHGGTQPPGGGQ
P996 SQHGGTQPPGGGQPL
Y1028 RLIEQDPYEHPERLQ
Y1092 RHQDVMPYDSNRVVL
R1458 FSLDSSLRGKQRMSK
R1478 AHNGQGLRAAQPTDD
Q1481 GQGLRAAQPTDDPLS
K1498 DPLWTLNKT______
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