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SB0144 : Striatal-enriched protein tyrosine phosphatase (STEP)

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namestyrosine-protein phosphatase non-receptor type 5 isoform c [Homo sapiens]; tyrosine-protein phosphatase non-receptor type 5 isoform c; protein-tyrosine phosphatase striatum-enriched; neural-specific protein-tyrosine phosphatase; tyrosine-protein phosphatase non-receptor type 5; striatum-enriched protein-tyrosine phosphatase; Tyrosine-protein phosphatase non-receptor type 5; 3.1.3.48; Neural-specific protein-tyrosine phosphatase; Striatum-enriched protein-tyrosine phosphatase; STEP
Gene NamesPTPN5; protein tyrosine phosphatase, non-receptor type 5 (striatum-enriched)
Gene Locus11p15.1; chromosome 11
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001265167 NM_001278238 84867 P54829 176879 HGNC:9657 N/A hsa:84867

* Information From OMIM

Function: In rat neuronal cell cultures, Paul et al. (2003) showed that glutamate-mediated activation of N-methyl-D-aspartate (NMDA) receptors (see OMIM:138249) leads to the rapid but transient phosphorylation of extracellular signal-related kinase-2 (ERK2; OMIM:176948). NMDA-mediated influx of calcium, but not increased intracellular calcium from other sources, led to activation of the calcium-dependent phosphatase calcineurin and the subsequent dephosphorylation and activation of STEP. STEP then inactivated ERK2 through dephosphorylation of the tyrosine residue in its activation domain and blocked nuclear translocation of the kinase. Thus, STEP is important in regulating the duration of ERK activation and downstream signaling in neurons.

* Structure Information

1. Primary Information

Length: 541 aa

Average Mass: 60.961 kDa

Monoisotopic Mass: 60.922 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
--- cleavage 224 ---
Tyrosine phosphatase family 1. 458488120.00.0

3. Sequence Information

Fasta Sequence: SB0144.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 2BIJ (X-ray; 205 A; A=282-563), 2BV5 (X-ray; 180 A; A=280-561), 2CJZ (X-ray; 170 A; A=282-563)

* Cleavage Information

1 [sites] cleaved by Calpain 1

Source Reference: [PubMed ID: 19625523] Xu J, Kurup P, Zhang Y, Goebel-Goody SM, Wu PH, Hawasli AH, Baum ML, Bibb JA, Lombroso PJ, Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEP. J Neurosci. 2009 Jul 22;29(29):9330-43. doi: 10.1523/JNEUROSCI.2212-09.2009.

Cleavage sites (±10aa)

[Site 1] LQERRGSNVS224-LTLDMCTPGC

Ser224 Leu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Leu215Gln216Glu217Arg218Arg219Gly220Ser221Asn222Val223Ser224
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Leu225Thr226Leu227Asp228Met229Cys230Thr231Pro232Gly233Cys234

Sequence conservation (by blast)

* References

[PubMed ID: 23648065] Low SK, Chung S, Takahashi A, Zembutsu H, Mushiroda T, Kubo M, Nakamura Y, Genome-wide association study of chemotherapeutic agent-induced severe neutropenia/leucopenia for patients in Biobank Japan. Cancer Sci. 2013 Aug;104(8):1074-82. doi: 10.1111/cas.12186. Epub 2013 Jun 10.

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