Search by BoMiProt ID - Bomi3194


Primary Information

BoMiProt ID Bomi3194
Protein Name Tyrosine-protein phosphatase non-receptor type substrate 1
Organism Bos taurus
Uniprot IDO46631
Milk FractionWhey
Ref Sequence ID NP_786982.1
Aminoacid Length 506
Molecular Weight 55093
FASTA Sequence Download
Gene Name SIRPA
Gene ID 327666
Protein Existence Status Reveiwed:Experimental evidence at transcript level

Secondary Information

Protein Function SHP-1 and SHP-2 are non-transmembrane, Src homology 2 (SH2) domain-containing PTPs, which play critical roles in many signaling pathways and disease processes
Biochemical Properties The two enzymes share >55% sequence identity, a similar 3D structure, and a common regulatory mechanism. However, they often perform opposite cellular functions, with SHP-1 typically acting as a negative regulator of signaling, whereas SHP-2 is a positive regulator. Some of the functional differences may be attributed to the SH2 domains, which display overlapping but non-identical binding specificities and may therefore direct their respective PTP domains to different pY proteins.
PTMs Disulfide bond formation,N-Linked Glycosylation at Asn, Phosphorylation atTyr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions 1-6,137-155,194-199,355-365,401-419,437-469,492-501
DisProt Annotation
TM Helix Prediction 1TMH;(372-394)
Bibliography 1.Ren L, Chen X, Luechapanichkul R, Selner NG, Meyer TM, Wavreille AS, Chan R, Iorio C, Zhou X, Neel BG, Pei D. Substrate specificity of protein tyrosine phosphatases 1B, RPTPα, SHP-1, and SHP-2. Biochemistry. 2011 Mar 29;50(12):2339-56. doi: 10.1021/bi1014453. Epub 2011 Feb 18. PMID: 21291263; PMCID: PMC3074353. 2.Crystal structure of the tyrosine phosphatase SHP-2.Hof P, Pluskey S, Dhe-Paganon S, Eck MJ, Shoelson SE.Cell. 1998 Feb 20; 92(4):441-50. 3.Crystal structure of human protein-tyrosine phosphatase SHP-1.Yang J, Liu L, He D, Song X, Liang X, Zhao ZJ, Zhou GW.J Biol Chem. 2003 Feb 21; 278(8):6516-20. 4.Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains.Sweeney MC, Wavreille AS, Park J, Butchar JP, Tridandapani S, Pei D.Biochemistry. 2005 Nov 15; 44(45):14932-47.