PTPR2_HUMAN - dbPTM
PTPR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPR2_HUMAN
UniProt AC Q92932
Protein Name Receptor-type tyrosine-protein phosphatase N2
Gene Name PTPRN2
Organism Homo sapiens (Human).
Sequence Length 1015
Subcellular Localization Cytoplasmic vesicle, secretory vesicle membrane
Single-pass type I membrane protein . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Single-pass type I membrane protein . Predominantly found on dense-core secretory granules. So
Protein Description Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (By similarity). Required to maintain normal levels of renin expression and renin release (By similarity). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (By similarity). Has phosphatidylinositol phosphatase activity; the PIPase activity is involved in its ability to regulate insulin secretion. Can dephosphorylate phosphatidylinositol 4,5-biphosphate (PI(4,5)P2), phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate (By similarity). Regulates PI(4,5)P2 level in the plasma membrane and localization of cofilin at the plasma membrane and thus is indirectly involved in regulation of actin dynamics related to cell migration and metastasis; upon hydrolyzation of PI(4,5)P2 cofilin is released from the plasma membrane and acts in the cytoplasm in severing F-actin filaments. [PubMed: 26620550]
Protein Sequence MGPPLPLLLLLLLLLPPRVLPAAPSSVPRGRQLPGRLGCLLEEGLCGASEACVNDGVFGRCQKVPAMDFYRYEVSPVALQRLRVALQKLSGTGFTWQDDYTQYVMDQELADLPKTYLRRPEASSPARPSKHSVGSERRYSREGGAALANALRRHLPFLEALSQAPASDVLARTHTAQDRPPAEGDDRFSESILTYVAHTSALTYPPGSRTQLREDLLPRTLGQLQPDELSPKVDSGVDRHHLMAALSAYAAQRPPAPPGEGSLEPQYLLRAPSRMPRPLLAPAAPQKWPSPLGDSEDPSSTGDGARIHTLLKDLQRQPAEVRGLSGLELDGMAELMAGLMQGVDHGVARGSPGRAALGESGEQADGPKATLRGDSFPDDGVQDDDDRLYQEVHRLSATLGGLLQDHGSRLLPGALPFARPLDMERKKSEHPESSLSSEEETAGVENVKSQTYSKDLLGQQPHSEPGAAAFGELQNQMPGPSKEEQSLPAGAQEALSDGLQLEVQPSEEEARGYIVTDRDPLRPEEGRRLVEDVARLLQVPSSAFADVEVLGPAVTFKVSANVQNVTTEDVEKATVDNKDKLEETSGLKILQTGVGSKSKLKFLPPQAEQEDSTKFIALTLVSLACILGVLLASGLIYCLRHSSQHRLKEKLSGLGGDPGADATAAYQELCRQRMATRPPDRPEGPHTSRISSVSSQFSDGPIPSPSARSSASSWSEEPVQSNMDISTGHMILSYMEDHLKNKNRLEKEWEALCAYQAEPNSSFVAQREENVPKNRSLAVLTYDHSRVLLKAENSHSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVRQCYHYWPDEGSNLYHIYEVNLVSEHIWCEDFLVRSFYLKNLQTNETRTVTQFHFLSWYDRGVPSSSRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAILKALPQ
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
25PhosphorylationRVLPAAPSSVPRGRQ
CCCCCCCCCCCCCCC		38.96-
26PhosphorylationVLPAAPSSVPRGRQL
CCCCCCCCCCCCCCC		34.77-
124PhosphorylationLRRPEASSPARPSKH
HCCCCCCCCCCCCCC		29.62-
129PhosphorylationASSPARPSKHSVGSE
CCCCCCCCCCCCCCC		37.13-
139PhosphorylationSVGSERRYSREGGAA
CCCCCCCCCHHHHHH		20.50-
199PhosphorylationILTYVAHTSALTYPP
HHHHHHHHHCCCCCC		13.12-
220PhosphorylationREDLLPRTLGQLQPD
HHHHHHHCCCCCCCC		33.0424719451
220O-linked_GlycosylationREDLLPRTLGQLQPD
HHHHHHHCCCCCCCC		33.04101008221
230PhosphorylationQLQPDELSPKVDSGV
CCCCCCCCCCCCCCC		22.1924719451
230O-linked_GlycosylationQLQPDELSPKVDSGV
CCCCCCCCCCCCCCC		22.19101008229
247PhosphorylationHHLMAALSAYAAQRP
HHHHHHHHHHHHHCC		17.95-
249PhosphorylationLMAALSAYAAQRPPA
HHHHHHHHHHHCCCC		10.09-
360PhosphorylationGRAALGESGEQADGP
CCCCCCCCCCCCCCC		45.9226657352
375PhosphorylationKATLRGDSFPDDGVQ
CCCCCCCCCCCCCCC		41.3126657352
398O-linked_GlycosylationEVHRLSATLGGLLQD
HHHHHHHHHHHHHHH		23.6655831127
428PhosphorylationLDMERKKSEHPESSL
CCCCHHHCCCCCCCC		44.1429691806
433PhosphorylationKKSEHPESSLSSEEE
HHCCCCCCCCCCHHH		40.8229691806
434PhosphorylationKSEHPESSLSSEEET
HCCCCCCCCCCHHHH		30.5226657352
436PhosphorylationEHPESSLSSEEETAG
CCCCCCCCCHHHHHC		37.3426657352
437PhosphorylationHPESSLSSEEETAGV
CCCCCCCCHHHHHCC		55.0826657352
441PhosphorylationSLSSEEETAGVENVK
CCCCHHHHHCCCCHH		31.8029691806
516 (in isoform 2)O-linked_Glycosylation-18.76OGP
526 (in isoform 2)O-linked_Glycosylation-20.53OGP
564N-linked_GlycosylationKVSANVQNVTTEDVE
EEECCCEECCHHHHH		28.90UniProtKB CARBOHYD
592PhosphorylationSGLKILQTGVGSKSK
HCCEEEECCCCCHHH		30.3222210691
596PhosphorylationILQTGVGSKSKLKFL
EEECCCCCHHHCEEC		31.2022210691
598PhosphorylationQTGVGSKSKLKFLPP
ECCCCCHHHCEECCC		44.9424719451
619PhosphorylationSTKFIALTLVSLACI
CHHHHHHHHHHHHHH		18.98-
622PhosphorylationFIALTLVSLACILGV
HHHHHHHHHHHHHHH		17.23-
643PhosphorylationIYCLRHSSQHRLKEK
HHHHHHCCHHHHHHH		24.71-
666PhosphorylationGADATAAYQELCRQR
CHHHHHHHHHHHHHH		10.4725884760
691PhosphorylationGPHTSRISSVSSQFS
CCCCCCCCCCCCCCC		24.4727251275
692PhosphorylationPHTSRISSVSSQFSD
CCCCCCCCCCCCCCC		24.5226657352
694PhosphorylationTSRISSVSSQFSDGP
CCCCCCCCCCCCCCC		21.9927251275
695PhosphorylationSRISSVSSQFSDGPI
CCCCCCCCCCCCCCC		32.8427251275
698PhosphorylationSSVSSQFSDGPIPSP
CCCCCCCCCCCCCCC		33.7426657352
704PhosphorylationFSDGPIPSPSARSSA
CCCCCCCCCCCCCCC		32.0126657352
713PhosphorylationSARSSASSWSEEPVQ
CCCCCCCCCCCCCCC		34.0523286773
776PhosphorylationENVPKNRSLAVLTYD
HCCCCCCEEEEEEEC		30.0323312004
782PhosphorylationRSLAVLTYDHSRVLL
CEEEEEEECCHHEEE		13.9026503514
934PhosphorylationRRKVNKCYRGRSCPI
HHHHHHHHCCCCCCE		20.0829457462
941AcetylationYRGRSCPIIVHCSDG
HCCCCCCEEEECCCC		6.3619608861
953AcetylationSDGAGRSGTYVLIDM
CCCCCCCCCHHHHHH		21.5019608861
970AcetylationNKMAKGAKEIDIAAT
HHHHCCCCCCCHHHH		64.9619608861
977PhosphorylationKEIDIAATLEHLRDQ
CCCCHHHHHHHHHHC		24.5318187866
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 PTPR2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPR2_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 PTPR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPTN4_HUMANSPTBN4physical
11086001
CKAP5_HUMANCKAP5physical
12421765
INT11_HUMANCPSF3Lphysical
27880917
MON2_HUMANMON2physical
27880917
MSPD2_HUMANMOSPD2physical
27880917
S61A1_HUMANSEC61A1physical
27880917
SORT_HUMANSORT1physical
27880917
TELO2_HUMANTELO2physical
27880917
HID1_HUMANHID1physical
27880917
SNX19_HUMANSNX19physical
27880917
K1C17_HUMANKRT17physical
27880917
HGS_HUMANHGSphysical
27880917
K1C16_HUMANKRT16physical
27880917
STAM1_HUMANSTAMphysical
27880917
GRP78_HUMANHSPA5physical
27880917
STIM1_HUMANSTIM1physical
27880917
CLCC1_HUMANCLCC1physical
27880917
STAM2_HUMANSTAM2physical
27880917
K1C14_HUMANKRT14physical
27880917
GOGA4_HUMANGOLGA4physical
27880917
ANKL2_HUMANANKLE2physical
27880917
NU155_HUMANNUP155physical
27880917
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 PTPR2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-970, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-977, AND MASSSPECTROMETRY.

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