PTPRN_HUMAN - dbPTM
PTPRN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRN_HUMAN
UniProt AC Q16849
Protein Name Receptor-type tyrosine-protein phosphatase-like N
Gene Name PTPRN
Organism Homo sapiens (Human).
Sequence Length 979
Subcellular Localization Membrane
Single-pass type I membrane protein . Cytoplasmic vesicle, secretory vesicle membrane
Single-pass type I membrane protein . Perikaryon . Cell projection, axon . Cell junction, synapse . Cell membrane
Single-pass type I membrane protein . En
Protein Description Plays a role in vesicle-mediated secretory processes. [PubMed: 24843546 Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets (By similarity Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation]
Protein Sequence MRRPRRPGGLGGSGGLRLLLCLLLLSSRPGGCSAVSAHGCLFDRRLCSHLEVCIQDGLFGQCQVGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPRPRDRSGLAPKRPGPAGELLLQDIPTGSAPAAQHRLPQPPVGKGGAGASSSLSPLQAELLPPLLEHLLLPPQPPHPSLSYEPALLQPYLFHQFGSRDGSRVSEGSPGMVSVGPLPKAEAPALFSRTASKGIFGDHPGHSYGDLPGPSPAQLFQDSGLLYLAQELPAPSRARVPRLPEQGSSSRAEDSPEGYEKEGLGDRGEKPASPAVQPDAALQRLAAVLAGYGVELRQLTPEQLSTLLTLLQLLPKGAGRNPGGVVNVGADIKKTMEGPVEGRDTAELPARTSPMPGHPTASPTSSEVQQVPSPVSSEPPKAARPPVTPVLLEKKSPLGQSQPTVAGQPSARPAAEEYGYIVTDQKPLSLAAGVKLLEILAEHVHMSSGSFINISVVGPALTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQILQTGVGQREEAAAVLPQTAHSTSPMRSVLLTLVALAGVAGLLVALAVALCVRQHARQQDKERLAALGPEGAHGDTTFEYQDLCRQHMATKSLFNRAEGPPEPSRVSSVSSQFSDAAQASPSSHSSTPSWCEEPAQANMDISTGHMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGASLYHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAILKALPQ
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
26PhosphorylationLLCLLLLSSRPGGCS
HHHHHHHHCCCCCCC		25.0324719451
27PhosphorylationLCLLLLSSRPGGCSA
HHHHHHHCCCCCCCH		42.3324719451
96PhosphorylationQLMSQGLSWHDDLTQ
HHHHCCCCCCHHHHH		29.2322798277
104PhosphorylationWHDDLTQYVISQEME
CCHHHHHHHHHHHHH		8.4322798277
127PhosphorylationEPRPRDRSGLAPKRP
CCCCCCCCCCCCCCC		42.3128188228
226PhosphorylationGSRVSEGSPGMVSVG
CCCCCCCCCCCEEEC		17.7721712546
231PhosphorylationEGSPGMVSVGPLPKA
CCCCCCEEECCCCCC		16.6821712546
301PhosphorylationPRLPEQGSSSRAEDS
CCCCCCCCCCCCCCC		25.4925307156
302PhosphorylationRLPEQGSSSRAEDSP
CCCCCCCCCCCCCCC		30.5726657352
303PhosphorylationLPEQGSSSRAEDSPE
CCCCCCCCCCCCCCC		36.8925307156
308PhosphorylationSSSRAEDSPEGYEKE
CCCCCCCCCCCCCCC		19.16-
326PhosphorylationDRGEKPASPAVQPDA
CCCCCCCCCCCCHHH		23.1721214269
345PhosphorylationLAAVLAGYGVELRQL
HHHHHHCCCCCHHHC		16.6421214269
353PhosphorylationGVELRQLTPEQLSTL
CCCHHHCCHHHHHHH		19.2124043423
358PhosphorylationQLTPEQLSTLLTLLQ
HCCHHHHHHHHHHHH		19.3924043423
359PhosphorylationLTPEQLSTLLTLLQL
CCHHHHHHHHHHHHH		34.0924043423
362PhosphorylationEQLSTLLTLLQLLPK
HHHHHHHHHHHHCCC		28.6524043423
441O-linked_GlycosylationKAARPPVTPVLLEKK
CCCCCCCCCEEEEEC		17.2922171320
506N-linked_GlycosylationMSSGSFINISVVGPA
CCCCCCEEEEEECCE		20.6225561468
524N-linked_GlycosylationRIRHNEQNLSLADVT
EECCCCCCCCHHHHH		25.9725561468
628PhosphorylationHGDTTFEYQDLCRQH
CCCCCHHHHHHHHHH		11.7925884760
746PhosphorylationRHPDFLPYDHARIKL
CCCCCCCCCCEEEEE		23.6225884760
754SumoylationDHARIKLKVESSPSR
CCEEEEEEECCCCCH		38.6716622421
880PhosphorylationLSWPAEGTPASTRPL
CCCCCCCCCCCCCCH		13.7422210691
898PhosphorylationRRKVNKCYRGRSCPI
HHHHHHHHCCCCCCE		20.0829457462
918PhosphorylationDGAGRTGTYILIDMV
CCCCCCCHHHHHHHH		13.5324719451
919PhosphorylationGAGRTGTYILIDMVL
CCCCCCHHHHHHHHH		8.6224719451
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 PTPRN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
754KSumoylation

16622421
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 PTPRN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNTB2_HUMANSNTB2physical
11483505
SPTN4_HUMANSPTBN4physical
11086001
GT251_HUMANCOLGALT1physical
27880917
PLOD3_HUMANPLOD3physical
27880917
CALR_HUMANCALRphysical
27880917
PPIB_HUMANPPIBphysical
27880917
GANAB_HUMANGANABphysical
27880917
UGGG1_HUMANUGGT1physical
27880917
GLU2B_HUMANPRKCSHphysical
27880917
PDIA4_HUMANPDIA4physical
27880917
PLOD1_HUMANPLOD1physical
27880917
TXND5_HUMANTXNDC5physical
27880917
HYOU1_HUMANHYOU1physical
27880917
PO210_HUMANNUP210physical
27880917
PDIA1_HUMANP4HBphysical
27880917
PDIA3_HUMANPDIA3physical
27880917
ENPL_HUMANHSP90B1physical
27880917
CALU_HUMANCALUphysical
27880917
GRM1A_HUMANGRAMD1Aphysical
27880917
DJB11_HUMANDNAJB11physical
27880917
CALX_HUMANCANXphysical
27880917
GRP78_HUMANHSPA5physical
27880917
OST48_HUMANDDOSTphysical
27880917
SNX19_HUMANSNX19physical
27880917
PDIA6_HUMANPDIA6physical
27880917
RPN2_HUMANRPN2physical
27880917
TGO1_HUMANMIA3physical
27880917
MICA2_HUMANMICAL2physical
28514442
SGSM2_HUMANSGSM2physical
28514442
CCD51_HUMANCCDC51physical
28514442
TM214_HUMANTMEM214physical
28514442
PTPR2_HUMANPTPRN2physical
28514442
MFSD8_HUMANMFSD8physical
28514442
HLAF_HUMANHLA-Fphysical
28514442
NEUFC_HUMANCYB5D2physical
28514442
ADPGK_HUMANADPGKphysical
28514442
PTPRN_HUMANPTPRNphysical
27432908
PEX19_HUMANPEX19physical
27432908
CS025_HUMANC19orf25physical
27432908
XPO4_HUMANXPO4physical
27432908
TM214_HUMANTMEM214physical
27432908
CNIH4_HUMANCNIH4physical
27432908
CKLF6_HUMANCMTM6physical
27432908
SAAL1_HUMANSAAL1physical
27432908
CIP2A_HUMANKIAA1524physical
27432908
BZW2_HUMANBZW2physical
27432908
S61A2_HUMANSEC61A2physical
27432908
EIF3K_HUMANEIF3Kphysical
27432908
LMBRL_HUMANLMBR1Lphysical
27432908
TRI13_HUMANTRIM13physical
27432908
XPO5_HUMANXPO5physical
27432908
ATX10_HUMANATXN10physical
27432908
TBC15_HUMANTBC1D15physical
27432908
HEAT3_HUMANHEATR3physical
27432908
NCDN_HUMANNCDNphysical
27432908
XPO6_HUMANXPO6physical
27432908
TMM43_HUMANTMEM43physical
27432908
SCO2_HUMANSCO2physical
27432908
TNPO3_HUMANTNPO3physical
27432908
PDIA4_HUMANPDIA4physical
27432908
COX2_HUMANCOX2physical
27432908
TNPO1_HUMANTNPO1physical
27432908
CAND2_HUMANCAND2physical
27432908
PDIA1_HUMANP4HBphysical
27432908
LTN1_HUMANLTN1physical
27432908
DAAF5_HUMANDNAAF5physical
27432908
OS9_HUMANOS9physical
27432908
RINT1_HUMANRINT1physical
27432908
TTYH3_HUMANTTYH3physical
27432908
XPO2_HUMANCSE1Lphysical
27432908
PDIA6_HUMANPDIA6physical
27432908
CALX_HUMANCANXphysical
27432908
GANAB_HUMANGANABphysical
27432908
S61A1_HUMANSEC61A1physical
27432908
CLN6_HUMANCLN6physical
27432908
DYM_HUMANDYMphysical
27432908
ERP44_HUMANERP44physical
27432908
XPOT_HUMANXPOTphysical
27432908
KIF14_HUMANKIF14physical
27432908
ZW10_HUMANZW10physical
27432908
S39A7_HUMANSLC39A7physical
27432908
IPO5_HUMANIPO5physical
27432908
RNBP6_HUMANRANBP6physical
27432908
SPTC2_HUMANSPTLC2physical
27432908
MON2_HUMANMON2physical
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 PTPRN_HUMAN

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-441, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.

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