UniProt ID | PTPRZ_HUMAN | |
---|---|---|
UniProt AC | P23471 | |
Protein Name | Receptor-type tyrosine-protein phosphatase zeta | |
Gene Name | PTPRZ1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 2315 | |
Subcellular Localization |
Isoform 1: Cell membrane Single-pass type I membrane protein. Secreted. A secreted form is apparently generated by shedding of the extracellular domain.. Isoform 2: Secreted . |
|
Protein Description | Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades (By similarity).. | |
Protein Sequence | MRILKRFLACIQLLCVCRLDWANGYYRQQRKLVEEIGWSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEMVFKASKITFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMDYLQNNFREQQYKFSRQVFSSYTGKEEIHEAVCSSEPENVQADPENYTSLLVTWERPRVVYDTMIEKFAVLYQQLDGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAICTNGLYGKYSDQLIVDMPTDNPELDLFPELIGTEEIIKEEEEGKDIEEGAIVNPGRDSATNQIRKKEPQISTTTHYNRIGTKYNEAKTNRSPTRGSEFSGKGDVPNTSLNSTSQPVTKLATEKDISLTSQTVTELPPHTVEGTSASLNDGSKTVLRSPHMNLSGTAESLNTVSITEYEEESLLTSFKLDTGAEDSSGSSPATSAIPFISENISQGYIFSSENPETITYDVLIPESARNASEDSTSSGSEESLKDPSMEGNVWFPSSTDITAQPDVGSGRESFLQTNYTEIRVDESEKTTKSFSAGPVMSQGPSVTDLEMPHYSTFAYFPTEVTPHAFTPSSRQQDLVSTVNVVYSQTTQPVYNGETPLQPSYSSEVFPLVTPLLLDNQILNTTPAASSSDSALHATPVFPSVDVSFESILSSYDGAPLLPFSSASFSSELFRHLHTVSQILPQVTSATESDKVPLHASLPVAGGDLLLEPSLAQYSDVLSTTHAASETLEFGSESGVLYKTLMFSQVEPPSSDAMMHARSSGPEPSYALSDNEGSQHIFTVSYSSAIPVHDSVGVTYQGSLFSGPSHIPIPKSSLITPTASLLQPTHALSGDGEWSGASSDSEFLLPDTDGLTALNISSPVSVAEFTYTTSVFGDDNKALSKSEIIYGNETELQIPSFNEMVYPSESTVMPNMYDNVNKLNASLQETSVSISSTKGMFPGSLAHTTTKVFDHEISQVPENNFSVQPTHTVSQASGDTSLKPVLSANSEPASSDPASSEMLSPSTQLLFYETSASFSTEVLLQPSFQASDVDTLLKTVLPAVPSDPILVETPKVDKISSTMLHLIVSNSASSENMLHSTSVPVFDVSPTSHMHSASLQGLTISYASEKYEPVLLKSESSHQVVPSLYSNDELFQTANLEINQAHPPKGRHVFATPVLSIDEPLNTLINKLIHSDEILTSTKSSVTGKVFAGIPTVASDTFVSTDHSVPIGNGHVAITAVSPHRDGSVTSTKLLFPSKATSELSHSAKSDAGLVGGGEDGDTDDDGDDDDDDRGSDGLSIHKCMSCSSYRESQEKVMNDSDTHENSLMDQNNPISYSLSENSEEDNRVTSVSSDSQTGMDRSPGKSPSANGLSQKHNDGKEENDIQTGSALLPLSPESKAWAVLTSDEESGSGQGTSDSLNENETSTDFSFADTNEKDADGILAAGDSEITPGFPQSPTSSVTSENSEVFHVSEAEASNSSHESRIGLAEGLESEKKAVIPLVIVSALTFICLVVLVGILIYWRKCFQTAHFYLEDSTSPRVISTPPTPIFPISDDVGAIPIKHFPKHVADLHASSGFTEEFETLKEFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVLDSHIHAYVNALLIPGPAGKTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVSTRQEENPSTSLDSNGAALPDGNIAESLESLV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
53 | Phosphorylation | QKNWGKKYPTCNSPK CCCCCCCCCCCCCCC | 13.78 | 24719451 | |
55 | Phosphorylation | NWGKKYPTCNSPKQS CCCCCCCCCCCCCCC | 22.64 | 24719451 | |
60 | Acetylation | YPTCNSPKQSPINID CCCCCCCCCCCCCCC | 64.33 | 19828889 | |
78 | Acetylation | TQVNVNLKKLKFQGW CEECCCHHHCEECCC | 51.35 | 19828897 | |
101 | Phosphorylation | FIHNTGKTVEINLTN EEECCCCEEEEECCC | 25.39 | 30622161 | |
105 | N-linked_Glycosylation | TGKTVEINLTNDYRV CCCEEEEECCCCCEE | 27.57 | 16335952 | |
107 | Phosphorylation | KTVEINLTNDYRVSG CEEEEECCCCCEECC | 22.89 | 30622161 | |
107 | O-linked_Glycosylation | KTVEINLTNDYRVSG CEEEEECCCCCEECC | 22.89 | 28657654 | |
134 | N-linked_Glycosylation | TFHWGKCNMSSDGSE EEEEECCCCCCCCCC | 36.54 | UniProtKB CARBOHYD | |
136 | Phosphorylation | HWGKCNMSSDGSEHS EEECCCCCCCCCCCC | 15.99 | - | |
156 | Phosphorylation | FPLEMQIYCFDADRF CCCEEEEEEEEHHHC | 3.11 | 28270605 | |
164 | Phosphorylation | CFDADRFSSFEEAVK EEEHHHCCCHHHHHC | 34.70 | 28270605 | |
165 | Phosphorylation | FDADRFSSFEEAVKG EEHHHCCCHHHHHCC | 33.68 | 28270605 | |
187 | Phosphorylation | SILFEVGTEENLDFK HHHEECCCCCCCCHH | 45.35 | 23879269 | |
223 | N-linked_Glycosylation | ILLNLLPNSTDKYYI HHHHCCCCCCCCEEE | 58.47 | UniProtKB CARBOHYD | |
232 | N-linked_Glycosylation | TDKYYIYNGSLTSPP CCCEEEECCCCCCCC | 24.82 | UniProtKB CARBOHYD | |
293 | Phosphorylation | REQQYKFSRQVFSSY HHHHHHHHHHHHHHC | 20.04 | 24719451 | |
324 | N-linked_Glycosylation | NVQADPENYTSLLVT CCCCCCCCCCEEEEE | 51.26 | UniProtKB CARBOHYD | |
381 | N-linked_Glycosylation | ILNNLLPNMSYVLQI HHHHHCCCHHHHHHH | 31.81 | UniProtKB CARBOHYD | |
479 | O-linked_Glycosylation | TKYNEAKTNRSPTRG CCCCCCCCCCCCCCC | 42.80 | 55827771 | |
482 | O-linked_Glycosylation | NEAKTNRSPTRGSEF CCCCCCCCCCCCCCC | 32.47 | 55827777 | |
484 | O-linked_Glycosylation | AKTNRSPTRGSEFSG CCCCCCCCCCCCCCC | 49.24 | 55827783 | |
497 | N-linked_Glycosylation | SGKGDVPNTSLNSTS CCCCCCCCCCCCCCC | 41.99 | UniProtKB CARBOHYD | |
501 | N-linked_Glycosylation | DVPNTSLNSTSQPVT CCCCCCCCCCCCCCC | 42.90 | UniProtKB CARBOHYD | |
544 | Phosphorylation | SLNDGSKTVLRSPHM ECCCCCCEEEECCCC | 26.86 | 24719451 | |
552 | N-linked_Glycosylation | VLRSPHMNLSGTAES EEECCCCCCCCCCCC | 28.20 | UniProtKB CARBOHYD | |
587 | O-linked_Glycosylation | DTGAEDSSGSSPATS CCCCCCCCCCCCCCC | 55.82 | - | |
600 | O-linked_Glycosylation | TSAIPFISENISQGY CCCCCCCCCCCCCCE | 25.60 | 55834893 | |
602 | N-linked_Glycosylation | AIPFISENISQGYIF CCCCCCCCCCCCEEE | 32.21 | UniProtKB CARBOHYD | |
604 | O-linked_Glycosylation | PFISENISQGYIFSS CCCCCCCCCCEEECC | 29.18 | 55834899 | |
629 | N-linked_Glycosylation | LIPESARNASEDSTS ECCHHHCCCCCCCCC | 47.75 | UniProtKB CARBOHYD | |
637 | O-linked_Glycosylation | ASEDSTSSGSEESLK CCCCCCCCCCHHHHC | 46.56 | - | |
637 | Phosphorylation | ASEDSTSSGSEESLK CCCCCCCCCCHHHHC | 46.56 | - | |
639 | Phosphorylation | EDSTSSGSEESLKDP CCCCCCCCHHHHCCC | 39.89 | - | |
677 | N-linked_Glycosylation | RESFLQTNYTEIRVD HHHHHCCCCEEEEEC | 28.86 | UniProtKB CARBOHYD | |
686 | O-linked_Glycosylation | TEIRVDESEKTTKSF EEEEECCCCCCCCCC | 39.67 | 55826247 | |
689 | O-linked_Glycosylation | RVDESEKTTKSFSAG EECCCCCCCCCCCCC | 35.09 | 55826253 | |
690 | O-linked_Glycosylation | VDESEKTTKSFSAGP ECCCCCCCCCCCCCC | 35.44 | 55826259 | |
700 | Phosphorylation | FSAGPVMSQGPSVTD CCCCCCCCCCCCCCC | 32.02 | 26657352 | |
721 | O-linked_Glycosylation | STFAYFPTEVTPHAF EEEEECCCCCCCCCC | 32.94 | 55828989 | |
724 | O-linked_Glycosylation | AYFPTEVTPHAFTPS EECCCCCCCCCCCCC | 11.79 | 55828995 | |
997 | O-linked_Glycosylation | LSGDGEWSGASSDSE CCCCCCCCCCCCCCC | 21.85 | - | |
1017 | N-linked_Glycosylation | TDGLTALNISSPVSV CCCCEEEECCCCCEE | 29.63 | UniProtKB CARBOHYD | |
1050 | N-linked_Glycosylation | KSEIIYGNETELQIP CCEEEECCCCEEECC | 35.72 | UniProtKB CARBOHYD | |
1082 | N-linked_Glycosylation | YDNVNKLNASLQETS HCCHHHHCHHHHHCE | 29.14 | UniProtKB CARBOHYD | |
1122 | N-linked_Glycosylation | ISQVPENNFSVQPTH HHCCCCCCCCCCCCC | 28.98 | UniProtKB CARBOHYD | |
1211 | Phosphorylation | SDPILVETPKVDKIS CCCEEECCCCCCCCC | 22.41 | - | |
1338 | O-linked_Glycosylation | IHSDEILTSTKSSVT HCCCHHHHCCCCCCC | 39.76 | 55831031 | |
1339 | O-linked_Glycosylation | HSDEILTSTKSSVTG CCCHHHHCCCCCCCC | 30.32 | 55831035 | |
1340 | O-linked_Glycosylation | SDEILTSTKSSVTGK CCHHHHCCCCCCCCC | 29.70 | 55831041 | |
1396 | O-linked_Glycosylation | STKLLFPSKATSELS EEEEECCCCCCCCCC | 27.82 | 55823807 | |
1399 | Phosphorylation | LLFPSKATSELSHSA EECCCCCCCCCCCCC | 26.86 | 28270605 | |
1400 | Phosphorylation | LFPSKATSELSHSAK ECCCCCCCCCCCCCC | 41.21 | 28270605 | |
1403 | Phosphorylation | SKATSELSHSAKSDA CCCCCCCCCCCCCCC | 16.02 | 28270605 | |
1405 | Phosphorylation | ATSELSHSAKSDAGL CCCCCCCCCCCCCCC | 33.73 | 28270605 | |
1421 | Phosphorylation | GGGEDGDTDDDGDDD CCCCCCCCCCCCCCC | 47.02 | - | |
1457 | N-linked_Glycosylation | ESQEKVMNDSDTHEN HHHHHHHCCCCHHCC | 48.93 | UniProtKB CARBOHYD | |
1478 | Phosphorylation | NPISYSLSENSEEDN CCCCEECCCCCCCCC | 28.88 | 25332170 | |
1481 | Phosphorylation | SYSLSENSEEDNRVT CEECCCCCCCCCCCE | 38.01 | 25332170 | |
1545 | Phosphorylation | KAWAVLTSDEESGSG CCEEEEECCCCCCCC | 38.57 | 29759185 | |
1549 | O-linked_Glycosylation | VLTSDEESGSGQGTS EEECCCCCCCCCCCC | 35.89 | - | |
1551 | O-linked_Glycosylation | TSDEESGSGQGTSDS ECCCCCCCCCCCCCC | 36.90 | - | |
1562 | N-linked_Glycosylation | TSDSLNENETSTDFS CCCCCCCCCCCCCCC | 57.69 | UniProtKB CARBOHYD | |
1618 | N-linked_Glycosylation | VSEAEASNSSHESRI ECHHHHCCCCCHHHH | 55.36 | UniProtKB CARBOHYD | |
1668 | Phosphorylation | YWRKCFQTAHFYLED HHHHHHCHHCEECCC | 11.22 | - | |
1672 | Phosphorylation | CFQTAHFYLEDSTSP HHCHHCEECCCCCCC | 10.18 | - | |
1683 | Phosphorylation | STSPRVISTPPTPIF CCCCCEECCCCCCCC | 31.81 | 25850435 | |
1684 | Phosphorylation | TSPRVISTPPTPIFP CCCCEECCCCCCCCC | 23.35 | 25850435 | |
1687 | Phosphorylation | RVISTPPTPIFPISD CEECCCCCCCCCCCC | 30.16 | 25850435 | |
1693 | Phosphorylation | PTPIFPISDDVGAIP CCCCCCCCCCCCCEE | 28.17 | 21406692 | |
1756 | Phosphorylation | DNKHKNRYINIVAYD CCCCCCCEEEEEEEC | 14.02 | 24173317 | |
1762 | Phosphorylation | RYINIVAYDHSRVKL CEEEEEEECCCHHHH | 11.86 | 24173317 | |
1871 | Phosphorylation | YYTVRNFTLRNTKIK EEEECCEEECCCEEC | 28.49 | 24719451 | |
1998 | Phosphorylation | EAILSKETEVLDSHI HHHHCCCCHHHHHHH | 34.82 | 24719451 | |
2021 | Phosphorylation | IPGPAGKTKLEKQFQ CCCCCCHHHHHHHHH | 39.69 | 24719451 | |
2031 | Phosphorylation | EKQFQLLSQSNIQQS HHHHHHHHHCCCCHH | 39.91 | 29978859 | |
2033 | Phosphorylation | QFQLLSQSNIQQSDY HHHHHHHCCCCHHHH | 32.31 | 29978859 | |
2038 | Phosphorylation | SQSNIQQSDYSAALK HHCCCCHHHHHHHHH | 23.34 | 29978859 | |
2040 | Phosphorylation | SNIQQSDYSAALKQC CCCCHHHHHHHHHHH | 12.88 | 29978859 | |
2041 | Phosphorylation | NIQQSDYSAALKQCN CCCHHHHHHHHHHHH | 16.44 | 29978859 | |
2054 | Phosphorylation | CNREKNRTSSIIPVE HHHHCCCCCCEEEEC | 35.90 | 20639409 | |
2055 | Phosphorylation | NREKNRTSSIIPVER HHHCCCCCCEEEECH | 19.12 | 8387522 | |
2056 | Phosphorylation | REKNRTSSIIPVERS HHCCCCCCEEEECHH | 24.75 | 20639409 | |
2179 | Phosphorylation | LEATQDDYVLEVRHF HHHHCCCEEEEEEEC | 18.41 | 24927040 | |
2199 | Phosphorylation | PNPDSPISKTFELIS CCCCCCCHHHHHHHH | 29.09 | - | |
2237 | Phosphorylation | AGTFCALTTLMHQLE HHHHHHHHHHHHHHH | 10.19 | 30377224 | |
2238 | Phosphorylation | GTFCALTTLMHQLEK HHHHHHHHHHHHHHH | 23.96 | 30377224 | |
2276 | Phosphorylation | IEQYQFLYKVILSLV HHHHHHHHHHHHHHH | 12.42 | - | |
2281 | Phosphorylation | FLYKVILSLVSTRQE HHHHHHHHHHHCCCC | 18.66 | 21712546 | |
2284 | Phosphorylation | KVILSLVSTRQEENP HHHHHHHHCCCCCCC | 24.14 | 22496350 | |
2285 | Phosphorylation | VILSLVSTRQEENPS HHHHHHHCCCCCCCC | 28.97 | 18452278 |
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 PTPRZ_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTPRZ_HUMAN !! |
* 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 PTPRZ_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CNTN1_HUMAN | CNTN1 | physical | 12700241 | |
CTNB1_HUMAN | CTNNB1 | physical | 10706604 | |
VEGFA_HUMAN | VEGFA | physical | 25644401 | |
PTN_HUMAN | PTN | physical | 25644401 |
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. |
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N-linked Glycosylation | |
Reference | PubMed |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASSSPECTROMETRY. |