CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014447
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase zeta 
Protein Synonyms/Alias
 R-PTP-zeta; 3F8 chondroitin sulfate proteoglycan; 3H1 keratan sulfate proteoglycan; Phosphacan 
Gene Name
 Ptprz1 
Gene Synonyms/Alias
 Ptprz; Ptpz 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
81NVNLKKLKFQGWEKPacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 May be involved in the regulation of specific developmental processes in the CNS. 
Sequence Annotation
 DOMAIN 36 300 Alpha-carbonic anhydrase.
 DOMAIN 311 406 Fibronectin type-III.
 DOMAIN 1718 1993 Tyrosine-protein phosphatase 1.
 DOMAIN 2024 2283 Tyrosine-protein phosphatase 2.
 REGION 1934 1940 Substrate binding (By similarity).
 ACT_SITE 1934 1934 Phosphocysteine intermediate (By
 BINDING 1902 1902 Substrate (By similarity).
 BINDING 1978 1978 Substrate (By similarity).
 MOD_RES 2056 2056 Phosphoserine (By similarity).
 CARBOHYD 105 105 N-linked (GlcNAc...) (Potential).
 CARBOHYD 134 134 N-linked (GlcNAc...) (Potential).
 CARBOHYD 223 223 N-linked (GlcNAc...) (Potential).
 CARBOHYD 232 232 N-linked (GlcNAc...) (Potential).
 CARBOHYD 324 324 N-linked (GlcNAc...) (Potential).
 CARBOHYD 381 381 N-linked (GlcNAc...) (Potential).
 CARBOHYD 497 497 N-linked (GlcNAc...) (Potential).
 CARBOHYD 552 552 N-linked (GlcNAc...) (Potential).
 CARBOHYD 595 595 O-linked (Xyl...) (chondroitin sulfate)
 CARBOHYD 610 610 N-linked (GlcNAc...) (Potential).
 CARBOHYD 645 645 O-linked (Xyl...) (chondroitin sulfate)
 CARBOHYD 685 685 N-linked (GlcNAc...) (Potential).
 CARBOHYD 786 786 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1005 1005 O-linked (Xyl...) (chondroitin sulfate)
 CARBOHYD 1025 1025 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1058 1058 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1463 1463 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1550 1550 O-linked (Xyl...) (chondroitin sulfate)
 CARBOHYD 1552 1552 O-linked (Xyl...) (chondroitin sulfate)
 CARBOHYD 1563 1563 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1611 1611 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1619 1619 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2316 AA 
Protein Sequence
MRILQSFLAC VQLLCVCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK 60
QSPINIDEDL TQVNVNLKKL KFQGWEKPSL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV 120
FKASKMTFHW GKCNVSSEGS EHSLEGQKFP LEMQIYCFDA DRFSSFEETV KGKGRLRALS 180
ILFEIGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFILQNL LPNSTDKYYI YNGSLTSPPC 240
TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY 300
TGKEEIHEAV CSSEPENVQA DPENYTSLLI TWERPRVVYD TMIEKFAVLY QPLEGNDQTK 360
HEFLTDGYQD LGAILNNLIP NMSYVLQIVA ICSNGLYGKY SDQLIVDMPT EDAELDLFPE 420
LIGTEEIIKE ENYGKGNEED TGLNPGRDSA TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN 480
RSPTRGSEFS GKSDVLNTSL NPTSQQVAEF NPEREMSLPS QIGTNLPPHS VEGTSASLNS 540
GSKTLLVFPQ MNLSGTAESL NMVSITEYKE VSADLSEEEN LLTDFKLDSG ADDSSGSSPA 600
SSTVPFSTDN LSHGYTSSSD TPEAVTYDVL RPESTRNALE DSAPSGSEES LKDPSLEGSV 660
WFPGSTDLTT QSETGSGREG FLQVNSTDFQ VDESRETTET FSPDATASRG PSVTDMEMPH 720
YSTFAYPPTE VTSHAFTPSS RPLDLAPTSN ILHSQTTQPV YNGETPLQPS YSSEVFPLVT 780
PLLLDNQTLN TTPAASSSDS ALHATPVFPS VGVSFDSILS SYDDAPLLPF SSASFSSDLF 840
HHLHTVSQTL PQVTSAAERD ELSLHASLLV AGGDLLLEPS LVQYSDVMSH QVTIHAASDT 900
LEFGSESAVL YKTSMVSQIE SPSSDVVMHA YSSGPETSYA IEGSHHVLTV SSSSAIPVHD 960
SVGVADQGSL LINPSHISLP ESSFITPTAS LLQLPPALSG DGEWSGASSD SELLLPDTDG 1020
LRTLNMSSPV SVADFTYTTS VSGDDIKPLS KGEMMYGNET ELKMSSFSDM AYPSKSTVVP 1080
KMSDIVNKWS ESLKETSVSV SSINSVFTES LVYPITKVFD QEISRVPEII FPVKPTHTAS 1140
QASGDTWLKP GLSTNSEPAL SDTASSEVSH PSTQPLLYEA ASPFNTEALL QPSFPASDVD 1200
TLLKTALPSG PRDPVLTETP MVEQSSSSVS LPLASESASS KSTLHFTSVP VLNMSPSDVH 1260
PTSLQRLTVP HSREEYFEQG LLKSKSPQQV LPSLHSHDEF FQTAHLDISQ AYPPKGRHAF 1320
ATPILSINEP QNTLINRLVY SEDIFMHPEI SITDKALTGL PTTVSDVLIA TDHSVPLGSG 1380
PISMTTVSPN RDDSVTTTKL LLPSKATSKP THSARSDADL VGGGEDGDDY DDDDYDDIDS 1440
DRFPVNKCMS CSPYRESQEK VMNDSDTQES SLVDQSDPIS HLLSENTEEE NGGTGVTRVD 1500
KSPDKSPPPS MLPQKHNDGR EDRDIQMGSA VLPHTPGSKA WAVLTSDEES GSGQGTSDSL 1560
NDNETSTDFS FPDVNEKDAD GVLEADDTGI APGSPRSSTP SVTSGHSGVS NSSEAEASNS 1620
SHESRIGLAE GLESEKKAVI PLVIVSALTF ICLVVLVGIL IYWRKCFQTA HFYLEDNTSP 1680
RVISTPPTPI FPISDDIGAI PIKHFPKHVA DLHASNGFTE EFETLKEFYQ EVQSCTVDLG 1740
ITADSSNHPD NKHKNRYVNI VAYDHSRVKL TQLAEKDGKL TDYINANYVD GYNRPKAYIA 1800
AQGPLKSTAE DFWRMIWEHN VEVIVMITNL VEKGRRKCDQ YWPTDGSEEY GSFLVNQKNV 1860
QVLAYYTVRN FTLRNTKIKK GSQKGRSSGR LVTQYHYTQW PDMGVPEYSL PVLAFVRKTA 1920
QAKRHAVGPV VVHCSAGVGR TGTYIVLDSM LQQIQHEGTV NIFGFLKHIR SQRNYLVQTE 1980
EQYVFIHDTL VEAILSKETE VPDSHIHSYV NTLLIPGPSG KTKLEKQFQL LSQSNILQSD 2040
YSTALKQCNR EKNRTSSIIP VERSRVGISS LSGEGTDYIN ASYIMGYYQS NEFIITQHPL 2100
LHTIKDFWRM IWDHNAQLVV MIPDGQNMAE DEFVYWPNKD EPINCESFKV TLMSEEHKCL 2160
SNEEKLIVQD FILEATQDDY VLEVRHFQCP KWPNPDSPIS KTFELISIIK EEAANRDGPM 2220
IVHDEHGGVT AGTFCALTTL MHQLEKENSM DVYQVAKMIN LMRPGVFTDI EQYQFLYKVV 2280
LSLVSTRQEE NPSTSLDSNG AALPDGNIAE SLESLV 2316 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC. 
Interpro
 IPR001148; Carbonic_anhydrase_a.
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00194; Carb_anhydrase
 PF00041; fn3
 PF00102; Y_phosphatase 
SMART
 SM01057; Carb_anhydrase
 SM00060; FN3
 SM00194; PTPc 
PROSITE
 PS51144; ALPHA_CA_2
 PS50853; FN3
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.