CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015242
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein phosphatase non-receptor type 23 
Protein Synonyms/Alias
  
Gene Name
 Ptpn23 
Gene Synonyms/Alias
 Kiaa1471 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
32AVKKFVLKNYGENPEubiquitination[1]
215AQVVDYYKEACRALEacetylation[2]
279YFQSALDKLNEAIKLubiquitination[1]
285DKLNEAIKLAKGQPDacetylation[3]
285DKLNEAIKLAKGQPDsuccinylation[3]
285DKLNEAIKLAKGQPDubiquitination[1]
288NEAIKLAKGQPDTVQubiquitination[1]
340VKGAPLVKPLPVNPTubiquitination[1]
502EVRREWAKYMEVHEKubiquitination[1]
559KAVLQNLKRILAKVQacetylation[4]
602TDHSEMKKLFEEQLKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753
Functional Description
 Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a role in ciliogenesis (By similarity). 
Sequence Annotation
 DOMAIN 8 394 BRO1.
 REPEAT 250 283 TPR 1.
 REPEAT 374 407 TPR 2.
 REPEAT 977 978 1.
 REPEAT 979 980 2.
 REPEAT 981 982 3.
 REPEAT 983 984 4.
 REPEAT 985 986 5.
 REPEAT 987 988 6.
 REPEAT 989 990 7.
 REPEAT 991 992 8.
 REPEAT 993 994 9.
 REPEAT 995 996 10.
 REPEAT 997 998 11.
 REPEAT 999 1000 12.
 REPEAT 1001 1002 13.
 REPEAT 1003 1004 14.
 REPEAT 1005 1006 15.
 REPEAT 1007 1008 16.
 REPEAT 1009 1010 17.
 REPEAT 1011 1012 18.
 REPEAT 1013 1014 19.
 REPEAT 1015 1016 20.
 REPEAT 1017 1018 21.
 DOMAIN 1248 1508 Tyrosine-protein phosphatase.
 REGION 773 1186 His.
 REGION 977 1018 21 X 2 AA approximate tandem repeats of
 ACT_SITE 1448 1448 Phosphocysteine intermediate (By
 MOD_RES 1179 1179 Phosphoserine (By similarity).
 MOD_RES 1182 1182 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome; Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase; Protein transport; Reference proteome; Repeat; TPR repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1692 AA 
Protein Sequence
MEAVPRMPMI WLDLKEAGDF HFQSAVKKFV LKNYGENPEA YNEELKKLEL LRQNAIRVAR 60
DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVAVTWTEIF SGKSVSHEDI KYEQACILYN 120
LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAFSVDMS RQILTLNVNL 180
MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL 240
VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF 300
AMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL 360
VPMAAHEASS LYSEEKAKLL REMLAKIEDK NEVLDQFMDS MQLDPETVDN LDAYNHIPPQ 420
LMEKCAALSV RPDTVKNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELQE QKLQETLGQA 480
GAGPGPSVAK AELAEVRREW AKYMEVHEKA SFTNSELHRA MNLHVGNLRL LSGPLDQVRA 540
ALPTPALTPE DKAVLQNLKR ILAKVQEMRD QRVSLEQQLR ELIQKDDITA SLVTTDHSEM 600
KKLFEEQLKK YDQLKVYLEQ NLAAQDNVLR ALTEANVQYA AVRRVLSELD QKWNSTLQTL 660
VASYEAYEDL MKKSQEGKDF YADLESKVAT LLERAQSICR AQEAARQQLL DRELKKKAPP 720
PRPTAPKPLL SRREEGEAVE AGDTPEELRS LPPDMMVGPR LPDPFLGTTA PLHFSPGPFP 780
SSTGPATHYL SGPLPPGTYS GPTQLMQPRA AVPMAPATVL YPAPAYTSEL GLVPRSSPQH 840
GIVSSPYAGV GPPQPVVGLP SAPPPQLSGP ELAMTVRPAT TTVDSVQAPI SSHTAPRPNP 900
TPALPQPCFP VPQPVPQSVP QPQPLPVPYT YSIGTKQPLP APYTYSIGTK QHLTGPLPQH 960
QFPPGIPTGF PVPRTGPQAQ AQPQPQPQPQ PQPQPQPQPQ PQPQSQSQPQ PQPQPQPQRP 1020
AFGPQPTQQP LPFQHPHLFP SQAPGILPPP PPTPYHFTPQ PGVLGQPPPT LHTQLYPGPS 1080
QDPLPPHSGA LPFPSPGPPH PHPTLAYGPA PSPRPLGPQA TPVSIRGPPP ASQPTPSPHL 1140
VPSPAPSPGP GPVPSRPPTA EPPPCLRRGA AAADLLSSSP ESQHGGTQPP GGGQPLLQPT 1200
KVDAAEGRRP QALRLIEQDP YEHPERLQQL QQELEAFRGQ LGDAGALDAI WRELQEAQEH 1260
DARGRSIAIA RCYSLKNRHQ DVMPYDSNRV VLRSGKDDYI NASCVEGLSP YCPPLVATQA 1320
PLPGTAADFW LMVHEQKVSV IVMLVSEAEM EKQKVARYFP TERGQPMVHG ALSVALSSIR 1380
TTETHVERVL SLQFRDQSLK RSLVHLHFPT WPELGLPDSP GNLLRFIQEV HAHYLHQRPL 1440
HTPIVVHCSS GVGRTGAFAL LYAAVQEVEA GNGIPELPQL VRRMRQQRKH MLQEKLHLKF 1500
CHEALVRHVE QVLQRHGVPP PGKPVASVNI SQKNHLPQDS QDLVLGGDVP ISSIQATIAK 1560
LSIRPLGGLD SPAASLPGLV EPPGLPPASL PESTPVPSSS PPPLSSPLPE APQPEEEPSV 1620
PEAPSLGPPS SSLELLASLT PEAFSLDSSL RGKQRMSKQN FLQAHNGQGL RAAQPTDDPL 1680
SLLDPLWTLN KT 1692 
Gene Ontology
 GO:0005929; C:cilium; IEA:UniProtKB-KW.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005769; C:early endosome; ISS:UniProtKB.
 GO:0005932; C:microtubule basal body; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0060271; P:cilium morphogenesis; ISS:UniProtKB.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB. 
Interpro
 IPR025304; ALIX_V_dom.
 IPR004328; BRO1_dom.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF13949; ALIX_LYPXL_bnd
 PF03097; BRO1
 PF00102; Y_phosphatase 
SMART
 SM01041; BRO1
 SM00194; PTPc 
PROSITE
 PS51180; BRO1
 PS50005; TPR
 PS50293; TPR_REGION
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.