CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021348
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine-protein phosphatase non-receptor type 23 
Protein Synonyms/Alias
 His domain-containing protein tyrosine phosphatase; HD-PTP; Protein tyrosine phosphatase TD14; PTP-TD14 
Gene Name
 PTPN23 
Gene Synonyms/Alias
 KIAA1471 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
32AVKKFVLKNYGENPEubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
46EAYNEELKKLELLRQubiquitination[2, 6]
47AYNEELKKLELLRQNubiquitination[6]
70EGCSVLRKYLGQLHYubiquitination[6]
215AQVVDYYKEACRALEubiquitination[3, 6]
235SLLGRIQKDWKKLVQubiquitination[7]
279YFQSALDKLNEAIKLubiquitination[1, 2, 5, 6, 7, 8]
285DKLNEAIKLAKGQPDubiquitination[2, 5, 6]
288NEAIKLAKGQPDTVQubiquitination[2, 6, 7]
308TMDVIGGKYNSAKKDubiquitination[6]
313GGKYNSAKKDNDFIYubiquitination[6]
314GKYNSAKKDNDFIYHubiquitination[6]
340VKGAPLVKPLPVNPTubiquitination[2, 6, 7]
1220IARCYSLKNRHQDVMubiquitination[6]
1635DPLWTLNKT******ubiquitination[6, 7]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
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. 
Sequence Annotation
 DOMAIN 8 394 BRO1.
 REPEAT 250 283 TPR 1.
 REPEAT 374 407 TPR 2.
 REPEAT 953 954 1.
 REPEAT 955 956 2.
 REPEAT 957 958 3.
 REPEAT 959 960 4.
 REPEAT 961 962 5.
 REPEAT 963 964 6.
 DOMAIN 1192 1452 Tyrosine-protein phosphatase.
 REGION 770 1130 His.
 REGION 953 964 6 X 2 AA approximate tandem repeats of P-
 ACT_SITE 1392 1392 Phosphocysteine intermediate (By
 MOD_RES 1123 1123 Phosphoserine.
 MOD_RES 1126 1126 Phosphoserine (By similarity).  
Keyword
 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase; Protein transport; Reference proteome; Repeat; TPR repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1636 AA 
Protein Sequence
MEAVPRMPMI WLDLKEAGDF HFQPAVKKFV LKNYGENPEA YNEELKKLEL LRQNAVRVPR 60
DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVPVTWTEIF SGKSVAHEDI KYEQACILYN 120
LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAYSVDMS RQILTLNVNL 180
MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL 240
VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF 300
TMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL 360
VPMAAHEASS LYSEEKAKLL REMMAKIEDK NEVLDQFMDS MQLDPETVDN LDAYSHIPPQ 420
LMEKCAALSV RPDTVRNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELLE QKFQEAVGQA 480
GAISITSKAE LAEVRREWAK YMEVHEKASF TNSELHRAMN LHVGNLRLLS GPLDQVRAAL 540
PTPALSPEDK AVLQNLKRIL AKVQEMRDQR VSLEQQLREL IQKDDITASL VTTDHSEMKK 600
LFEEQLKKYD QLKVYLEQNL AAQDRVLCAL TEANVQYAAV RRVLSDLDQK WNSTLQTLVA 660
SYEAYEDLMK KSQEGRDFYA DLESKVAALL ERTQSTCQAR EAARQQLLDR ELKKKPPPRP 720
TAPKPLLPRR EESEAVEAGD PPEELRSLPP DMVAGPRLPD TFLGSATPLH FPPSPFPSST 780
GPGPHYLSGP LPPGTYSGPT QLIQPRAPGP HAMPVAPGPA LYPAPAYTPE LGLVPRSSPQ 840
HGVVSSPYVG VGPAPPVAGL PSAPPPQFSG PELAMAVRPA TTTVDSIQAP IPSHTAPRPN 900
PTPAPPPPCF PVPPPQPLPT PYTYPAGAKQ PIPAQHHFSS GIPAGFPAPR IGPQPQPHPQ 960
PHPSQAFGPQ PPQQPLPLQH PHLFPPQAPG LLPPQSPYPY APQPGVLGQP PPPLHTQLYP 1020
GPAQDPLPAH SGALPFPSPG PPQPPHPPLA YGPAPSTRPM GPQAAPLTIR GPSSAGQSTP 1080
SPHLVPSPAP SPGPGPVPPR PPAAEPPPCL RRGAAAADLL SSSPESQHGG TQSPGGGQPL 1140
LQPTKVDAAE GRRPQALRLI ERDPYEHPER LRQLQQELEA FRGQLGDVGA LDTVWRELQD 1200
AQEHDARGRS IAIARCYSLK NRHQDVMPYD SNRVVLRSGK DDYINASCVE GLSPYCPPLV 1260
ATQAPLPGTA ADFWLMVHEQ KVSVIVMLVS EAEMEKQKVA RYFPTERGQP MVHGALSLAL 1320
SSVRSTETHV ERVLSLQFRD QSLKRSLVHL HFPTWPELGL PDSPSNLLRF IQEVHAHYLH 1380
QRPLHTPIIV HCSSGVGRTG AFALLYAAVQ EVEAGNGIPE LPQLVRRMRQ QRKHMLQEKL 1440
HLRFCYEAVV RHVEQVLQRH GVPPPCKPLA SASISQKNHL PQDSQDLVLG GDVPISSIQA 1500
TIAKLSIRPP GGLESPVASL PGPAEPPGLP PASLPESTPI PSSSPPPLSS PLPEAPQPKE 1560
EPPVPEAPSS GPPSSSLELL ASLTPEAFSL DSSLRGKQRM SKHNFLQAHN GQGLRATRPS 1620
DDPLSLLDPL WTLNKT 1636 
Gene Ontology
 GO:0005929; C:cilium; IEA:UniProtKB-KW.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0005932; C:microtubule basal body; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0060271; P:cilium morphogenesis; IMP: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; IMP: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.