CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006040
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Type II inositol 1,4,5-trisphosphate 5-phosphatase 
Protein Synonyms/Alias
 75 kDa inositol polyphosphate-5-phosphatase; Phosphoinositide 5-phosphatase; 5PTase 
Gene Name
 INPP5B 
Gene Synonyms/Alias
 OCRL2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
312STITVSDKAHILSMQubiquitination[1, 2, 3]
360NVNGQSPKECLRLWLubiquitination[2]
404PKEEEWFKAVSEGLHubiquitination[1, 3]
496ERRNQDYKDICSRMQubiquitination[2]
542LDVEKVKKLIEEKDFubiquitination[2]
547VKKLIEEKDFQMLYAubiquitination[2]
596DDWDTSEKCRAPAWCubiquitination[2, 4]
630ALKTSDHKPVSSVFDubiquitination[2]
650VNDELYRKTLEEIVRubiquitination[2]
674IPSVSLSKREFCFQNubiquitination[2, 5]
972RNPAGHQKLDMTEKKubiquitination[2, 5]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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
Functional Description
 Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. 
Sequence Annotation
 DOMAIN 22 148 PH.
 DOMAIN 821 993 Rho-GAP.
 REGION 342 668 5-phosphatase (By similarity).
 REGION 459 460 Substrate binding.
 REGION 582 583 Substrate binding.
 REGION 596 598 Substrate binding.
 REGION 669 782 ASH (By similarity).
 METAL 355 355 Magnesium.
 METAL 383 383 Magnesium.
 BINDING 383 383 Substrate.
 MOD_RES 990 990 Cysteine methyl ester (Potential).
 LIPID 990 990 S-farnesyl cysteine (Potential).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Endosome; Golgi apparatus; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding; Methylation; Polymorphism; Prenylation; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 993 AA 
Protein Sequence
MDQSVAIQET LAEGEYCVIA VQGVLCEGDS RQSRLLGLVR YRLEHGGQEH ALFLYTHRRM 60
AITGDDVSLD QIVPVSRDFT LEEVSPDGEL YILGSDVTVQ LDTAELSLVF QLPFGSQTRM 120
FLHEVARACP GFDSATRDPE FLWLSRYRCA ELELEMPTPR GCNSALVTWP GYATIGGGRY 180
PSRKKRWGLE EARPQGAGSV LFWGGAMEKT GFRLMERAHG GGFVWGRSAR DGRRDEELEE 240
AGREMSAAAG SRERNTAGGS NFDGLRPNGK GVPMDQSSRG QDKPESLQPR QNKSKSEITD 300
MVRSSTITVS DKAHILSMQK FGLRDTIVKS HLLQKEEDYT YIQNFRFFAG TYNVNGQSPK 360
ECLRLWLSNG IQAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSEGL HPDAKYAKVK 420
LIRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQFH NTSICVVNSH 480
LAAHIEEYER RNQDYKDICS RMQFCQPDPS LPPLTISNHD VILWLGDLNY RIEELDVEKV 540
KKLIEEKDFQ MLYAYDQLKI QVAAKTVFEG FTEGELTFQP TYKYDTGSDD WDTSEKCRAP 600
AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNDELYRK TLEEIVRSLD 660
KMENANIPSV SLSKREFCFQ NVKYMQLKVE SFTIHNGQVP CHFEFINKPD EESYCKQWLN 720
ANPSRGFLLP DSDVEIDLEL FVNKMTATKL NSGEDKIEDI LVLHLDRGKD YFLSVSGNYL 780
PSCFGSPIHT LCYMREPILD LPLETISELT LMPVWTGDDG SQLDSPMEIP KELWMMVDYL 840
YRNAVQQEDL FQQPGLRSEF EHIRDCLDTG MIDNLSASNH SVAEALLLFL ESLPEPVICY 900
STYHNCLECS GNYTASKQVI STLPIFHKNV FHYLMAFLRE LLKNSAKNHL DENILASIFG 960
SLLLRNPAGH QKLDMTEKKK AQEFIHQFLC NPL 993 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:Compara.
 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
 GO:0070613; P:regulation of protein processing; IEA:Compara.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
 GO:0030317; P:sperm motility; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR005135; Endo/exonuclease/phosphatase.
 IPR000300; IPPc.
 IPR008936; Rho_GTPase_activation_prot.
 IPR000198; RhoGAP_dom. 
Pfam
 PF03372; Exo_endo_phos
 PF00620; RhoGAP 
SMART
 SM00128; IPPc
 SM00324; RhoGAP 
PROSITE
 PS50003; PH_DOMAIN
 PS50238; RHOGAP 
PRINTS