CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010902
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inositol polyphosphate 5-phosphatase OCRL-1 
Protein Synonyms/Alias
 Lowe oculocerebrorenal syndrome protein 
Gene Name
 OCRL 
Gene Synonyms/Alias
 INPP5F; OCRL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
127QLLVPEQKDSSSWYQubiquitination[1, 2]
135DSSSWYQKLDTKDKPubiquitination[3]
351VGTGIMGKMGNKGGVubiquitination[2]
391ERRNQDYKDICARMSubiquitination[3, 4]
449KDLQRLLKFDQLNIQubiquitination[1]
461NIQRTQKKAFVDFNEubiquitination[1, 4]
578EFVFENVKFRQLQKEubiquitination[1]
612LNDSQYCKPWLRAEPubiquitination[3]
701IREVPVTKLIDLEEDubiquitination[1]
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] 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]
 [4] 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
Functional Description
 Converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. Also converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate and inositol 1,3,4,5- tetrakisphosphate to inositol 1,3,4-trisphosphate. May function in lysosomal membrane trafficking by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with lysosomes. Involved in primary cilia assembly. 
Sequence Annotation
 DOMAIN 1 119 PH.
 DOMAIN 721 901 Rho-GAP.
 REGION 237 563 5-phosphatase.
 REGION 564 678 ASH.
 MOTIF 73 77 Clathrin box 1.
 MOTIF 702 706 Clathrin box 2.  
Keyword
 3D-structure; Alternative splicing; Cataract; Cell projection; Ciliopathy; Cilium; Cilium biogenesis/degradation; Coated pit; Complete proteome; Cytoplasmic vesicle; Disease mutation; Endosome; Golgi apparatus; Hydrolase; Membrane; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 901 AA 
Protein Sequence
MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ HVQDIIPINS 60
HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD EEHCLKFLSA VLAAQKAQSQ 120
LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG FEDNFSSMNL DKKINSQNQP TGIHREPPPP 180
PFSVNKMLPR EKEASNKEQP KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF 240
RFFVGTWNVN GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA 300
VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG KMGNKGGVAV 360
RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV VPNQTLPQLN IMKHEVVIWL 420
GDLNYRLCMP DANEVKSLIN KKDLQRLLKF DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD 480
SKTDRWDSSG KCRVPAWCDR ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE 540
RRYRKVFEDS VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS 600
FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE DKIEDILVLH 660
LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT KLIDLEEDSF LEKEKSLLQM 720
VPLDEGASER PLQVPKEIWL LVDHLFKYAC HQEDLFQTPG MQEELQQIID CLDTSIPETI 780
PGSNHSVAEA LLIFLEALPE PVICYELYQR CLDSAYDPRI CRQVISQLPR CHRNVFRYLM 840
AFLRELLKFS EYNSVNANMI ATLFTSLLLR PPPNLMARQT PSDRQRAIQF LLGFLLGSEE 900
D 901 
Gene Ontology
 GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
 GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005769; C:early endosome; IDA:UniProtKB.
 GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005795; C:Golgi stack; TAS:ProtInc.
 GO:0005798; C:Golgi-associated vesicle; TAS:ProtInc.
 GO:0005634; C:nucleus; IDA:FlyBase.
 GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:FlyBase.
 GO:0005802; C:trans-Golgi network; IDA:FlyBase.
 GO:0052745; F:inositol phosphate phosphatase activity; NAS:UniProtKB.
 GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; TAS:ProtInc.
 GO:0030675; F:Rac GTPase activator activity; IDA:FlyBase.
 GO:0042384; P:cilium assembly; IMP:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
 GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
 GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:Compara.
 GO:0032314; P:regulation of Rac GTPase activity; IDA:FlyBase.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. 
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