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Q01968

- OCRL_HUMAN

UniProt

Q01968 - OCRL_HUMAN

Protein

Inositol polyphosphate 5-phosphatase OCRL-1

Gene

OCRL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 3 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate.

    GO - Molecular functioni

    1. inositol phosphate phosphatase activity Source: UniProtKB
    2. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: ProtInc
    3. protein binding Source: UniProtKB
    4. Rac GTPase activator activity Source: FlyBase
    5. Rac GTPase binding Source: FlyBase

    GO - Biological processi

    1. cilium assembly Source: UniProtKB
    2. inositol phosphate metabolic process Source: Reactome
    3. in utero embryonic development Source: Ensembl
    4. lipid metabolic process Source: UniProtKB
    5. phosphatidylinositol biosynthetic process Source: Reactome
    6. phosphatidylinositol dephosphorylation Source: Ensembl
    7. phospholipid metabolic process Source: Reactome
    8. positive regulation of Rac GTPase activity Source: GOC
    9. regulation of Rac GTPase activity Source: FlyBase
    10. regulation of small GTPase mediated signal transduction Source: Reactome
    11. small GTPase mediated signal transduction Source: Reactome
    12. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04546-MONOMER.
    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_120836. Synthesis of PIPs at the Golgi membrane.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    SignaLinkiQ01968.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol polyphosphate 5-phosphatase OCRL-1 (EC:3.1.3.36)
    Alternative name(s):
    Lowe oculocerebrorenal syndrome protein
    Gene namesi
    Name:OCRL
    Synonyms:INPP5F, OCRL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8108. OCRL.

    Subcellular locationi

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: UniProtKB
    2. coated pit Source: UniProtKB-SubCell
    3. cytoplasm Source: FlyBase
    4. cytosol Source: Reactome
    5. early endosome Source: UniProtKB
    6. early endosome membrane Source: UniProtKB-SubCell
    7. extracellular vesicular exosome Source: UniProt
    8. Golgi-associated vesicle Source: ProtInc
    9. Golgi stack Source: ProtInc
    10. nucleus Source: FlyBase
    11. phagocytic vesicle membrane Source: UniProtKB-SubCell
    12. photoreceptor outer segment Source: UniProtKB
    13. plasma membrane Source: FlyBase
    14. trans-Golgi network Source: FlyBase

    Keywords - Cellular componenti

    Cell projection, Cilium, Coated pit, Cytoplasmic vesicle, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Lowe oculocerebrorenal syndrome (OCRL) [MIM:309000]: X-linked multisystem disorder affecting eyes, nervous system, and kidney. It is characterized by hydrophthalmia, cataract, mental retardation, vitamin D-resistant rickets, aminoaciduria, and reduced ammonia production by the kidney. Ocular abnormalities include cataract, glaucoma, microphthalmos, and decreased visual acuity. Developmental delay, hypotonia, behavior abnormalities, and areflexia are also present. Renal tubular involvement is characterized by impaired reabsorption of bicarbonate, amino acids, and phosphate. Musculoskeletal abnormalities such as joint hypermobility, dislocated hips, and fractures may develop as consequences of renal tubular acidosis and hypophosphatemia. Cataract is the only significant manifestation in carriers and is detected by slit-lamp examination.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti242 – 2421F → S in OCRL. 1 Publication
    Corresponds to variant rs137853828 [ dbSNP | Ensembl ].
    VAR_064773
    Natural varianti274 – 2741I → T in OCRL. 1 Publication
    Corresponds to variant rs137853829 [ dbSNP | Ensembl ].
    VAR_064774
    Natural varianti277 – 2771Q → R in OCRL. 1 Publication
    Corresponds to variant rs137853830 [ dbSNP | Ensembl ].
    VAR_064775
    Natural varianti318 – 3181R → C in DD2 and OCRL. 3 Publications
    Corresponds to variant rs137853263 [ dbSNP | Ensembl ].
    VAR_022698
    Natural varianti337 – 3371R → C in OCRL; associated with I-361. 1 Publication
    Corresponds to variant rs137853831 [ dbSNP | Ensembl ].
    VAR_064776
    Natural varianti337 – 3371R → P in OCRL.
    VAR_010169
    Natural varianti357 – 3571G → E in OCRL; uncertain pathological significance. 1 Publication
    Corresponds to variant rs137853854 [ dbSNP | Ensembl ].
    VAR_010170
    Natural varianti361 – 3611R → I in OCRL; associated with C-337. 1 Publication
    Corresponds to variant rs137853832 [ dbSNP | Ensembl ].
    VAR_064778
    Natural varianti367 – 3671Missing in OCRL. 1 Publication
    VAR_010171
    Natural varianti372 – 3721V → G in OCRL. 1 Publication
    Corresponds to variant rs137853834 [ dbSNP | Ensembl ].
    VAR_010172
    Natural varianti373 – 3731N → Y in OCRL. 1 Publication
    Corresponds to variant rs137853835 [ dbSNP | Ensembl ].
    VAR_064779
    Natural varianti374 – 3741S → F in OCRL. 1 Publication
    Corresponds to variant rs137853836 [ dbSNP | Ensembl ].
    VAR_064780
    Natural varianti375 – 3751H → Y in OCRL. 1 Publication
    Corresponds to variant rs137853848 [ dbSNP | Ensembl ].
    VAR_010173
    Natural varianti414 – 4141H → R in OCRL. 1 Publication
    Corresponds to variant rs137853837 [ dbSNP | Ensembl ].
    VAR_064781
    Natural varianti421 – 4211G → E in OCRL. 1 Publication
    Corresponds to variant rs137853855 [ dbSNP | Ensembl ].
    VAR_010174
    Natural varianti424 – 4241N → D in OCRL. 1 Publication
    Corresponds to variant rs137853856 [ dbSNP | Ensembl ].
    VAR_010175
    Natural varianti451 – 4511D → G in OCRL. 1 Publication
    Corresponds to variant rs137853850 [ dbSNP | Ensembl ].
    VAR_010176
    Natural varianti451 – 4511D → N in OCRL. 1 Publication
    Corresponds to variant rs137853838 [ dbSNP | Ensembl ].
    VAR_064782
    Natural varianti457 – 4571R → G in OCRL. 1 Publication
    Corresponds to variant rs137853839 [ dbSNP | Ensembl ].
    VAR_064783
    Natural varianti463 – 4631F → S in OCRL. 1 Publication
    Corresponds to variant rs137853851 [ dbSNP | Ensembl ].
    VAR_010177
    Natural varianti468 – 4681E → G in OCRL. 1 Publication
    Corresponds to variant rs137853841 [ dbSNP | Ensembl ].
    VAR_064784
    Natural varianti468 – 4681E → K in OCRL. 1 Publication
    Corresponds to variant rs137853840 [ dbSNP | Ensembl ].
    VAR_064785
    Natural varianti478 – 4792Missing in OCRL.
    VAR_023957
    Natural varianti495 – 4951P → L in OCRL. 1 Publication
    VAR_064787
    Natural varianti498 – 4981C → Y in OCRL. 1 Publication
    Corresponds to variant rs137853857 [ dbSNP | Ensembl ].
    VAR_010178
    Natural varianti499 – 4991D → H in OCRL. 1 Publication
    Corresponds to variant rs137853842 [ dbSNP | Ensembl ].
    VAR_064788
    Natural varianti500 – 5001R → G in OCRL.
    VAR_010179
    Natural varianti500 – 5001R → Q in OCRL. 3 Publications
    Corresponds to variant rs137853260 [ dbSNP | Ensembl ].
    VAR_010180
    Natural varianti503 – 5031W → R in OCRL. 1 Publication
    Corresponds to variant rs137853843 [ dbSNP | Ensembl ].
    VAR_064789
    Natural varianti508 – 5081V → D in OCRL. 1 Publication
    Corresponds to variant rs137853849 [ dbSNP | Ensembl ].
    VAR_010181
    Natural varianti513 – 5131Y → C in OCRL. 1 Publication
    Corresponds to variant rs137853847 [ dbSNP | Ensembl ].
    VAR_010182
    Natural varianti522 – 5221S → R in OCRL. 1 Publication
    Corresponds to variant rs137853853 [ dbSNP | Ensembl ].
    VAR_010183
    Natural varianti524 – 5241H → Q in OCRL. 1 Publication
    Corresponds to variant rs137853261 [ dbSNP | Ensembl ].
    VAR_010184
    Natural varianti524 – 5241H → R in OCRL. 1 Publication
    Corresponds to variant rs137853852 [ dbSNP | Ensembl ].
    VAR_010185
    Natural varianti526 – 5261P → L in OCRL. 1 Publication
    Corresponds to variant rs137853858 [ dbSNP | Ensembl ].
    VAR_023958
    Natural varianti533 – 5331I → S in OCRL.
    VAR_010187
    Natural varianti591 – 5911N → K in OCRL. 2 Publications
    Corresponds to variant rs137853844 [ dbSNP | Ensembl ].
    VAR_064790
    Natural varianti742 – 7421Missing in OCRL. 1 Publication
    VAR_064791
    Natural varianti768 – 7681I → N in OCRL; uncertain pathological significance; abolishes FAM109A-binding; does not affect clathrin-binding. 2 Publications
    VAR_010188
    Natural varianti797 – 7971A → P in OCRL; uncertain pathological significance; abolishes FAM109A-, FAM109B- and APPL1-binding; does not affect clathrin-binding. 2 Publications
    VAR_010189
    Natural varianti801 – 8011P → L in OCRL. 1 Publication
    VAR_064793
    Natural varianti891 – 8911L → R in OCRL. 1 Publication
    Corresponds to variant rs137853845 [ dbSNP | Ensembl ].
    VAR_064794
    Dent disease 2 (DD2) [MIM:300555]: A renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Characteristic abnormalities include low-molecular-weight proteinuria and other features of Fanconi syndrome, such as glycosuria, aminoaciduria, and phosphaturia, but typically do not include proximal renal tubular acidosis. Progressive renal failure is common, as are nephrocalcinosis and kidney stones.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti318 – 3181R → C in DD2 and OCRL. 3 Publications
    Corresponds to variant rs137853263 [ dbSNP | Ensembl ].
    VAR_022698
    Natural varianti354 – 3541N → H in DD2. 1 Publication
    Corresponds to variant rs137853833 [ dbSNP | Ensembl ].
    VAR_064777
    Natural varianti479 – 4791Y → C in DD2. 1 Publication
    Corresponds to variant rs137853262 [ dbSNP | Ensembl ].
    VAR_022699
    Natural varianti493 – 4931R → W in DD2. 1 Publication
    Corresponds to variant rs137853846 [ dbSNP | Ensembl ].
    VAR_064786
    Natural varianti799 – 7991P → L in DD2. 1 Publication
    VAR_064792

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi422 – 4221D → A: Does not affect interaction with RAB8A. 1 Publication
    Mutagenesisi499 – 4991D → A: Does not affect interaction with RAB8A. 1 Publication
    Mutagenesisi668 – 6681F → V: Does not interact with RAB8A. Does not localize to cilia. 1 Publication

    Keywords - Diseasei

    Cataract, Ciliopathy, Disease mutation

    Organism-specific databases

    MIMi300555. phenotype.
    309000. phenotype.
    Orphaneti93623. Dent disease type 2.
    534. Oculocerebrorenal syndrome.
    PharmGKBiPA31896.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 901901Inositol polyphosphate 5-phosphatase OCRL-1PRO_0000209721Add
    BLAST

    Proteomic databases

    MaxQBiQ01968.
    PaxDbiQ01968.
    PRIDEiQ01968.

    PTM databases

    PhosphoSiteiQ01968.

    Expressioni

    Tissue specificityi

    Brain, skeletal muscle, heart, kidney, lung, placenta and fibroblasts. Expressed in the retina and the retinal pigment epithelium.1 Publication

    Gene expression databases

    BgeeiQ01968.
    CleanExiHS_INPP5F.
    GenevestigatoriQ01968.

    Organism-specific databases

    HPAiHPA012495.

    Interactioni

    Subunit structurei

    Interacts with APPL1, FAM109A/SES1 and FAM109B/SES2; APPL1-binding and FAM109A-binding are mutually exclusive. Interacts with clathrin heavy chain. Interacts with several Rab GTPases, at least RAB1B, RAB5A, RAB6A, RAB8A and RAB31; these interactions may play a dual role in targeting OCRL to the specific membranes and stimulating the phosphatase activity. Interaction with RAB8A modulates OCRL recruitment to cilia.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLTCQ006104EBI-6148898,EBI-354967
    CltcP114425EBI-6148898,EBI-397997From a different organism.
    RAB14P611063EBI-6148898,EBI-1056404
    RAB1AP628207EBI-6148898,EBI-716845
    RAB1BQ9H0U42EBI-6148898,EBI-1045214
    RAB5AP2033910EBI-6148898,EBI-399437
    RAB6AP2034011EBI-6148898,EBI-1052826
    RAB8AP6100611EBI-6148898,EBI-722293
    RAC1P630003EBI-6148898,EBI-413628

    Protein-protein interaction databases

    BioGridi111006. 6 interactions.
    IntActiQ01968. 21 interactions.
    MINTiMINT-5004450.

    Structurei

    Secondary structure

    1
    901
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 2112
    Beta strandi24 – 3512
    Beta strandi38 – 458
    Beta strandi52 – 576
    Beta strandi59 – 613
    Beta strandi63 – 708
    Helixi76 – 783
    Beta strandi80 – 9011
    Beta strandi94 – 985
    Helixi101 – 11818
    Helixi222 – 2298
    Helixi231 – 2344
    Beta strandi235 – 24814
    Helixi259 – 2624
    Beta strandi265 – 2673
    Beta strandi270 – 2778
    Helixi283 – 2864
    Helixi292 – 30413
    Beta strandi311 – 3199
    Beta strandi322 – 3298
    Helixi332 – 3354
    Beta strandi336 – 34510
    Helixi348 – 3503
    Beta strandi355 – 36410
    Beta strandi367 – 3759
    Helixi383 – 39614
    Helixi411 – 4133
    Beta strandi414 – 4229
    Helixi432 – 4409
    Helixi444 – 4485
    Helixi452 – 4587
    Beta strandi461 – 4633
    Beta strandi483 – 4864
    Beta strandi489 – 4913
    Beta strandi499 – 5046
    Beta strandi506 – 5105
    Beta strandi521 – 5244
    Beta strandi527 – 53812
    Helixi553 – 5608
    Beta strandi565 – 5684
    Beta strandi571 – 5777
    Beta strandi583 – 5919
    Beta strandi593 – 5953
    Beta strandi597 – 6026
    Beta strandi608 – 6114
    Beta strandi615 – 6195
    Beta strandi621 – 6244
    Beta strandi629 – 6368
    Helixi640 – 6489
    Beta strandi649 – 6513
    Beta strandi655 – 6617
    Beta strandi666 – 67510
    Helixi684 – 6896
    Helixi700 – 7023
    Helixi736 – 74813
    Turni753 – 7575
    Helixi762 – 77413
    Helixi784 – 79714
    Helixi805 – 81410
    Helixi818 – 8269
    Helixi830 – 84718
    Helixi850 – 8534
    Helixi857 – 86812
    Helixi873 – 8753
    Helixi883 – 89513

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KIENMR-A1-119[»]
    2QV2X-ray2.40A564-901[»]
    3QBTX-ray2.00B/D/F/H540-678[»]
    3QISX-ray2.30A536-901[»]
    4CMNX-ray3.13A215-560[»]
    ProteinModelPortaliQ01968.
    SMRiQ01968. Positions 1-119, 234-538, 540-898.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01968.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 119119PHAdd
    BLAST
    Domaini721 – 901181Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni237 – 5633275-phosphataseAdd
    BLAST
    Regioni564 – 678115ASHAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi73 – 775Clathrin box 1
    Motifi702 – 7065Clathrin box 2

    Domaini

    The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by FAM109A and FAM109B as endosomes mature.1 Publication

    Sequence similaritiesi

    Contains 1 PH domain.Curated
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5411.
    HOVERGENiHBG000070.
    InParanoidiQ01968.
    KOiK01099.
    OMAiAKYKKVQ.
    OrthoDBiEOG7J4465.
    PhylomeDBiQ01968.
    TreeFamiTF317034.

    Family and domain databases

    Gene3Di1.10.555.10. 2 hits.
    3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00128. IPPc. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 2 hits.
    SSF56219. SSF56219. 1 hit.
    PROSITEiPS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q01968-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ    50
    HVQDIIPINS HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD 100
    EEHCLKFLSA VLAAQKAQSQ LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG 150
    FEDNFSSMNL DKKINSQNQP TGIHREPPPP PFSVNKMLPR EKEASNKEQP 200
    KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF RFFVGTWNVN 250
    GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA 300
    VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG 350
    KMGNKGGVAV RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV 400
    VPNQTLPQLN IMKHEVVIWL GDLNYRLCMP DANEVKSLIN KKDLQRLLKF 450
    DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD SKTDRWDSSG KCRVPAWCDR 500
    ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE RRYRKVFEDS 550
    VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS 600
    FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE 650
    DKIEDILVLH LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT 700
    KLIDLEEDSF LEKEKSLLQM VPLDEGASER PLQVPKEIWL LVDHLFKYAC 750
    HQEDLFQTPG MQEELQQIID CLDTSIPETI PGSNHSVAEA LLIFLEALPE 800
    PVICYELYQR CLDSAYDPRI CRQVISQLPR CHRNVFRYLM AFLRELLKFS 850
    EYNSVNANMI ATLFTSLLLR PPPNLMARQT PSDRQRAIQF LLGFLLGSEE 900
    D 901
    Length:901
    Mass (Da):104,205
    Last modified:June 7, 2005 - v3
    Checksum:i476BFCCC3655C1FE
    GO
    Isoform B (identifier: Q01968-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         707-714: Missing.

    Show »
    Length:893
    Mass (Da):103,227
    Checksum:iE61E59C6AD0AC650
    GO

    Sequence cautioni

    The sequence AAA59964.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801P → L in BAF85796. (PubMed:14702039)Curated
    Sequence conflicti321 – 3211G → E in AAI44107. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti242 – 2421F → S in OCRL. 1 Publication
    Corresponds to variant rs137853828 [ dbSNP | Ensembl ].
    VAR_064773
    Natural varianti274 – 2741I → T in OCRL. 1 Publication
    Corresponds to variant rs137853829 [ dbSNP | Ensembl ].
    VAR_064774
    Natural varianti277 – 2771Q → R in OCRL. 1 Publication
    Corresponds to variant rs137853830 [ dbSNP | Ensembl ].
    VAR_064775
    Natural varianti318 – 3181R → C in DD2 and OCRL. 3 Publications
    Corresponds to variant rs137853263 [ dbSNP | Ensembl ].
    VAR_022698
    Natural varianti337 – 3371R → C in OCRL; associated with I-361. 1 Publication
    Corresponds to variant rs137853831 [ dbSNP | Ensembl ].
    VAR_064776
    Natural varianti337 – 3371R → P in OCRL.
    VAR_010169
    Natural varianti354 – 3541N → H in DD2. 1 Publication
    Corresponds to variant rs137853833 [ dbSNP | Ensembl ].
    VAR_064777
    Natural varianti357 – 3571G → E in OCRL; uncertain pathological significance. 1 Publication
    Corresponds to variant rs137853854 [ dbSNP | Ensembl ].
    VAR_010170
    Natural varianti361 – 3611R → I in OCRL; associated with C-337. 1 Publication
    Corresponds to variant rs137853832 [ dbSNP | Ensembl ].
    VAR_064778
    Natural varianti367 – 3671Missing in OCRL. 1 Publication
    VAR_010171
    Natural varianti372 – 3721V → G in OCRL. 1 Publication
    Corresponds to variant rs137853834 [ dbSNP | Ensembl ].
    VAR_010172
    Natural varianti373 – 3731N → Y in OCRL. 1 Publication
    Corresponds to variant rs137853835 [ dbSNP | Ensembl ].
    VAR_064779
    Natural varianti374 – 3741S → F in OCRL. 1 Publication
    Corresponds to variant rs137853836 [ dbSNP | Ensembl ].
    VAR_064780
    Natural varianti375 – 3751H → Y in OCRL. 1 Publication
    Corresponds to variant rs137853848 [ dbSNP | Ensembl ].
    VAR_010173
    Natural varianti414 – 4141H → R in OCRL. 1 Publication
    Corresponds to variant rs137853837 [ dbSNP | Ensembl ].
    VAR_064781
    Natural varianti421 – 4211G → E in OCRL. 1 Publication
    Corresponds to variant rs137853855 [ dbSNP | Ensembl ].
    VAR_010174
    Natural varianti424 – 4241N → D in OCRL. 1 Publication
    Corresponds to variant rs137853856 [ dbSNP | Ensembl ].
    VAR_010175
    Natural varianti451 – 4511D → G in OCRL. 1 Publication
    Corresponds to variant rs137853850 [ dbSNP | Ensembl ].
    VAR_010176
    Natural varianti451 – 4511D → N in OCRL. 1 Publication
    Corresponds to variant rs137853838 [ dbSNP | Ensembl ].
    VAR_064782
    Natural varianti457 – 4571R → G in OCRL. 1 Publication
    Corresponds to variant rs137853839 [ dbSNP | Ensembl ].
    VAR_064783
    Natural varianti463 – 4631F → S in OCRL. 1 Publication
    Corresponds to variant rs137853851 [ dbSNP | Ensembl ].
    VAR_010177
    Natural varianti468 – 4681E → G in OCRL. 1 Publication
    Corresponds to variant rs137853841 [ dbSNP | Ensembl ].
    VAR_064784
    Natural varianti468 – 4681E → K in OCRL. 1 Publication
    Corresponds to variant rs137853840 [ dbSNP | Ensembl ].
    VAR_064785
    Natural varianti478 – 4792Missing in OCRL.
    VAR_023957
    Natural varianti479 – 4791Y → C in DD2. 1 Publication
    Corresponds to variant rs137853262 [ dbSNP | Ensembl ].
    VAR_022699
    Natural varianti493 – 4931R → W in DD2. 1 Publication
    Corresponds to variant rs137853846 [ dbSNP | Ensembl ].
    VAR_064786
    Natural varianti495 – 4951P → L in OCRL. 1 Publication
    VAR_064787
    Natural varianti498 – 4981C → Y in OCRL. 1 Publication
    Corresponds to variant rs137853857 [ dbSNP | Ensembl ].
    VAR_010178
    Natural varianti499 – 4991D → H in OCRL. 1 Publication
    Corresponds to variant rs137853842 [ dbSNP | Ensembl ].
    VAR_064788
    Natural varianti500 – 5001R → G in OCRL.
    VAR_010179
    Natural varianti500 – 5001R → Q in OCRL. 3 Publications
    Corresponds to variant rs137853260 [ dbSNP | Ensembl ].
    VAR_010180
    Natural varianti503 – 5031W → R in OCRL. 1 Publication
    Corresponds to variant rs137853843 [ dbSNP | Ensembl ].
    VAR_064789
    Natural varianti508 – 5081V → D in OCRL. 1 Publication
    Corresponds to variant rs137853849 [ dbSNP | Ensembl ].
    VAR_010181
    Natural varianti513 – 5131Y → C in OCRL. 1 Publication
    Corresponds to variant rs137853847 [ dbSNP | Ensembl ].
    VAR_010182
    Natural varianti522 – 5221S → R in OCRL. 1 Publication
    Corresponds to variant rs137853853 [ dbSNP | Ensembl ].
    VAR_010183
    Natural varianti524 – 5241H → Q in OCRL. 1 Publication
    Corresponds to variant rs137853261 [ dbSNP | Ensembl ].
    VAR_010184
    Natural varianti524 – 5241H → R in OCRL. 1 Publication
    Corresponds to variant rs137853852 [ dbSNP | Ensembl ].
    VAR_010185
    Natural varianti526 – 5261P → L in OCRL. 1 Publication
    Corresponds to variant rs137853858 [ dbSNP | Ensembl ].
    VAR_023958
    Natural varianti533 – 5331I → S in OCRL.
    VAR_010187
    Natural varianti591 – 5911N → K in OCRL. 2 Publications
    Corresponds to variant rs137853844 [ dbSNP | Ensembl ].
    VAR_064790
    Natural varianti742 – 7421Missing in OCRL. 1 Publication
    VAR_064791
    Natural varianti768 – 7681I → N in OCRL; uncertain pathological significance; abolishes FAM109A-binding; does not affect clathrin-binding. 2 Publications
    VAR_010188
    Natural varianti797 – 7971A → P in OCRL; uncertain pathological significance; abolishes FAM109A-, FAM109B- and APPL1-binding; does not affect clathrin-binding. 2 Publications
    VAR_010189
    Natural varianti799 – 7991P → L in DD2. 1 Publication
    VAR_064792
    Natural varianti801 – 8011P → L in OCRL. 1 Publication
    VAR_064793
    Natural varianti891 – 8911L → R in OCRL. 1 Publication
    Corresponds to variant rs137853845 [ dbSNP | Ensembl ].
    VAR_064794

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei707 – 7148Missing in isoform B. 2 PublicationsVSP_002681

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88162 mRNA. Translation: AAA59964.2. Different initiation.
    U57627 mRNA. Translation: AAB03839.2.
    AK293107 mRNA. Translation: BAF85796.1.
    AL022162, AL138745, AL662877 Genomic DNA. Translation: CAI95695.1.
    AL022162, AL138745, AL662877 Genomic DNA. Translation: CAI95696.1.
    AL138745, AL022162, AL662877 Genomic DNA. Translation: CAI42615.1.
    AL138745, AL022162, AL662877 Genomic DNA. Translation: CAI42616.1.
    AL662877, AL022162, AL138745 Genomic DNA. Translation: CAI41087.1.
    AL662877, AL022162, AL138745 Genomic DNA. Translation: CAI41088.1.
    Z73496 Genomic DNA. No translation available.
    CH471107 Genomic DNA. Translation: EAX11831.1.
    CH471107 Genomic DNA. Translation: EAX11832.1.
    BC130612 mRNA. Translation: AAI30613.1.
    BC144106 mRNA. Translation: AAI44107.1.
    S62085 mRNA. Translation: AAB26926.1.
    CCDSiCCDS35393.1. [Q01968-1]
    CCDS35394.1. [Q01968-2]
    PIRiS29069.
    RefSeqiNP_000267.2. NM_000276.3. [Q01968-1]
    NP_001578.2. NM_001587.3. [Q01968-2]
    UniGeneiHs.126357.

    Genome annotation databases

    EnsembliENST00000357121; ENSP00000349635; ENSG00000122126. [Q01968-2]
    ENST00000371113; ENSP00000360154; ENSG00000122126. [Q01968-1]
    GeneIDi4952.
    KEGGihsa:4952.
    UCSCiuc004euq.3. human. [Q01968-1]
    uc004eur.3. human. [Q01968-2]

    Polymorphism databases

    DMDMi67477390.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Lowe Syndrome mutation database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88162 mRNA. Translation: AAA59964.2 . Different initiation.
    U57627 mRNA. Translation: AAB03839.2 .
    AK293107 mRNA. Translation: BAF85796.1 .
    AL022162 , AL138745 , AL662877 Genomic DNA. Translation: CAI95695.1 .
    AL022162 , AL138745 , AL662877 Genomic DNA. Translation: CAI95696.1 .
    AL138745 , AL022162 , AL662877 Genomic DNA. Translation: CAI42615.1 .
    AL138745 , AL022162 , AL662877 Genomic DNA. Translation: CAI42616.1 .
    AL662877 , AL022162 , AL138745 Genomic DNA. Translation: CAI41087.1 .
    AL662877 , AL022162 , AL138745 Genomic DNA. Translation: CAI41088.1 .
    Z73496 Genomic DNA. No translation available.
    CH471107 Genomic DNA. Translation: EAX11831.1 .
    CH471107 Genomic DNA. Translation: EAX11832.1 .
    BC130612 mRNA. Translation: AAI30613.1 .
    BC144106 mRNA. Translation: AAI44107.1 .
    S62085 mRNA. Translation: AAB26926.1 .
    CCDSi CCDS35393.1. [Q01968-1 ]
    CCDS35394.1. [Q01968-2 ]
    PIRi S29069.
    RefSeqi NP_000267.2. NM_000276.3. [Q01968-1 ]
    NP_001578.2. NM_001587.3. [Q01968-2 ]
    UniGenei Hs.126357.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KIE NMR - A 1-119 [» ]
    2QV2 X-ray 2.40 A 564-901 [» ]
    3QBT X-ray 2.00 B/D/F/H 540-678 [» ]
    3QIS X-ray 2.30 A 536-901 [» ]
    4CMN X-ray 3.13 A 215-560 [» ]
    ProteinModelPortali Q01968.
    SMRi Q01968. Positions 1-119, 234-538, 540-898.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111006. 6 interactions.
    IntActi Q01968. 21 interactions.
    MINTi MINT-5004450.

    PTM databases

    PhosphoSitei Q01968.

    Polymorphism databases

    DMDMi 67477390.

    Proteomic databases

    MaxQBi Q01968.
    PaxDbi Q01968.
    PRIDEi Q01968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357121 ; ENSP00000349635 ; ENSG00000122126 . [Q01968-2 ]
    ENST00000371113 ; ENSP00000360154 ; ENSG00000122126 . [Q01968-1 ]
    GeneIDi 4952.
    KEGGi hsa:4952.
    UCSCi uc004euq.3. human. [Q01968-1 ]
    uc004eur.3. human. [Q01968-2 ]

    Organism-specific databases

    CTDi 4952.
    GeneCardsi GC0XP128673.
    GeneReviewsi OCRL.
    HGNCi HGNC:8108. OCRL.
    HPAi HPA012495.
    MIMi 300535. gene.
    300555. phenotype.
    309000. phenotype.
    neXtProti NX_Q01968.
    Orphaneti 93623. Dent disease type 2.
    534. Oculocerebrorenal syndrome.
    PharmGKBi PA31896.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5411.
    HOVERGENi HBG000070.
    InParanoidi Q01968.
    KOi K01099.
    OMAi AKYKKVQ.
    OrthoDBi EOG7J4465.
    PhylomeDBi Q01968.
    TreeFami TF317034.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04546-MONOMER.
    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_120836. Synthesis of PIPs at the Golgi membrane.
    REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
    REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    SignaLinki Q01968.

    Miscellaneous databases

    EvolutionaryTracei Q01968.
    GeneWikii OCRL.
    GenomeRNAii 4952.
    NextBioi 19074.
    PROi Q01968.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q01968.
    CleanExi HS_INPP5F.
    Genevestigatori Q01968.

    Family and domain databases

    Gene3Di 1.10.555.10. 2 hits.
    3.60.10.10. 1 hit.
    InterProi IPR005135. Endo/exonuclease/phosphatase.
    IPR000300. IPPc.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF03372. Exo_endo_phos. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00128. IPPc. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 2 hits.
    SSF56219. SSF56219. 1 hit.
    PROSITEi PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase."
      Attree O., Olivos I.M., Okabe I., Bailey L.C., Nelson D.L., Lewis R.A., McInnes R.R., Nussbaum R.L.
      Nature 358:239-242(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
      Tissue: Kidney.
    2. Attree O., Olivos I.M., Okabe I., Bailey L.C., Nelson D.L., Lewis R.A., McInnes R.R., Nussbaum R.L.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 585.
    3. "Physical mapping and genomic structure of the Lowe syndrome gene OCRL1."
      Nussbaum R.L., Orrison B.M., Janne P.A., Charnas L.R., Chinault A.C.
      Hum. Genet. 99:145-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Tissue: Uterus.
    5. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    8. "Nonsense mutations in the OCRL-1 gene in patients with the oculocerebrorenal syndrome of Lowe."
      Leahey A.-M., Charnas L.R., Nussbaum R.L.
      Hum. Mol. Genet. 2:461-463(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 814-843.
    9. "The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphosphate 5-phosphatase."
      Zhang X., Jefferson A.B., Auethavekiat V., Majerus P.W.
      Proc. Natl. Acad. Sci. U.S.A. 92:4853-4856(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    10. "Cell lines from kidney proximal tubules of a patient with Lowe syndrome lack OCRL inositol polyphosphate 5-phosphatase and accumulate phosphatidylinositol 4,5-bisphosphate."
      Zhang X., Hartz P.A., Philip E., Racusen L.C., Majerus P.W.
      J. Biol. Chem. 273:1574-1582(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Two closely related endocytic proteins that share a common OCRL-binding motif with APPL1."
      Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.
      Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APPL1; CLATHRIN; FAM109A AND FAM109B, SUBCELLULAR LOCATION, VARIANTS OCRL ASN-768 AND PRO-797.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in the endocytic pathway."
      Noakes C.J., Lee G., Lowe M.
      Mol. Biol. Cell 22:606-623(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APPL1; FAM109A AND FAM109B, VARIANT OCRL ASN-768.
    14. Cited for: FUNCTION IN CILIA ASSEMBLY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH RAB8A, MUTAGENESIS OF ASP-422; ASP-499 AND PHE-668.
    15. Cited for: FUNCTION IN CILIOGENESIS.
    16. "Inositol 5-phosphatases: insights from the Lowe syndrome protein OCRL."
      Pirruccello M., De Camilli P.
      Trends Biochem. Sci. 37:134-143(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    17. "A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism."
      Mao Y., Balkin D.M., Zoncu R., Erdmann K.S., Tomasini L., Hu F., Jin M.M., Hodsdon M.E., De Camilli P.
      EMBO J. 28:1831-1842(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-119, DOMAIN PH, INTERACTION WITH CLATHRIN, SUBCELLULAR LOCATION.
    18. "A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1."
      Hou X., Hagemann N., Schoebel S., Blankenfeldt W., Goody R.S., Erdmann K.S., Itzen A.
      EMBO J. 30:1659-1670(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 540-678 IN COMPLEX WITH RAB8A.
    19. "A role of the Lowe syndrome protein OCRL in early steps of the endocytic pathway."
      Erdmann K.S., Mao Y., McCrea H.J., Zoncu R., Lee S., Paradise S., Modregger J., Biemesderfer D., Toomre D., De Camilli P.
      Dev. Cell 13:377-390(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 564-901, SUBCELLULAR LOCATION, INTERACTION WITH APPL1.
    20. "Recognition of the F&H motif by the Lowe syndrome protein OCRL."
      Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.
      Nat. Struct. Mol. Biol. 18:789-795(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 536-901 IN COMPLEX WITH FAM109A.
    21. "Spectrum of mutations in the OCRL1 gene in the Lowe oculocerebrorenal syndrome."
      Lin T., Orrison B.M., Leahey A.-M., Suchy S.F., Bernard D.J., Lewis R.A., Nussbaum R.L.
      Am. J. Hum. Genet. 60:1384-1388(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OCRL THR-367 DEL; GLY-451; SER-463 AND ARG-524.
    22. "Mutations are not uniformly distributed throughout the OCRL1 gene in Lowe syndrome patients."
      Lin T., Orrison B.M., Suchy S.F., Lewis R.A., Nussbaum R.L.
      Mol. Genet. Metab. 64:58-61(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OCRL TYR-375; GLN-500; ASP-508 AND CYS-513.
    23. "Oculocerebrorenal syndrome of Lowe: three mutations in the OCRL1 gene derived from three patients with different phenotypes."
      Kawano T., Indo Y., Nakazato H., Shimadzu M., Matsuda I.
      Am. J. Med. Genet. 77:348-355(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OCRL GLN-500 AND GLN-524.
    24. "Identification of two novel mutations in the OCRL1 gene in Japanese families with Lowe syndrome."
      Kubota T., Sakurai A., Arakawa K., Shimazu M., Wakui K., Furihata K., Fukushima Y.
      Clin. Genet. 54:199-202(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OCRL ARG-522.
    25. "OCRL1 mutation analysis in French Lowe syndrome patients: implications for molecular diagnosis strategy and genetic counseling."
      Monnier N., Satre V., Lerouge E., Berthoin F., Lunardi J.
      Hum. Mutat. 16:157-165(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OCRL GLU-357; GLU-421; ASP-424 AND TYR-498.
    26. "Carrier assessment in families with Lowe oculocerebrorenal syndrome: novel mutations in the OCRL1 gene and correlation of direct DNA diagnosis with ocular examination."
      Roeschinger W., Muntau A.C., Rudolph G., Roscher A.A., Kammerer S.
      Mol. Genet. Metab. 69:213-222(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OCRL LYS-478-479-TYR DEL; GLN-500 AND LEU-526.
    27. Cited for: VARIANTS DD2 CYS-318 AND CYS-479.
    28. Cited for: VARIANTS DD2 CYS-318 AND TRP-493.
    29. "Magnetic resonance imaging, magnetic resonance spectroscopy, and facial dysmorphism in a case of Lowe syndrome with novel OCRL1 gene mutation."
      Yuksel A., Karaca E., Albayram M.S.
      J. Child Neurol. 24:93-96(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OCRL LYS-591.
    30. "From Lowe syndrome to Dent disease: correlations between mutations of the OCRL1 gene and clinical and biochemical phenotypes."
      Hichri H., Rendu J., Monnier N., Coutton C., Dorseuil O., Poussou R.V., Baujat G., Blanchard A., Nobili F., Ranchin B., Remesy M., Salomon R., Satre V., Lunardi J.
      Hum. Mutat. 32:379-388(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OCRL SER-242; THR-274; ARG-277; CYS-318; CYS-337; ILE-361; GLY-372; TYR-373; PHE-374; ARG-414; ASN-451; GLY-457; LYS-468; GLY-468; LEU-495; HIS-499; ARG-503; LYS-591; VAL-742 DEL; PRO-797; LEU-801 AND ARG-891, VARIANTS DD2 HIS-354 AND LEU-799.

    Entry informationi

    Entry nameiOCRL_HUMAN
    AccessioniPrimary (citable) accession number: Q01968
    Secondary accession number(s): A6NKI1
    , A8KAP2, B7ZLX2, O60800, Q15684, Q15774, Q4VY09, Q4VY10, Q5JQF1, Q5JQF2, Q9UJG5, Q9UMA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 158 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    It is uncertain whether Met-1, Met-18 or Met-20 is the initiator.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3