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Q01968

- OCRL_HUMAN

UniProt

Q01968 - OCRL_HUMAN

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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

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. Rac GTPase activator activity Source: FlyBase
  4. 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
Complete GO annotation...

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-KW
  3. cytoplasm Source: FlyBase
  4. cytosol Source: Reactome
  5. early endosome Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
  7. Golgi-associated vesicle Source: ProtInc
  8. Golgi stack Source: ProtInc
  9. nucleus Source: FlyBase
  10. photoreceptor outer segment Source: UniProtKB
  11. plasma membrane Source: FlyBase
  12. trans-Golgi network Source: FlyBase
Complete GO annotation...

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. 15 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 – 2112Combined sources
Beta strandi24 – 3512Combined sources
Beta strandi38 – 458Combined sources
Beta strandi52 – 576Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 708Combined sources
Helixi76 – 783Combined sources
Beta strandi80 – 9011Combined sources
Beta strandi94 – 985Combined sources
Helixi101 – 11818Combined sources
Helixi222 – 2298Combined sources
Helixi231 – 2344Combined sources
Beta strandi235 – 24814Combined sources
Helixi259 – 2624Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi270 – 2778Combined sources
Helixi283 – 2864Combined sources
Helixi292 – 30413Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi322 – 3298Combined sources
Helixi332 – 3354Combined sources
Beta strandi336 – 34510Combined sources
Helixi348 – 3503Combined sources
Beta strandi355 – 36410Combined sources
Beta strandi367 – 3759Combined sources
Helixi383 – 39614Combined sources
Helixi411 – 4133Combined sources
Beta strandi414 – 4229Combined sources
Helixi432 – 4409Combined sources
Helixi444 – 4485Combined sources
Helixi452 – 4587Combined sources
Beta strandi461 – 4633Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi489 – 4913Combined sources
Beta strandi499 – 5046Combined sources
Beta strandi506 – 5105Combined sources
Beta strandi521 – 5244Combined sources
Beta strandi527 – 53812Combined sources
Helixi553 – 5608Combined sources
Beta strandi565 – 5684Combined sources
Beta strandi571 – 5777Combined sources
Beta strandi583 – 5919Combined sources
Beta strandi593 – 5953Combined sources
Beta strandi597 – 6026Combined sources
Beta strandi608 – 6114Combined sources
Beta strandi615 – 6195Combined sources
Beta strandi621 – 6244Combined sources
Beta strandi629 – 6368Combined sources
Helixi640 – 6489Combined sources
Beta strandi649 – 6513Combined sources
Beta strandi655 – 6617Combined sources
Beta strandi666 – 67510Combined sources
Helixi684 – 6896Combined sources
Helixi736 – 74813Combined sources
Turni753 – 7575Combined sources
Helixi762 – 77413Combined sources
Helixi784 – 79714Combined sources
Helixi805 – 81410Combined sources
Helixi818 – 8269Combined sources
Helixi830 – 84718Combined sources
Helixi850 – 8534Combined sources
Helixi857 – 86812Combined sources
Helixi883 – 89513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 219-898.
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.
GeneTreeiENSGT00760000119075.
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

        10         20         30         40         50
MEPPLPVGAQ PLATVEGMEM KGPLREPCAL TLAQRNGQYE LIIQLHEKEQ
60 70 80 90 100
HVQDIIPINS HFRCVQEAEE TLLIDIASNS GCKIRVQGDW IRERRFEIPD
110 120 130 140 150
EEHCLKFLSA VLAAQKAQSQ LLVPEQKDSS SWYQKLDTKD KPSVFSGLLG
160 170 180 190 200
FEDNFSSMNL DKKINSQNQP TGIHREPPPP PFSVNKMLPR EKEASNKEQP
210 220 230 240 250
KVTNTMRKLF VPNTQSGQRE GLIKHILAKR EKEYVNIQTF RFFVGTWNVN
260 270 280 290 300
GQSPDSGLEP WLNCDPNPPD IYCIGFQELD LSTEAFFYFE SVKEQEWSMA
310 320 330 340 350
VERGLHSKAK YKKVQLVRLV GMMLLIFARK DQCRYIRDIA TETVGTGIMG
360 370 380 390 400
KMGNKGGVAV RFVFHNTTFC IVNSHLAAHV EDFERRNQDY KDICARMSFV
410 420 430 440 450
VPNQTLPQLN IMKHEVVIWL GDLNYRLCMP DANEVKSLIN KKDLQRLLKF
460 470 480 490 500
DQLNIQRTQK KAFVDFNEGE IKFIPTYKYD SKTDRWDSSG KCRVPAWCDR
510 520 530 540 550
ILWRGTNVNQ LNYRSHMELK TSDHKPVSAL FHIGVKVVDE RRYRKVFEDS
560 570 580 590 600
VRIMDRMEND FLPSLELSRR EFVFENVKFR QLQKEKFQIS NNGQVPCHFS
610 620 630 640 650
FIPKLNDSQY CKPWLRAEPF EGYLEPNETV DISLDVYVSK DSVTILNSGE
660 670 680 690 700
DKIEDILVLH LDRGKDYFLT ISGNYLPSCF GTSLEALCRM KRPIREVPVT
710 720 730 740 750
KLIDLEEDSF LEKEKSLLQM VPLDEGASER PLQVPKEIWL LVDHLFKYAC
760 770 780 790 800
HQEDLFQTPG MQEELQQIID CLDTSIPETI PGSNHSVAEA LLIFLEALPE
810 820 830 840 850
PVICYELYQR CLDSAYDPRI CRQVISQLPR CHRNVFRYLM AFLRELLKFS
860 870 880 890 900
EYNSVNANMI ATLFTSLLLR PPPNLMARQT PSDRQRAIQF LLGFLLGSEE

D
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 219-898.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111006. 15 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.
GeneTreei ENSGT00760000119075.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 160 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