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O00294

- TULP1_HUMAN

UniProt

O00294 - TULP1_HUMAN

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Protein

Tubby-related protein 1

Gene
TULP1, TUBL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells By similarity. Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages.2 Publications

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB
  2. G-protein coupled photoreceptor activity Source: Ensembl
  3. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. dendrite development Source: UniProtKB
  2. detection of light stimulus involved in visual perception Source: UniProt
  3. eye photoreceptor cell development Source: UniProtKB
  4. phagocytosis Source: UniProtKB-KW
  5. photoreceptor cell maintenance Source: UniProtKB
  6. phototransduction Source: Ensembl
  7. positive regulation of phagocytosis Source: UniProtKB
  8. retina development in camera-type eye Source: Ensembl
  9. retina homeostasis Source: UniProt
  10. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Phagocytosis, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Tubby-related protein 1
Alternative name(s):
Tubby-like protein 1
Gene namesi
Name:TULP1
Synonyms:TUBL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:12423. TULP1.

Subcellular locationi

Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Secreted By similarity. Cell junctionsynapse By similarity
Note: Detected at synapses between photoreceptor cells and second-order neurons. Does not have a cleavable signal peptide and is secreted by an alternative pathway By similarity.1 Publication

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB
  3. cytoplasm Source: UniProtKB-SubCell
  4. extracellular region Source: UniProtKB-SubCell
  5. photoreceptor inner segment Source: UniProtKB
  6. photoreceptor outer segment Source: UniProtKB
  7. plasma membrane Source: UniProtKB
  8. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Secreted, Synapse

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 14 (RP14) [MIM:600132]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1278Missing in RP14.
VAR_013310
Natural varianti245 – 2451A → V in RP14.
VAR_008275
Natural varianti261 – 2611K → T in RP14.
VAR_008277
Natural varianti378 – 3781R → H in RP14.
VAR_008278
Natural varianti382 – 3821F → S in RP14. 1 Publication
VAR_037584
Natural varianti420 – 4201R → P in RP14; no effect on RPE phagocytosis. 2 Publications
VAR_007941
Natural varianti454 – 4541T → M in RP14.
Corresponds to variant rs138200747 [ dbSNP | Ensembl ].
VAR_008279
Natural varianti459 – 4591I → K in RP14; no effect on RPE phagocytosis. 2 Publications
Corresponds to variant rs121909075 [ dbSNP | Ensembl ].
VAR_007942
Natural varianti482 – 4821R → W in RP14. 1 Publication
VAR_065502
Natural varianti489 – 4891K → R in RP14; abolishes RPE phagocytosis. 2 Publications
VAR_008280
Natural varianti491 – 4911F → L in RP14; abolishes RPE phagocytosis. 2 Publications
VAR_007943
Natural varianti496 – 4961A → T in RP14; unknown pathological significance. 2 Publications
Corresponds to variant rs141980901 [ dbSNP | Ensembl ].
VAR_008281
Leber congenital amaurosis 15 (LCA15) [MIM:613843]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti368 – 3681G → W in LCA15. 1 Publication
VAR_065500
Natural varianti400 – 4001R → W in LCA15. 1 Publication
VAR_065501
Natural varianti529 – 5291A → AFA in LCA15.
VAR_065503

Keywords - Diseasei

Disease mutation, Leber congenital amaurosis, Retinitis pigmentosa

Organism-specific databases

MIMi600132. phenotype.
613843. phenotype.
Orphaneti65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
PharmGKBiPA37085.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542Tubby-related protein 1PRO_0000186466Add
BLAST

Proteomic databases

PaxDbiO00294.
PRIDEiO00294.

PTM databases

PhosphoSiteiO00294.

Expressioni

Tissue specificityi

Retina-specific.

Gene expression databases

ArrayExpressiO00294.
BgeeiO00294.
CleanExiHS_TULP1.
GenevestigatoriO00294.

Interactioni

Subunit structurei

Homodimer Inferred. May interact with ABCF1, PSIP1, ZEB1 and HMGB2 Reviewed prediction. Interacts with DNM1 By similarity. Interacts with F-actin. Interacts with TUB By similarity. Interacts with TYRO3 By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-1756778,EBI-389883

Protein-protein interaction databases

IntActiO00294. 3 interactions.
STRINGi9606.ENSP00000229771.

Structurei

Secondary structure

1
542
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi294 – 2963
Beta strandi304 – 3118
Beta strandi323 – 33210
Beta strandi335 – 3417
Beta strandi349 – 3546
Beta strandi366 – 3727
Beta strandi374 – 3829
Beta strandi384 – 3863
Helixi388 – 3903
Helixi396 – 3983
Beta strandi402 – 4087
Beta strandi421 – 4266
Helixi446 – 4527
Beta strandi458 – 4636
Beta strandi467 – 4693
Turni470 – 4734
Beta strandi474 – 4763
Beta strandi491 – 4955
Beta strandi503 – 5108
Beta strandi513 – 5197
Helixi524 – 53310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FIMX-ray1.90A/B290-542[»]
3C5NX-ray1.80A/B291-536[»]
ProteinModelPortaliO00294.
SMRiO00294. Positions 291-536.

Miscellaneous databases

EvolutionaryTraceiO00294.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi115 – 13117Poly-GluAdd
BLAST
Compositional biasi248 – 2547Poly-Glu

Sequence similaritiesi

Belongs to the TUB family.

Phylogenomic databases

eggNOGiNOG286778.
HOGENOMiHOG000016044.
HOVERGENiHBG018010.
InParanoidiO00294.
OMAiEAPESPC.
OrthoDBiEOG77HDDQ.
PhylomeDBiO00294.
TreeFamiTF314076.

Family and domain databases

Gene3Di3.20.90.10. 1 hit.
InterProiIPR000007. Tubby_C.
IPR025659. Tubby_C-like.
IPR018066. Tubby_C_CS.
[Graphical view]
PfamiPF01167. Tub. 1 hit.
[Graphical view]
PRINTSiPR01573. SUPERTUBBY.
SUPFAMiSSF54518. SSF54518. 1 hit.
PROSITEiPS01200. TUB_1. 1 hit.
PS01201. TUB_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00294-1) [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

MPLRDETLRE VWASDSGHEE ESLSPEAPRR PKQRPAPAQR LRKKRTEAPE    50
SPCPTGSKPR KPGAGRTGRP REEPSPDPAQ ARAPQTVYAR FLRDPEAKKR 100
DPRETFLVAR APDAEDEEEE EEEDEEDEEE EAEEKKEKIL LPPKKPLREK 150
SSADLKERRA KAQGPRGDLG SPDPPPKPLR VRNKEAPAGE GTKMRKTKKK 200
GSGEADKDPS GSPASARKSP AAMFLVGEGS PDKKALKKKG TPKGARKEEE 250
EEEEAATVIK KSNQKGKAKG KGKKKAKEER APSPPVEVDE PREFVLRPAP 300
QGRTVRCRLT RDKKGMDRGM YPSYFLHLDT EKKVFLLAGR KRKRSKTANY 350
LISIDPTNLS RGGENFIGKL RSNLLGNRFT VFDNGQNPQR GYSTNVASLR 400
QELAAVIYET NVLGFRGPRR MTVIIPGMSA ENERVPIRPR NASDGLLVRW 450
QNKTLESLIE LHNKPPVWND DSGSYTLNFQ GRVTQASVKN FQIVHADDPD 500
YIVLQFGRVA EDAFTLDYRY PLCALQAFAI ALSSFDGKLA CE 542
Length:542
Mass (Da):60,609
Last modified:September 23, 2008 - v3
Checksum:i65320103E2674B60
GO
Isoform 2 (identifier: O00294-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     64-116: Missing.

Show »
Length:489
Mass (Da):54,667
Checksum:iA687CD39AB3E8000
GO

Sequence cautioni

The sequence CAI20251.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671T → R.2 Publications
Corresponds to variant rs7764472 [ dbSNP | Ensembl ].
VAR_008274
Natural varianti120 – 1278Missing in RP14.
VAR_013310
Natural varianti245 – 2451A → V in RP14.
VAR_008275
Natural varianti259 – 2591I → T.1 Publication
Corresponds to variant rs2064317 [ dbSNP | Ensembl ].
VAR_008276
Natural varianti261 – 2611K → N.4 Publications
Corresponds to variant rs2064318 [ dbSNP | Ensembl ].
VAR_034575
Natural varianti261 – 2611K → T in RP14.
VAR_008277
Natural varianti368 – 3681G → W in LCA15. 1 Publication
VAR_065500
Natural varianti378 – 3781R → H in RP14.
VAR_008278
Natural varianti382 – 3821F → S in RP14. 1 Publication
VAR_037584
Natural varianti400 – 4001R → W in LCA15. 1 Publication
VAR_065501
Natural varianti420 – 4201R → P in RP14; no effect on RPE phagocytosis. 2 Publications
VAR_007941
Natural varianti454 – 4541T → M in RP14.
Corresponds to variant rs138200747 [ dbSNP | Ensembl ].
VAR_008279
Natural varianti459 – 4591I → K in RP14; no effect on RPE phagocytosis. 2 Publications
Corresponds to variant rs121909075 [ dbSNP | Ensembl ].
VAR_007942
Natural varianti482 – 4821R → W in RP14. 1 Publication
VAR_065502
Natural varianti489 – 4891K → R in RP14; abolishes RPE phagocytosis. 2 Publications
VAR_008280
Natural varianti491 – 4911F → L in RP14; abolishes RPE phagocytosis. 2 Publications
VAR_007943
Natural varianti496 – 4961A → T in RP14; unknown pathological significance. 2 Publications
Corresponds to variant rs141980901 [ dbSNP | Ensembl ].
VAR_008281
Natural varianti529 – 5291A → AFA in LCA15.
VAR_065503

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei64 – 11653Missing in isoform 2. VSP_023031Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82468 mRNA. Translation: AAB53700.1.
AF034923
, AF034919, AF034920, AF034921, AF034922 Genomic DNA. Translation: AAB97966.1.
AL033519 Genomic DNA. Translation: CAI20251.1. Sequence problems.
BC032714 mRNA. Translation: AAH32714.1.
BC065261 mRNA. Translation: AAH65261.1.
CCDSiCCDS4807.1. [O00294-1]
RefSeqiNP_001276324.1. NM_001289395.1. [O00294-2]
NP_003313.3. NM_003322.4. [O00294-1]
UniGeneiHs.485208.

Genome annotation databases

EnsembliENST00000229771; ENSP00000229771; ENSG00000112041. [O00294-1]
ENST00000322263; ENSP00000319414; ENSG00000112041. [O00294-2]
GeneIDi7287.
KEGGihsa:7287.
UCSCiuc003okv.4. human. [O00294-1]
uc003okw.4. human. [O00294-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the TULP1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U82468 mRNA. Translation: AAB53700.1 .
AF034923
, AF034919 , AF034920 , AF034921 , AF034922 Genomic DNA. Translation: AAB97966.1 .
AL033519 Genomic DNA. Translation: CAI20251.1 . Sequence problems.
BC032714 mRNA. Translation: AAH32714.1 .
BC065261 mRNA. Translation: AAH65261.1 .
CCDSi CCDS4807.1. [O00294-1 ]
RefSeqi NP_001276324.1. NM_001289395.1. [O00294-2 ]
NP_003313.3. NM_003322.4. [O00294-1 ]
UniGenei Hs.485208.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FIM X-ray 1.90 A/B 290-542 [» ]
3C5N X-ray 1.80 A/B 291-536 [» ]
ProteinModelPortali O00294.
SMRi O00294. Positions 291-536.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O00294. 3 interactions.
STRINGi 9606.ENSP00000229771.

PTM databases

PhosphoSitei O00294.

Proteomic databases

PaxDbi O00294.
PRIDEi O00294.

Protocols and materials databases

DNASUi 7287.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229771 ; ENSP00000229771 ; ENSG00000112041 . [O00294-1 ]
ENST00000322263 ; ENSP00000319414 ; ENSG00000112041 . [O00294-2 ]
GeneIDi 7287.
KEGGi hsa:7287.
UCSCi uc003okv.4. human. [O00294-1 ]
uc003okw.4. human. [O00294-2 ]

Organism-specific databases

CTDi 7287.
GeneCardsi GC06M035465.
GeneReviewsi TULP1.
H-InvDB HIX0005807.
HGNCi HGNC:12423. TULP1.
MIMi 600132. phenotype.
602280. gene.
613843. phenotype.
neXtProti NX_O00294.
Orphaneti 65. Leber congenital amaurosis.
791. Retinitis pigmentosa.
PharmGKBi PA37085.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286778.
HOGENOMi HOG000016044.
HOVERGENi HBG018010.
InParanoidi O00294.
OMAi EAPESPC.
OrthoDBi EOG77HDDQ.
PhylomeDBi O00294.
TreeFami TF314076.

Miscellaneous databases

EvolutionaryTracei O00294.
GeneWikii TULP1.
GenomeRNAii 7287.
NextBioi 28491.
PROi O00294.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00294.
Bgeei O00294.
CleanExi HS_TULP1.
Genevestigatori O00294.

Family and domain databases

Gene3Di 3.20.90.10. 1 hit.
InterProi IPR000007. Tubby_C.
IPR025659. Tubby_C-like.
IPR018066. Tubby_C_CS.
[Graphical view ]
Pfami PF01167. Tub. 1 hit.
[Graphical view ]
PRINTSi PR01573. SUPERTUBBY.
SUPFAMi SSF54518. SSF54518. 1 hit.
PROSITEi PS01200. TUB_1. 1 hit.
PS01201. TUB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of TUB, TULP1, and TULP2, members of the novel tubby gene family and their possible relation to ocular diseases."
    North M.A., Naggert J.K., Yan Y., Noben-Trauth K., Nishina P.M.
    Proc. Natl. Acad. Sci. U.S.A. 94:3128-3133(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-67 AND ASN-261.
    Tissue: Retina.
  2. "TULP1 mutation in two extended Dominican kindreds with autosomal recessive retinitis pigmentosa."
    Banerjee P., Kleyn P.W., Knowles J.A., Lewis C.A., Ross B.M., Parano E., Kovats S.G., Lee J.J., Penchaszadeh G.K., Ott J., Jacobson S.G., Gilliam T.C.
    Nat. Genet. 18:177-179(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-67 AND ASN-261.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2), VARIANT ASN-261.
    Tissue: Eye.
  5. "Tubby-like protein 1 (TULP1) interacts with F-actin in photoreceptor cells."
    Xi Q., Pauer G.J.T., Marmorstein A.D., Crabb J.W., Hagstrom S.A.
    Invest. Ophthalmol. Vis. Sci. 46:4754-4761(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHOSPHATIDYLINOSITOL PHOSPHOLIPIDS, SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN.
  6. "Identification of tubby and tubby-like protein 1 as eat-me signals by phage display."
    Caberoy N.B., Maiguel D., Kim Y., Li W.
    Exp. Cell Res. 316:245-257(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS RP14 PRO-420; LYS-459; ARG-489 AND LEU-491.
  7. "Structure of human TULP1 in complex with IP3."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 291-536 IN COMPLEX WITH IP3.
  8. "Tubby-like protein-1 mutations in autosomal recessive retinitis pigmentosa."
    Gu S., Lennon A., Li Y., Lorenz B., Fossarello M., North M., Gal A., Wright A.
    Lancet 351:1103-1104(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP14 120-GLU--ASP-127 DEL; ARG-489 AND THR-496.
  9. "Recessive mutations in the gene encoding the tubby-like protein TULP1 in patients with retinitis pigmentosa."
    Hagstrom S.A., North M.A., Nishina P.M., Berson E.L., Dryja T.P.
    Nat. Genet. 18:174-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RP14 PRO-420; LYS-459 AND LEU-491.
  10. "Leber congenital amaurosis: comprehensive survey of the genetic heterogeneity, refinement of the clinical definition, and genotype-phenotype correlations as a strategy for molecular diagnosis."
    Hanein S., Perrault I., Gerber S., Tanguy G., Barbet F., Ducroq D., Calvas P., Dollfus H., Hamel C., Lopponen T., Munier F., Santos L., Shalev S., Zafeiriou D., Dufier J.-L., Munnich A., Rozet J.-M., Kaplan J.
    Hum. Mutat. 23:306-317(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LCA15 TRP-368 AND TRP-400.
  11. "A homozygosity-based search for mutations in patients with autosomal recessive retinitis pigmentosa, using microsatellite markers."
    Kondo H., Qin M., Mizota A., Kondo M., Hayashi H., Hayashi K., Oshima K., Tahira T., Hayashi K.
    Invest. Ophthalmol. Vis. Sci. 45:4433-4439(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP14 SER-382.
  12. "Novel compound heterozygous TULP1 mutations in a family with severe early-onset retinitis pigmentosa."
    den Hollander A.I., van Lith-Verhoeven J.J., Arends M.L., Strom T.M., Cremers F.P., Hoyng C.B.
    Arch. Ophthalmol. 125:932-935(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP14 TRP-482.
  13. "Novel TULP1 mutation causing Leber congenital amaurosis or early onset retinal degeneration."
    Mataftsi A., Schorderet D.F., Chachoua L., Boussalah M., Nouri M.T., Barthelmes D., Borruat F.X., Munier F.L.
    Invest. Ophthalmol. Vis. Sci. 48:5160-5167(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCA15 PHE-ALA-529 INS, VARIANTS THR-259; ASN-261 AND THR-496.

Entry informationi

Entry nameiTULP1_HUMAN
AccessioniPrimary (citable) accession number: O00294
Secondary accession number(s): O43536, Q5TGM5, Q8N571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 130 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

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