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Q96D71 (REPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RalBP1-associated Eps domain-containing protein 1
Alternative name(s):
RalBP1-interacting protein 1
Gene names
Name:REPS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length796 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May coordinate the cellular actions of activated EGF receptors and Ral-GTPases By similarity.

Subunit structure

Homodimer Potential. Interacts with RAB11FIP2. Interacts with RALBP1, CRK and GRB2. Binding to RALBP1 does not affect its Ral-binding activity. Forms a complex with the SH3 domains of CRK and GRB2 which may link it to an EGF-responsive tyrosine kinase By similarity. Interacts with AMPH, ITSN1 (via SH3 domains) and SGIP1; may be involved in clathrin-mediated endocytosis. Ref.7 Ref.16

Subcellular location

Membraneclathrin-coated pit. Note: Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits. Ref.16

Tissue specificity

Widely expressed with highest levels in heart and testis. Ref.5

Post-translational modification

EGF stimulates phosphorylation on Tyr-residues By similarity.

Sequence similarities

Contains 1 EF-hand domain.

Contains 2 EH domains.

Sequence caution

The sequence AAH12764.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH21211.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAK34942.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCoated pit
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   LigandCalcium
Metal-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcoated pit

Inferred from direct assay Ref.16. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from physical interaction Ref.16. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96D71-1)

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.
Isoform 2 (identifier: Q96D71-2)

The sequence of this isoform differs from the canonical sequence as follows:
     420-446: Missing.
     510-573: Missing.
Isoform 3 (identifier: Q96D71-3)

The sequence of this isoform differs from the canonical sequence as follows:
     510-510: Missing.
Isoform 4 (identifier: Q96D71-4)

The sequence of this isoform differs from the canonical sequence as follows:
     420-446: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 796796RalBP1-associated Eps domain-containing protein 1
PRO_0000073829

Regions

Domain10 – 113104EH 1
Domain285 – 37490EH 2
Domain318 – 35336EF-hand
Calcium binding331 – 34212 Potential
Region652 – 796145Interaction with RALBP1 By similarity
Coiled coil751 – 79141 Potential
Compositional bias541 – 60464Pro-rich

Amino acid modifications

Modified residue1431Phosphoserine Ref.17
Modified residue1451Phosphoserine Ref.19
Modified residue1621Phosphoserine Ref.9 Ref.11 Ref.15
Modified residue1661Phosphoserine Ref.11
Modified residue1701Phosphoserine Ref.9 Ref.11 Ref.15 Ref.19
Modified residue1731Phosphothreonine Ref.15
Modified residue1741Phosphoserine Ref.15
Modified residue2721Phosphoserine By similarity
Modified residue2881Phosphotyrosine Potential
Modified residue3071Phosphoserine Ref.11
Modified residue4891Phosphoserine Ref.8
Modified residue5401Phosphoserine Ref.15
Modified residue5621Phosphoserine Ref.17 Ref.19
Modified residue7091Phosphoserine Ref.12 Ref.19
Modified residue7401Phosphoserine Ref.17

Natural variations

Alternative sequence420 – 44627Missing in isoform 2 and isoform 4.
VSP_007953
Alternative sequence510 – 57364Missing in isoform 2.
VSP_007954
Alternative sequence5101Missing in isoform 3.
VSP_007955

Experimental info

Sequence conflict6281A → V in AAK34942. Ref.5
Sequence conflict7171V → I in CAD38569. Ref.6
Sequence conflict794 – 7952SH → FP in AAH12764. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 3, 2009. Version 3.
Checksum: FAD7A57ED6206922

FASTA79686,662
        10         20         30         40         50         60 
MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL QIMELCGATR 

        70         80         90        100        110        120 
LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR FVASKNEQES RHAASYSSDS 

       130        140        150        160        170        180 
ENQGSYSGVI PPPPGRGQVK KGSVSHDTVQ PRTSADAQEP ASPVVSPQQS PPTSPHTWRK 

       190        200        210        220        230        240 
HSRHPSGGNS ERPLAGPGPF WSPFGEAQSG SSAGDAVWSG HSPPPPQENW VSFADTPPTS 

       250        260        270        280        290        300 
TLLTMHPASV QDQTTVRTVA SATTAIEIRR QSSSYDDPWK ITDEQRQYYV NQFKTIQPDL 

       310        320        330        340        350        360 
NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV VARKNGYDLP 

       370        380        390        400        410        420 
EKLPESLMPK LIDLEDSADV GDQPGEVGYS GSPAEAPPSK SPSMPSLNQT WPELNQSSEQ 

       430        440        450        460        470        480 
WETFSERSSS SQTLTQFDSN IAPADPDTAI VHPVPIRMTP SKIHMQEMEL KRTGSDHTNP 

       490        500        510        520        530        540 
TSPLLVKPSD LLEENKINSS VKFASGNTVA DGYSSSDSFT SDPEQIGSNV TRQRSHSGTS 

       550        560        570        580        590        600 
PDNTAPPPPP PRPQPSHSRS SSLDMNRTFT VTTGQQQAGV VAHPPAVPPR PQPSQAPGPA 

       610        620        630        640        650        660 
VHRPVDADGL ITHTSTSPQQ IPEQPNFADF SQFEVFAASN VNDEQDDEAE KHPEVLPAEK 

       670        680        690        700        710        720 
ASDPASSLRV AKTDSKTEEK TAASAPANVS KGTTPLAPPP KPVRRRLKSE DELRPEVDEH 

       730        740        750        760        770        780 
TQKTGVLAAV LASQPSIPRS VGKDKKAIQA SIRRNKETNT VLARLNSELQ QQLKDVLEER 

       790 
ISLEVQLEQL RPFSHL 

« Hide

Isoform 2 [UniParc].

Checksum: C375BFF6E173C843
Show »

FASTA70576,838
Isoform 3 [UniParc].

Checksum: 2D6D923DD16DF61C
Show »

FASTA79586,591
Isoform 4 [UniParc].

Checksum: 9AC8680B338B86D2
Show »

FASTA76983,650

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
[2]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORMS 2 AND 3).
Tissue: Brain and Lymph.
[4]"Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes."
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R. expand/collapse author list , Kanda K., Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.
Genome Res. 16:55-65(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-159 (ISOFORM 1).
Tissue: Uterus.
[5]"Cloning, expression and characterization of a novel human REPS1 gene."
Xu J., Zhou Z., Zeng L., Huang Y., Zhao W., Cheng C., Xu M., Xie Y., Mao Y.
Biochim. Biophys. Acta 1522:118-121(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-796 (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Fetal brain.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-796 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-796 (ISOFORM 1).
Tissue: Brain.
[7]"Rab11-FIP2, an adaptor protein connecting cellular components involved in internalization and recycling of epidermal growth factor receptors."
Cullis D.N., Philip B., Baleja J.D., Feig L.A.
J. Biol. Chem. 277:49158-49166(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB11FIP2.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-166; SER-170 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-170; THR-173; SER-174 AND SER-540, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits."
Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J., Rynditch A.
Biochem. Biophys. Res. Commun. 402:408-413(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMPH; ITSN1 AND SGIP1, SUBCELLULAR LOCATION.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-562 AND SER-740, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-170; SER-562 AND SER-709, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL121834, AL590308 Genomic DNA. Translation: CAI42877.2.
AL121834, AL590308 Genomic DNA. Translation: CAI42878.2.
AL121834, AL590308 Genomic DNA. Translation: CAI42879.2.
AL590308, AL121834 Genomic DNA. Translation: CAX15096.1.
AL590308, AL121834 Genomic DNA. Translation: CAX15097.1.
AL590308, AL121834 Genomic DNA. Translation: CAX15098.1.
AL591033 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW47904.1.
CH471051 Genomic DNA. Translation: EAW47906.1.
CH471051 Genomic DNA. Translation: EAW47907.1.
BC012764 mRNA. Translation: AAH12764.1. Different initiation.
BC021211 mRNA. Translation: AAH21211.1. Different initiation.
DB263697 mRNA. No translation available.
AF251052 mRNA. Translation: AAK34942.1. Different initiation.
AL832307 mRNA. No translation available.
AL831900 mRNA. Translation: CAD38569.1.
CCDSCCDS5193.2. [Q96D71-3]
CCDS69212.1. [Q96D71-2]
CCDS69213.1. [Q96D71-1]
RefSeqNP_001122089.1. NM_001128617.2. [Q96D71-4]
NP_001273540.1. NM_001286611.1. [Q96D71-1]
NP_001273541.1. NM_001286612.1. [Q96D71-2]
NP_114128.3. NM_031922.4. [Q96D71-3]
UniGeneHs.334603.
Hs.732041.

3D structure databases

ProteinModelPortalQ96D71.
SMRQ96D71. Positions 13-74, 245-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124433. 13 interactions.
IntActQ96D71. 11 interactions.
STRING9606.ENSP00000258062.

PTM databases

PhosphoSiteQ96D71.

Polymorphism databases

DMDM262527572.

Proteomic databases

MaxQBQ96D71.
PaxDbQ96D71.
PRIDEQ96D71.

Protocols and materials databases

DNASU85021.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258062; ENSP00000258062; ENSG00000135597. [Q96D71-3]
ENST00000367663; ENSP00000356635; ENSG00000135597.
ENST00000409812; ENSP00000386699; ENSG00000135597. [Q96D71-2]
ENST00000450536; ENSP00000392065; ENSG00000135597. [Q96D71-1]
GeneID85021.
KEGGhsa:85021.
UCSCuc003qii.3. human. [Q96D71-1]
uc003qij.3. human. [Q96D71-2]
uc011edr.2. human. [Q96D71-3]

Organism-specific databases

CTD85021.
GeneCardsGC06M139267.
HGNCHGNC:15578. REPS1.
HPAHPA029961.
MIM614825. gene.
neXtProtNX_Q96D71.
PharmGKBPA34329.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313227.
HOVERGENHBG056372.
InParanoidQ96D71.
OMAEQKYYSD.
OrthoDBEOG7B31MB.
PhylomeDBQ96D71.
TreeFamTF316546.

Gene expression databases

ArrayExpressQ96D71.
BgeeQ96D71.
CleanExHS_REPS1.
GenevestigatorQ96D71.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR026814. Reps1.
[Graphical view]
PANTHERPTHR11216:SF63. PTHR11216:SF63. 1 hit.
SMARTSM00027. EH. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSREPS1. human.
GeneWikiREPS1.
GenomeRNAi85021.
NextBio35535078.
PMAP-CutDBQ96D71.
PROQ96D71.
SOURCESearch...

Entry information

Entry nameREPS1_HUMAN
AccessionPrimary (citable) accession number: Q96D71
Secondary accession number(s): B7ZBZ8 expand/collapse secondary AC list , B7ZBZ9, B7ZC00, J3KP76, Q5JWJ5, Q5JWJ6, Q5JWJ7, Q8NDR7, Q8WU62, Q9BXY9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: November 3, 2009
Last modified: July 9, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM