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Q96D71

- REPS1_HUMAN

UniProt

Q96D71 - REPS1_HUMAN

Protein

RalBP1-associated Eps domain-containing protein 1

Gene

REPS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (03 Nov 2009)
      Previous versions | rss
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    Functioni

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi331 – 34212PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. receptor-mediated endocytosis Source: InterPro

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RalBP1-associated Eps domain-containing protein 1
    Alternative name(s):
    RalBP1-interacting protein 1
    Gene namesi
    Name:REPS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:15578. REPS1.

    Subcellular locationi

    Membraneclathrin-coated pit 1 Publication
    Note: Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits.

    GO - Cellular componenti

    1. coated pit Source: UniProtKB
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Coated pit, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34329.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 796796RalBP1-associated Eps domain-containing protein 1PRO_0000073829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei143 – 1431Phosphoserine1 Publication
    Modified residuei145 – 1451Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine3 Publications
    Modified residuei166 – 1661Phosphoserine1 Publication
    Modified residuei170 – 1701Phosphoserine4 Publications
    Modified residuei173 – 1731Phosphothreonine1 Publication
    Modified residuei174 – 1741Phosphoserine1 Publication
    Modified residuei272 – 2721PhosphoserineBy similarity
    Modified residuei288 – 2881PhosphotyrosineSequence Analysis
    Modified residuei307 – 3071Phosphoserine1 Publication
    Modified residuei489 – 4891Phosphoserine1 Publication
    Modified residuei540 – 5401Phosphoserine1 Publication
    Modified residuei562 – 5621Phosphoserine2 Publications
    Modified residuei709 – 7091Phosphoserine2 Publications
    Modified residuei740 – 7401Phosphoserine1 Publication

    Post-translational modificationi

    EGF stimulates phosphorylation on Tyr-residues.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96D71.
    PaxDbiQ96D71.
    PRIDEiQ96D71.

    PTM databases

    PhosphoSiteiQ96D71.

    Miscellaneous databases

    PMAP-CutDBQ96D71.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in heart and testis.1 Publication

    Gene expression databases

    ArrayExpressiQ96D71.
    BgeeiQ96D71.
    CleanExiHS_REPS1.
    GenevestigatoriQ96D71.

    Organism-specific databases

    HPAiHPA029961.

    Interactioni

    Subunit structurei

    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.By similarity2 PublicationsCurated

    Protein-protein interaction databases

    BioGridi124433. 14 interactions.
    IntActiQ96D71. 11 interactions.
    STRINGi9606.ENSP00000258062.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96D71.
    SMRiQ96D71. Positions 13-74, 245-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 113104EH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini285 – 37490EH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini318 – 35336EF-handPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni652 – 796145Interaction with RALBP1By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili751 – 79141Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi541 – 60464Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 2 EH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG313227.
    HOVERGENiHBG056372.
    InParanoidiQ96D71.
    OMAiEQKYYSD.
    OrthoDBiEOG7B31MB.
    PhylomeDBiQ96D71.
    TreeFamiTF316546.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR026814. Reps1.
    [Graphical view]
    PANTHERiPTHR11216:SF63. PTHR11216:SF63. 1 hit.
    SMARTiSM00027. EH. 2 hits.
    [Graphical view]
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50031. EH. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96D71-1) [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

    MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL    50
    QIMELCGATR LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR 100
    FVASKNEQES RHAASYSSDS ENQGSYSGVI PPPPGRGQVK KGSVSHDTVQ 150
    PRTSADAQEP ASPVVSPQQS PPTSPHTWRK HSRHPSGGNS ERPLAGPGPF 200
    WSPFGEAQSG SSAGDAVWSG HSPPPPQENW VSFADTPPTS TLLTMHPASV 250
    QDQTTVRTVA SATTAIEIRR QSSSYDDPWK ITDEQRQYYV NQFKTIQPDL 300
    NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV 350
    VARKNGYDLP EKLPESLMPK LIDLEDSADV GDQPGEVGYS GSPAEAPPSK 400
    SPSMPSLNQT WPELNQSSEQ WETFSERSSS SQTLTQFDSN IAPADPDTAI 450
    VHPVPIRMTP SKIHMQEMEL KRTGSDHTNP TSPLLVKPSD LLEENKINSS 500
    VKFASGNTVA DGYSSSDSFT SDPEQIGSNV TRQRSHSGTS PDNTAPPPPP 550
    PRPQPSHSRS SSLDMNRTFT VTTGQQQAGV VAHPPAVPPR PQPSQAPGPA 600
    VHRPVDADGL ITHTSTSPQQ IPEQPNFADF SQFEVFAASN VNDEQDDEAE 650
    KHPEVLPAEK ASDPASSLRV AKTDSKTEEK TAASAPANVS KGTTPLAPPP 700
    KPVRRRLKSE DELRPEVDEH TQKTGVLAAV LASQPSIPRS VGKDKKAIQA 750
    SIRRNKETNT VLARLNSELQ QQLKDVLEER ISLEVQLEQL RPFSHL 796
    Length:796
    Mass (Da):86,662
    Last modified:November 3, 2009 - v3
    Checksum:iFAD7A57ED6206922
    GO
    Isoform 2 (identifier: Q96D71-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         420-446: Missing.
         510-573: Missing.

    Show »
    Length:705
    Mass (Da):76,838
    Checksum:iC375BFF6E173C843
    GO
    Isoform 3 (identifier: Q96D71-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         510-510: Missing.

    Show »
    Length:795
    Mass (Da):86,591
    Checksum:i2D6D923DD16DF61C
    GO
    Isoform 4 (identifier: Q96D71-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:769
    Mass (Da):83,650
    Checksum:i9AC8680B338B86D2
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti628 – 6281A → V in AAK34942. (PubMed:11750063)Curated
    Sequence conflicti717 – 7171V → I in CAD38569. (PubMed:17974005)Curated
    Sequence conflicti794 – 7952SH → FP in AAH12764. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei420 – 44627Missing in isoform 2 and isoform 4. 2 PublicationsVSP_007953Add
    BLAST
    Alternative sequencei510 – 57364Missing in isoform 2. 1 PublicationVSP_007954Add
    BLAST
    Alternative sequencei510 – 5101Missing in isoform 3. 1 PublicationVSP_007955

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS47488.1. [Q96D71-4]
    CCDS5193.2. [Q96D71-3]
    CCDS69212.1. [Q96D71-2]
    CCDS69213.1. [Q96D71-1]
    RefSeqiNP_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]
    UniGeneiHs.334603.
    Hs.732041.

    Genome annotation databases

    EnsembliENST00000258062; ENSP00000258062; ENSG00000135597. [Q96D71-3]
    ENST00000367663; ENSP00000356635; ENSG00000135597. [Q96D71-4]
    ENST00000409812; ENSP00000386699; ENSG00000135597. [Q96D71-2]
    ENST00000450536; ENSP00000392065; ENSG00000135597. [Q96D71-1]
    GeneIDi85021.
    KEGGihsa:85021.
    UCSCiuc003qii.3. human. [Q96D71-1]
    uc003qij.3. human. [Q96D71-2]
    uc011edr.2. human. [Q96D71-3]

    Polymorphism databases

    DMDMi262527572.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS47488.1. [Q96D71-4 ]
    CCDS5193.2. [Q96D71-3 ]
    CCDS69212.1. [Q96D71-2 ]
    CCDS69213.1. [Q96D71-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.334603.
    Hs.732041.

    3D structure databases

    ProteinModelPortali Q96D71.
    SMRi Q96D71. Positions 13-74, 245-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124433. 14 interactions.
    IntActi Q96D71. 11 interactions.
    STRINGi 9606.ENSP00000258062.

    PTM databases

    PhosphoSitei Q96D71.

    Polymorphism databases

    DMDMi 262527572.

    Proteomic databases

    MaxQBi Q96D71.
    PaxDbi Q96D71.
    PRIDEi Q96D71.

    Protocols and materials databases

    DNASUi 85021.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258062 ; ENSP00000258062 ; ENSG00000135597 . [Q96D71-3 ]
    ENST00000367663 ; ENSP00000356635 ; ENSG00000135597 . [Q96D71-4 ]
    ENST00000409812 ; ENSP00000386699 ; ENSG00000135597 . [Q96D71-2 ]
    ENST00000450536 ; ENSP00000392065 ; ENSG00000135597 . [Q96D71-1 ]
    GeneIDi 85021.
    KEGGi hsa:85021.
    UCSCi uc003qii.3. human. [Q96D71-1 ]
    uc003qij.3. human. [Q96D71-2 ]
    uc011edr.2. human. [Q96D71-3 ]

    Organism-specific databases

    CTDi 85021.
    GeneCardsi GC06M139267.
    HGNCi HGNC:15578. REPS1.
    HPAi HPA029961.
    MIMi 614825. gene.
    neXtProti NX_Q96D71.
    PharmGKBi PA34329.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313227.
    HOVERGENi HBG056372.
    InParanoidi Q96D71.
    OMAi EQKYYSD.
    OrthoDBi EOG7B31MB.
    PhylomeDBi Q96D71.
    TreeFami TF316546.

    Miscellaneous databases

    ChiTaRSi REPS1. human.
    GeneWikii REPS1.
    GenomeRNAii 85021.
    NextBioi 35535078.
    PMAP-CutDB Q96D71.
    PROi Q96D71.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96D71.
    Bgeei Q96D71.
    CleanExi HS_REPS1.
    Genevestigatori Q96D71.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR026814. Reps1.
    [Graphical view ]
    PANTHERi PTHR11216:SF63. PTHR11216:SF63. 1 hit.
    SMARTi SM00027. EH. 2 hits.
    [Graphical view ]
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50031. EH. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    11. 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. 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. 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].

    Entry informationi

    Entry nameiREPS1_HUMAN
    AccessioniPrimary (citable) accession number: Q96D71
    Secondary accession number(s): B7ZBZ8
    , B7ZBZ9, B7ZC00, J3KP76, Q5JWJ5, Q5JWJ6, Q5JWJ7, Q8NDR7, Q8WU62, Q9BXY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 124 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3