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Q96D71

- REPS1_HUMAN

UniProt

Q96D71 - REPS1_HUMAN

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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

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. SH3 domain binding Source: UniProtKB

GO - Biological processi

  1. receptor-mediated endocytosis Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ96D71.
CleanExiHS_REPS1.
ExpressionAtlasiQ96D71. baseline and differential.
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

Binary interactionsi

WithEntry#Exp.IntActNotes
NUMBP497573EBI-1171195,EBI-915016
NumbQ9QZS3-13EBI-1171195,EBI-9547433From a different organism.
NumbQ9QZS3-22EBI-1171195,EBI-3896014From a different organism.

Protein-protein interaction databases

BioGridi124433. 18 interactions.
IntActiQ96D71. 13 interactions.
STRINGi9606.ENSP00000258062.

Structurei

3D structure databases

ProteinModelPortaliQ96D71.
SMRiQ96D71. Positions 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.
GeneTreeiENSGT00760000118985.
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

        10         20         30         40         50
MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL
60 70 80 90 100
QIMELCGATR LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR
110 120 130 140 150
FVASKNEQES RHAASYSSDS ENQGSYSGVI PPPPGRGQVK KGSVSHDTVQ
160 170 180 190 200
PRTSADAQEP ASPVVSPQQS PPTSPHTWRK HSRHPSGGNS ERPLAGPGPF
210 220 230 240 250
WSPFGEAQSG SSAGDAVWSG HSPPPPQENW VSFADTPPTS TLLTMHPASV
260 270 280 290 300
QDQTTVRTVA SATTAIEIRR QSSSYDDPWK ITDEQRQYYV NQFKTIQPDL
310 320 330 340 350
NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV
360 370 380 390 400
VARKNGYDLP EKLPESLMPK LIDLEDSADV GDQPGEVGYS GSPAEAPPSK
410 420 430 440 450
SPSMPSLNQT WPELNQSSEQ WETFSERSSS SQTLTQFDSN IAPADPDTAI
460 470 480 490 500
VHPVPIRMTP SKIHMQEMEL KRTGSDHTNP TSPLLVKPSD LLEENKINSS
510 520 530 540 550
VKFASGNTVA DGYSSSDSFT SDPEQIGSNV TRQRSHSGTS PDNTAPPPPP
560 570 580 590 600
PRPQPSHSRS SSLDMNRTFT VTTGQQQAGV VAHPPAVPPR PQPSQAPGPA
610 620 630 640 650
VHRPVDADGL ITHTSTSPQQ IPEQPNFADF SQFEVFAASN VNDEQDDEAE
660 670 680 690 700
KHPEVLPAEK ASDPASSLRV AKTDSKTEEK TAASAPANVS KGTTPLAPPP
710 720 730 740 750
KPVRRRLKSE DELRPEVDEH TQKTGVLAAV LASQPSIPRS VGKDKKAIQA
760 770 780 790
SIRRNKETNT VLARLNSELQ QQLKDVLEER ISLEVQLEQL RPFSHL
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 245-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124433. 18 interactions.
IntActi Q96D71. 13 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.
GeneTreei ENSGT00760000118985.
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

Bgeei Q96D71.
CleanExi HS_REPS1.
ExpressionAtlasi Q96D71. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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