Q96D71 (REPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RalBP1-associated Eps domain-containing protein 1

Alternative name(s):
RalBP1-interacting protein 1

Gene names

Name:

REPS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	796 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15
Subcellular location	Membrane › clathrin-coated pit. Note: Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits. Ref.15
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 component	Coated pit Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Ligand	Calcium Metal-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	receptor-mediated endocytosis Inferred from electronic annotation. Source: InterPro
Cellular_component	coated pit Inferred from direct assay Ref.15. Source: UniProtKB plasma membrane Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 796	796	RalBP1-associated Eps domain-containing protein 1		PRO_0000073829
Regions
	Domain	10 – 113	104	EH 1
	Domain	285 – 374	90	EH 2
	Domain	318 – 353	36	EF-hand
	Calcium binding	331 – 342	12	Potential
	Region	652 – 796	145	Interaction with RALBP1 By similarity
	Coiled coil	751 – 791	41	Potential
	Compositional bias	541 – 604	64	Pro-rich
Amino acid modifications
	Modified residue	143	1	Phosphoserine Ref.16
	Modified residue	145	1	Phosphoserine Ref.18
	Modified residue	162	1	Phosphoserine Ref.9 Ref.11 Ref.14
	Modified residue	166	1	Phosphoserine Ref.11
	Modified residue	170	1	Phosphoserine Ref.9 Ref.11 Ref.14 Ref.18
	Modified residue	173	1	Phosphothreonine Ref.14
	Modified residue	174	1	Phosphoserine Ref.14
	Modified residue	186	1	Phosphoserine By similarity
	Modified residue	272	1	Phosphoserine By similarity
	Modified residue	288	1	Phosphotyrosine Potential
	Modified residue	307	1	Phosphoserine Ref.11
	Modified residue	489	1	Phosphoserine Ref.8
	Modified residue	540	1	Phosphoserine Ref.14
	Modified residue	562	1	Phosphoserine Ref.16 Ref.18
	Modified residue	709	1	Phosphoserine Ref.12 Ref.18
	Modified residue	740	1	Phosphoserine Ref.16
Natural variations
	Alternative sequence	420 – 446	27	Missing in isoform 2.		VSP_007953
	Alternative sequence	510 – 573	64	Missing in isoform 2.		VSP_007954
	Alternative sequence	510	1	Missing in isoform 3.		VSP_007955
Experimental info
	Sequence conflict	628	1	A → V in AAK34942. Ref.5
	Sequence conflict	717	1	V → I in CAD38569. Ref.6
	Sequence conflict	794 – 795	2	SH → FP in AAH12764. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 3, 2009. Version 3. Checksum: FAD7A57ED6206922	FASTA	796	86,662
	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
	Isoform 2 [UniParc]. Checksum: C375BFF6E173C843	FASTA	705	76,838
	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 WPELNQSSED 430 440 450 460 470 480 TAIVHPVPIR MTPSKIHMQE MELKRTGSDH TNPTSPLLVK PSDLLEENKI NSSVKFASGN 490 500 510 520 530 540 TVGQQQAGVV AHPPAVPPRP QPSQAPGPAV HRPVDADGLI THTSTSPQQI PEQPNFADFS 550 560 570 580 590 600 QFEVFAASNV NDEQDDEAEK HPEVLPAEKA SDPASSLRVA KTDSKTEEKT AASAPANVSK 610 620 630 640 650 660 GTTPLAPPPK PVRRRLKSED ELRPEVDEHT QKTGVLAAVL ASQPSIPRSV GKDKKAIQAS 670 680 690 700 IRRNKETNTV LARLNSELQQ QLKDVLEERI SLEVQLEQLR PFSHL
	Isoform 3 [UniParc]. Checksum: 2D6D923DD16DF61C	FASTA	795	86,591
	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 VKFASGNTVD GYSSSDSFTS DPEQIGSNVT RQRSHSGTSP 550 560 570 580 590 600 DNTAPPPPPP RPQPSHSRSS SLDMNRTFTV TTGQQQAGVV AHPPAVPPRP QPSQAPGPAV 610 620 630 640 650 660 HRPVDADGLI THTSTSPQQI PEQPNFADFS QFEVFAASNV NDEQDDEAEK HPEVLPAEKA 670 680 690 700 710 720 SDPASSLRVA KTDSKTEEKT AASAPANVSK GTTPLAPPPK PVRRRLKSED ELRPEVDEHT 730 740 750 760 770 780 QKTGVLAAVL ASQPSIPRSV GKDKKAIQAS IRRNKETNTV LARLNSELQQ QLKDVLEERI 790 SLEVQLEQLR PFSHL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[13]	"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].
[14]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"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, MASS SPECTROMETRY.
+	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. 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. AL831900 mRNA. Translation: CAD38569.1.
IPI	IPI00783030. IPI00938352. IPI00940373.
RefSeq	NP_001122089.1. NM_001128617.1. NP_114128.3. NM_031922.3.
UniGene	Hs.334603.
3D structure databases
ProteinModelPortal	Q96D71.
SMR	Q96D71. Positions 279-370.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96D71. 9 interactions.
STRING	9606.ENSP00000258062.
PTM databases
PhosphoSite	Q96D71.
Polymorphism databases
DMDM	262527572.
Proteomic databases
PaxDb	Q96D71.
PRIDE	Q96D71.
Protocols and materials databases
DNASU	85021.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000258062; ENSP00000258062; ENSG00000135597. ENST00000409812; ENSP00000386699; ENSG00000135597. ENST00000450536; ENSP00000392065; ENSG00000135597.
GeneID	85021.
KEGG	hsa:85021.
UCSC	uc003qig.4. human. uc003qij.3. human. uc011edr.2. human.
Organism-specific databases
CTD	85021.
GeneCards	GC06M139267.
HGNC	HGNC:15578. REPS1.
HPA	HPA029961.
MIM	614825. gene.
neXtProt	NX_Q96D71.
PharmGKB	PA34329.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG313227.
HOVERGEN	HBG056372.
InParanoid	Q96D71.
OMA	EQKYYSD.
OrthoDB	EOG4Z36D5.
Gene expression databases
ArrayExpress	Q96D71.
Bgee	Q96D71.
CleanEx	HS_REPS1.
Genevestigator	Q96D71.
GermOnline	ENSG00000135597. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 2 hits.
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000261. EPS15_homology. IPR026814. Reps. [Graphical view]
PANTHER	PTHR11216:SF33. PTHR11216:SF33. 1 hit.
SMART	SM00027. EH. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50031. EH. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	REPS1. human.
GenomeRNAi	85021.
NextBio	75659.
PMAP-CutDB	Q96D71.
SOURCE	Search...

Entry information

Entry name

REPS1_HUMAN

Accession

Primary (citable) accession number: Q96D71
Secondary accession number(s): B7ZBZ8 , B7ZBZ9, B7ZC00, Q5JWJ5, Q5JWJ6, Q5JWJ7, Q8NDR7, Q8WU62, Q9BXY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	November 3, 2009
Last modified:	May 1, 2013
This is version 110 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.