O54916 (REPS1_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	795 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.
Subunit structure	Homodimer Potential. 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. Interacts with RAB11FIP2 By similarity. Interacts with AMPH, ITSN1 (via SH3 domains) and SGIP1; may be involved in clathrin-mediated endocytosis By similarity.
Subcellular location	Membrane › clathrin-coated pit By similarity. Note: Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits By similarity.
Tissue specificity	Expressed in all tissues examined. The highest level expression was found in the kidney and testis.
Post-translational modification	EGF stimulates phosphorylation on Tyr-residues.
Sequence similarities	Contains 1 EF-hand domain. Contains 2 EH domains.
Sequence caution	The sequence BAE29439.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE30291.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Coated pit Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Ligand	Calcium Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	receptor-mediated endocytosis Inferred from electronic annotation. Source: InterPro
Cellular_component	coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O54916-1)

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: O54916-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.
     420-454: QWETFSERSSSSQTLTQFDSNIAPADPDTAIVHPV → VSKTSLSLLEISLFTGRSFKQDRFTAGYLQYAHTP
     455-795: Missing.

Note: Due to intron retention. No experimental confirmation available.

Isoform 3 (identifier: O54916-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     420-446: Missing.

Isoform 4 (identifier: O54916-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 795

795

RalBP1-associated Eps domain-containing protein 1

PRO_0000073830

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

651 – 795

145

Interaction with RALBP1

Coiled coil

750 – 790

41

Potential

Compositional bias

540 – 603

64

Pro-rich

Amino acid modifications

Modified residue

145

1

Phosphoserine By similarity

Modified residue

162

1

Phosphoserine By similarity

Modified residue

166

1

Phosphoserine By similarity

Modified residue

170

1

Phosphoserine By similarity

Modified residue

173

1

Phosphothreonine By similarity

Modified residue

174

1

Phosphoserine By similarity

Modified residue

186

1

Phosphoserine Ref.6

Modified residue

272

1

Phosphoserine Ref.5

Modified residue

288

1

Phosphotyrosine Potential

Modified residue

307

1

Phosphoserine By similarity

Modified residue

489

1

Phosphoserine By similarity

Modified residue

539

1

Phosphoserine By similarity

Modified residue

561

1

Phosphoserine Ref.7

Modified residue

708

1

Phosphoserine Ref.6 Ref.7

Modified residue

739

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 244

244

Missing in isoform 2.

VSP_038337

Alternative sequence

1 – 52

52

Missing in isoform 3 and isoform 4.

VSP_038336

Alternative sequence

420 – 454

35

QWETF…IVHPV → VSKTSLSLLEISLFTGRSFK QDRFTAGYLQYAHTP in isoform 2.

VSP_007956

Alternative sequence

420 – 446

27

Missing in isoform 3.

VSP_038338

Alternative sequence

455 – 795

341

Missing in isoform 2.

VSP_007957

Experimental info

Sequence conflict

161

1

V → A in AAB94736. Ref.1

Sequence conflict

605

1

D → N in BAE29439. Ref.2

Sequence conflict

701

1

P → T in BAE29439. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

795

Helix Strand Turn

Details...

Helix

283 – 293

11

Turn

294 – 296

3

Beta strand

303 – 305

3

Helix

306 – 316

11

Helix

320 – 330

11

Beta strand

335 – 339

5

Helix

340 – 355

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 3, 2009. Version 2. Checksum: 98D788160F560509	FASTA	795	86,519
	10 20 30 40 50 60 MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL QIMELCGATR 70 80 90 100 110 120 LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR FVASKNEQES RLAASYSSDS 130 140 150 160 170 180 ENQGSYSGVI PPPPGRGQVK KGPGSHDAVQ PRPSAEQQEP VSPVVSPQQS PPTSPHTWRK 190 200 210 220 230 240 HSRHPSGGNS ERPLTGPGPF WSPFGDAQAG SSAGDAVWSG QSPPPPQDNW VSFADTPPTS 250 260 270 280 290 300 ALLTMHPASV QDQTTVRTVA SAATANEIRR QSSSYEDPWK ITDEQRQYYV NQFKTIQPDL 310 320 330 340 350 360 NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV VARKNGYDLP 370 380 390 400 410 420 EKLPESLMPK LIDLEDSADV GEQPGEVGYS GSPAEAPPSK SPSMPSLNQT WPELNQSSEQ 430 440 450 460 470 480 WETFSERSSS SQTLTQFDSN IAPADPDTAI VHPVPIRMTP SKIHMQEMEL KRTSSDHTNP 490 500 510 520 530 540 TSPLLVKPSD LSEENKINSS VKFPSGNTVD GYSSSDSFPS DPEQIGSSVT RQRSHSGTSP 550 560 570 580 590 600 DNTAPPPPPP RPQPSHSRSS SLDMNRTFAV TTGQQQAGVV AHPPAVPPRP QPSQAPGPSV 610 620 630 640 650 660 HRPVDADGLI THTSTSPQQI PEQPNFADFS QFEVFAASNV SEEQDSEAEK HPEVLPAEKA 670 680 690 700 710 720 SDPSSSLRAA QADSKAEEKT ATNVPANVSK GTTPLAPPPK PVRRRLKSED ELRPDVDEHT 730 740 750 760 770 780 QKTGVLAAVL TSQPSIPRSV GKDKKAIQAS IRRNKETNTV LARLNSELQQ QLKDVLEERI 790 SLEVQLEQLR PFSHL
	Isoform 2 [UniParc]. Checksum: 0F50314C618EC731	FASTA	210	23,378
	10 20 30 40 50 60 MHPASVQDQT TVRTVASAAT ANEIRRQSSS YEDPWKITDE QRQYYVNQFK TIQPDLNGFI 70 80 90 100 110 120 PGSAAKEFFT KSKLPILELS HIWELSDFDK DGALTLDEFC AAFHLVVARK NGYDLPEKLP 130 140 150 160 170 180 ESLMPKLIDL EDSADVGEQP GEVGYSGSPA EAPPSKSPSM PSLNQTWPEL NQSSEVSKTS 190 200 210 LSLLEISLFT GRSFKQDRFT AGYLQYAHTP
	Isoform 3 [UniParc]. Checksum: 2D37A40F959AA466	FASTA	716	77,614
	10 20 30 40 50 60 MELCGATRLG YFGRSQFYIA LKLVAVAQSG FPLRVESINT VKDLPLPRFV ASKNEQESRL 70 80 90 100 110 120 AASYSSDSEN QGSYSGVIPP PPGRGQVKKG PGSHDAVQPR PSAEQQEPVS PVVSPQQSPP 130 140 150 160 170 180 TSPHTWRKHS RHPSGGNSER PLTGPGPFWS PFGDAQAGSS AGDAVWSGQS PPPPQDNWVS 190 200 210 220 230 240 FADTPPTSAL LTMHPASVQD QTTVRTVASA ATANEIRRQS SSYEDPWKIT DEQRQYYVNQ 250 260 270 280 290 300 FKTIQPDLNG FIPGSAAKEF FTKSKLPILE LSHIWELSDF DKDGALTLDE FCAAFHLVVA 310 320 330 340 350 360 RKNGYDLPEK LPESLMPKLI DLEDSADVGE QPGEVGYSGS PAEAPPSKSP SMPSLNQTWP 370 380 390 400 410 420 ELNQSSEDTA IVHPVPIRMT PSKIHMQEME LKRTSSDHTN PTSPLLVKPS DLSEENKINS 430 440 450 460 470 480 SVKFPSGNTV DGYSSSDSFP SDPEQIGSSV TRQRSHSGTS PDNTAPPPPP PRPQPSHSRS 490 500 510 520 530 540 SSLDMNRTFA VTTGQQQAGV VAHPPAVPPR PQPSQAPGPS VHRPVDADGL ITHTSTSPQQ 550 560 570 580 590 600 IPEQPNFADF SQFEVFAASN VSEEQDSEAE KHPEVLPAEK ASDPSSSLRA AQADSKAEEK 610 620 630 640 650 660 TATNVPANVS KGTTPLAPPP KPVRRRLKSE DELRPDVDEH TQKTGVLAAV LTSQPSIPRS 670 680 690 700 710 VGKDKKAIQA SIRRNKETNT VLARLNSELQ QQLKDVLEER ISLEVQLEQL RPFSHL
	Isoform 4 [UniParc]. Checksum: 205B87DD9D8AC3A6	FASTA	743	80,626
	10 20 30 40 50 60 MELCGATRLG YFGRSQFYIA LKLVAVAQSG FPLRVESINT VKDLPLPRFV ASKNEQESRL 70 80 90 100 110 120 AASYSSDSEN QGSYSGVIPP PPGRGQVKKG PGSHDAVQPR PSAEQQEPVS PVVSPQQSPP 130 140 150 160 170 180 TSPHTWRKHS RHPSGGNSER PLTGPGPFWS PFGDAQAGSS AGDAVWSGQS PPPPQDNWVS 190 200 210 220 230 240 FADTPPTSAL LTMHPASVQD QTTVRTVASA ATANEIRRQS SSYEDPWKIT DEQRQYYVNQ 250 260 270 280 290 300 FKTIQPDLNG FIPGSAAKEF FTKSKLPILE LSHIWELSDF DKDGALTLDE FCAAFHLVVA 310 320 330 340 350 360 RKNGYDLPEK LPESLMPKLI DLEDSADVGE QPGEVGYSGS PAEAPPSKSP SMPSLNQTWP 370 380 390 400 410 420 ELNQSSEQWE TFSERSSSSQ TLTQFDSNIA PADPDTAIVH PVPIRMTPSK IHMQEMELKR 430 440 450 460 470 480 TSSDHTNPTS PLLVKPSDLS EENKINSSVK FPSGNTVDGY SSSDSFPSDP EQIGSSVTRQ 490 500 510 520 530 540 RSHSGTSPDN TAPPPPPPRP QPSHSRSSSL DMNRTFAVTT GQQQAGVVAH PPAVPPRPQP 550 560 570 580 590 600 SQAPGPSVHR PVDADGLITH TSTSPQQIPE QPNFADFSQF EVFAASNVSE EQDSEAEKHP 610 620 630 640 650 660 EVLPAEKASD PSSSLRAAQA DSKAEEKTAT NVPANVSKGT TPLAPPPKPV RRRLKSEDEL 670 680 690 700 710 720 RPDVDEHTQK TGVLAAVLTS QPSIPRSVGK DKKAIQASIR RNKETNTVLA RLNSELQQQL 730 740 KDVLEERISL EVQLEQLRPF SHL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An eps homology (EH) domain protein that binds to the ral-GTPase target, RalBP1." Yamaguchi A., Urano T., Goi T., Feig L.A. J. Biol. Chem. 272:31230-31234(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), CHARACTERIZATION. Tissue: Muscle.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-795 (ISOFORM 1). Strain: C57BL/6J. Tissue: Bone marrow and Thymus.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-795 (ISOFORM 1). Tissue: Embryo and Mammary tumor.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-708, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-708, MASS SPECTROMETRY. Tissue: Macrophage.
[8]	"Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences." Kim S., Cullis D.N., Feig L.A., Baleja J.D. Biochemistry 40:6776-6785(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 279-370.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF031939 mRNA. Translation: AAB94736.1.
AK150284 mRNA. Translation: BAE29439.1. Different initiation.
AK151309 mRNA. Translation: BAE30291.1. Different initiation.
AK041967 mRNA. Translation: BAC31117.1.
AC153433 Genomic DNA. No translation available.
BC002256 mRNA. No translation available.
BC087547 mRNA. Translation: AAH87547.1.

IPI

IPI00119795.
IPI00338228.
IPI00880345.
IPI00918818.

PIR

T09173.

RefSeq

NP_001104535.1. NM_001111065.1.
NP_033074.2. NM_009048.2.

UniGene

Mm.4479.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FI6	NMR	-	A	279-370	[»]

ProteinModelPortal

O54916.

SMR

O54916. Positions 279-370.

ModBase

Search...

Protein-protein interaction databases

IntAct

O54916. 2 interactions.

PTM databases

PhosphoSite

O54916.

Proteomic databases

PaxDb

O54916.

PRIDE

O54916.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000126390; ENSMUSP00000123238; ENSMUSG00000019854.

GeneID

19707.

KEGG

mmu:19707.

UCSC

uc007ema.2. mouse.

Organism-specific databases

CTD

85021.

MGI

MGI:1196373. Reps1.

Phylogenomic databases

eggNOG

NOG313227.

GeneTree

ENSGT00530000063792.

HOGENOM

HOG000231382.

HOVERGEN

HBG056372.

InParanoid

Q3UAM3.

OMA

EQKYYSD.

OrthoDB

EOG4Z36D5.

Gene expression databases

ArrayExpress

O54916.

Bgee

O54916.

CleanEx

MM_REPS1.

Genevestigator

O54916.

GermOnline

ENSMUSG00000019854. Mus musculus.

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. mouse.

EvolutionaryTrace

O54916.

NextBio

297082.

SOURCE

Search...

Entry information

Entry name

REPS1_MOUSE

Accession

Primary (citable) accession number: O54916
Secondary accession number(s): Q3UAM3 , Q5PPQ9, Q8C9J9, Q99LR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	November 3, 2009
Last modified:	May 1, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program