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Q6GYP7 (RGPA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Ral GTPase-activating protein subunit alpha-1
Alternative name(s):
GAP-related-interacting partner to E12
Short name=GRIPE
GTPase-activating RapGAP domain-like 1
Tuberin-like protein 1
p240
Gene names
Name:Ralgapa1
Synonyms:Garnl1, Kiaa0884, Tulip1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2035 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB By similarity. May interact with the HLH region of TCF3/isoform E12

Subunit structure

Component of the heterodimeric RalGAP1 complex with RALGAPB. Heterodimerization is required for activity By similarity. Interacts with the HLH region of TCF3/isoform E12 Ref.1

Subcellular location

Cytoplasm. Nucleus. Note: Translocated to the nucleus, when associated with TCF3/E12. Ref.1

Tissue specificity

Expressed during embryogenesis. Expressed in the adult brain, particularly in neurons of the cortex and hippocampus. Ref.1

Developmental stage

Expression decreased during development, but persists in the adult brain.

Sequence similarities

Contains 1 Rap-GAP domain.

Caution

Was initially thought (Ref.1) to act as a transcriptional regulator via its interaction with TCF3/E12.

Sequence caution

The sequence BAA92774.1 differs from that shown. Reason: Erroneous termination at position 1745. Translated as Lys.

The sequence BAC98046.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6GYP7-1)

Also known as: 3;

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: Q6GYP7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2034-2035: DH → VGSYPEIPPSDAAPAAQVDGADLASPMSPRTSKSR
Isoform 4 (identifier: Q6GYP7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1298: Missing.
     1299-1304: WICEEL → MMRFVE
Note: No experimental confirmation available.
Isoform 5 (identifier: Q6GYP7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1035-1037: EIS → GNA
     1038-2035: Missing.
Isoform 6 (identifier: Q6GYP7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1337: Missing.
     1897-1904: LRHLGNDE → VSAEGKHF
     1905-2035: Missing.
Note: No experimental confirmation available.
Isoform 1S (identifier: Q6GYP7-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-555: Missing.
Note: May be a partial isoform 1. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20352035Ral GTPase-activating protein subunit alpha-1
PRO_0000056754

Regions

Domain1795 – 2003209Rap-GAP
Region1326 – 2035710Minimal domain that binds to TCF3/E12
Coiled coil1713 – 174836 Potential
Compositional bias379 – 3824Poly-Ser

Amino acid modifications

Modified residue7531Phosphothreonine By similarity
Modified residue7721Phosphoserine By similarity
Modified residue7771Phosphothreonine By similarity
Modified residue7961Phosphoserine By similarity
Modified residue8591Phosphoserine Ref.6
Modified residue8601Phosphoserine Ref.6
Modified residue8631Phosphoserine By similarity

Natural variations

Alternative sequence1 – 13371337Missing in isoform 6.
VSP_011331
Alternative sequence1 – 12981298Missing in isoform 4.
VSP_011332
Alternative sequence1 – 555555Missing in isoform 1S.
VSP_011330
Alternative sequence1035 – 10373EIS → GNA in isoform 5.
VSP_011333
Alternative sequence1038 – 2035998Missing in isoform 5.
VSP_011334
Alternative sequence1299 – 13046WICEEL → MMRFVE in isoform 4.
VSP_011335
Alternative sequence1897 – 19048LRHLGNDE → VSAEGKHF in isoform 6.
VSP_011336
Alternative sequence1905 – 2035131Missing in isoform 6.
VSP_011337
Alternative sequence2034 – 20352DH → VGSYPEIPPSDAAPAAQVDG ADLASPMSPRTSKSR in isoform 2.
VSP_011338

Experimental info

Sequence conflict4201L → V in BAC98046. Ref.3
Sequence conflict6511L → S in AAL47577. Ref.1
Sequence conflict7241P → L in AAL47577. Ref.1
Sequence conflict7751E → V in AAL47577. Ref.1
Sequence conflict8691D → G in AAL47577. Ref.1
Sequence conflict11661D → N in AAL47577. Ref.1
Sequence conflict13651I → V in BAA92774. Ref.4
Sequence conflict13981I → T in BAA92774. Ref.4
Sequence conflict14941T → P in BAA92774. Ref.4
Sequence conflict15861G → S in BAA92774. Ref.4
Sequence conflict16341Q → P in BAA92774. Ref.4
Sequence conflict16381E → K in BAA92774. Ref.4
Sequence conflict16741R → Q in BAA92774. Ref.4
Sequence conflict1775 – 17806SWDKRR → WAAGIPGTNGG in AAL47577. Ref.1
Sequence conflict1966 – 19683VLP → SSA in AAL47577. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (3) [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 1F4C3E24022EBB54

FASTA2,035229,389
        10         20         30         40         50         60 
MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENAES IDLKQFFDQH FSHIYYVFFE 

        70         80         90        100        110        120 
NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH QRWQFHSIGL ILKKLLHTGN 

       130        140        150        160        170        180 
SLKIRREGVR LFLLWLQALQ DNCSKEQLWM FSCLIPGFSA PQSEYGPRTL DNLINPPLSL 

       190        200        210        220        230        240 
QETQVTIEEV TPLVPPQSGD KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL 

       250        260        270        280        290        300 
FSHFKKFYLP YIFPNICKEN SLYHPVLDIP QIRPKPHYVM IKKDAETNET IYCTKEPFIQ 

       310        320        330        340        350        360 
ARVIVIRWLV SFWLEPKPHS GPNIPGMEGE VLPKNIQRAA ASLVSREESK NDTVDKVDKS 

       370        380        390        400        410        420 
AEPEQSHSNT STLTEREPSS SSLCSIDEEH LTDIEIVRRV FSSKRSNVNF VTEIFRQAFL 

       430        440        450        460        470        480 
LPICEAAAMR KVVKVYQEWI QQEEKPLFMQ EPEDTAITCS DIPCSETVAD HDSAIEDGEK 

       490        500        510        520        530        540 
REEENGTSTS EHVRNSSWTK NGSYQEAFHV CEEATEQNIQ AGTQAVLQVF IINSSNIFLL 

       550        560        570        580        590        600 
EPANEIKNLL DEHTDMCKRI LNIYRYMVVQ VSMDKKTWEQ MLLVLLRVTE SVLKMSSQAF 

       610        620        630        640        650        660 
LQFQGKKSMT LAGRLAGPLF QTLIVAWIKA NLNVYISREL WDDLLSVLSS LTYWEELATE 

       670        680        690        700        710        720 
WSLTMETLTK VLARNLYSLD LSDLPLDKLS EQKQKKHKGK GVGHEFQKVS VDKSFSRGWS 

       730        740        750        760        770        780 
RDQPGQAPMR QRSATTTGSP GTEKARSIVR QKTVDIDDAQ ILPRSTRVRH FSQSEDTGNE 

       790        800        810        820        830        840 
VFGALHEEQP LPRSSSTSDI LEPFTVERAK VNKEDTSPKL PPLNSETGGN SANVPDLMDE 

       850        860        870        880        890        900 
FIAERLRSGN ASTMTRRGSS PGSLEIPKDL PDILNKQNQM RPVDDPGVPS EWTSPASAGS 

       910        920        930        940        950        960 
SDLMSSDSHS DSFSAFQCEG RKFDNFGFGT DIGIPSSADV DLGSGHHQST EEQEVASLTT 

       970        980        990       1000       1010       1020 
LHLDSETSSL NQQAFSAEVA TVTGSESASP VHSALGSRSQ TPSPSTLSRA HIEQKDLQLD 

      1030       1040       1050       1060       1070       1080 
EKLHHSVLQT PDDLEISEFP SECCSVMAGG TLTGWHADVA TVMWRRMLGI LGDVNAIMDP 

      1090       1100       1110       1120       1130       1140 
EIHAQVFDYL CELWQNLAKI RDNLGISADN LTSPSPPVLI PPLRILTPWL FKATMLTDKY 

      1150       1160       1170       1180       1190       1200 
KQGKLHAYKL ICNTMKRRQD VSPNRDFLTH FYNIMHCGLL HIDQDIVNTI IKHCSPQFFS 

      1210       1220       1230       1240       1250       1260 
LGLPGATMLI MDFIIAAGRV ASSAFLNAPR VEAQVLLGSL VCFPNLYCEL PALHPNIPDI 

      1270       1280       1290       1300       1310       1320 
AVSQFTDVKE LIIKTVLSSA RDEPSGPARC VALCSLGIWI CEELVHESHH PQIKEALNVI 

      1330       1340       1350       1360       1370       1380 
CVSLKFTNKT VAHVACNMLH MLVHYVPRLQ IHQPQSPLKI IQILIATITH LLPSTEASSY 

      1390       1400       1410       1420       1430       1440 
EMDKRLVVSL LLCLLDWIMA LPLKTLLQPV HATGAENDKT EKSVLNCIYK VLHGCVYGAQ 

      1450       1460       1470       1480       1490       1500 
SFSNPKYFPI SLSDLASVDY DPFMHLESLK EPEPLHSPDS ERSSKLQPVT EVKTQMQQGL 

      1510       1520       1530       1540       1550       1560 
ISIAARTVIT HLVNHLGHYP MSGGPAMLTS QVCENHDNHY SESTELSPEL FESPNIQFFV 

      1570       1580       1590       1600       1610       1620 
LNNTTLVSCI QIRSEESMPG GGLAAGLVSA NSNVRIIVRD LSGKYSWDSA ILYGPPIVSG 

      1630       1640       1650       1660       1670       1680 
LPEPTSFILS MSDQEKPEEP PTSNECLEDI AVKDGLSLQL RRFRETVPTW STIREEEDVL 

      1690       1700       1710       1720       1730       1740 
DELLQYLGTT SPECLQRTGI SLNVPAPQPL CISEKQENDV INAILKQYTE EKEFVEKHFN 

      1750       1760       1770       1780       1790       1800 
DLNMKASEQD EPTPQKPQSA FYYCRLLLSI LGMNSWDKRR SFHLLKKNEK LLRELRNLDS 

      1810       1820       1830       1840       1850       1860 
RQCRETHKIA VFYVAEGQED KYSILTNIGG SQAYEDFVAG LGWEVNLTNH CGFMGGLQKN 

      1870       1880       1890       1900       1910       1920 
RSTGLTTPYF ATSTVEVIFH VSTRMPSDSD DSLTKKLRHL GNDEVHIVWS EHTRDYRRGI 

      1930       1940       1950       1960       1970       1980 
IPTEFGDVLI VIYPMKNHMF SIQIMKKPEV PFFGPLFDGA IVNGKVLPIM VRSTAINASR 

      1990       2000       2010       2020       2030 
ALKSLIPLYQ NFYEERARYL QTIVQHHLEP TTFEDFAAQV FSPAPYHHFP ADADH 

« Hide

Isoform 2 [UniParc].

Checksum: CD55170FA5FBCF6B
Show »

FASTA2,068232,646
Isoform 4 [UniParc].

Checksum: 3D72CD7AA1E1F7D4
Show »

FASTA73783,311
Isoform 5 [UniParc].

Checksum: 23D34AB339388DC0
Show »

FASTA1,037117,170
Isoform 6 [UniParc].

Checksum: 0B413D16DC68FE68
Show »

FASTA56763,656
Isoform 1S [UniParc].

Checksum: 3628A0BE37D0D0BB
Show »

FASTA1,480165,341

References

« Hide 'large scale' references
[1]"Cloning and characterization of GRIPE, a novel interacting partner of the transcription factor E12 in developing mouse forebrain."
Heng J.I.T., Tan S.-S.
J. Biol. Chem. 277:43152-43159(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1S), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TCF3/E12.
Strain: C57BL/6J.
Tissue: Forebrain.
[2]"Cloning, genomic structure and expression profile of TULIP1 (GARNL1), a brain-expressed candidate gene for 14q13-linked neurological phenotypes and its murine homolog."
Schwarzbraun T., Vincent J.B., Schumacher A., Geschwind D.H., Oliveira J., Windpassinger C., Ofner L., Ledinegg M.K., Kroisel P.M., Wagner K., Petek E.
Genomics 84:577-586(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: BALB/c.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Embryonic tail.
[4]"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. expand/collapse author list , 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] (ISOFORMS 4; 5 AND 6).
Strain: C57BL/6J.
Tissue: Thymus.
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 339-350, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"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-859 AND SER-860, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY066011 mRNA. Translation: AAL47577.1.
AY596972 mRNA. Translation: AAT49273.1.
AY596973 mRNA. Translation: AAT49274.1.
AY596974 mRNA. Translation: AAT49275.1.
AK129236 mRNA. Translation: BAC98046.1. Different initiation.
AB032400 mRNA. Translation: BAA92774.1. Sequence problems.
AK042116 mRNA. Translation: BAC31171.1.
AK083518 mRNA. Translation: BAC38939.1.
CCDSCCDS36452.1. [Q6GYP7-1]
RefSeqNP_001003719.1. NM_001003719.2.
NP_001106185.1. NM_001112714.2. [Q6GYP7-1]
NP_001273192.1. NM_001286263.1.
NP_064378.4. NM_019994.5. [Q6GYP7-1]
UniGeneMm.292180.
Mm.398098.

3D structure databases

ProteinModelPortalQ6GYP7.
SMRQ6GYP7. Positions 1790-1955.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208171. 1 interaction.
IntActQ6GYP7. 1 interaction.
MINTMINT-4096796.

PTM databases

PhosphoSiteQ6GYP7.

Proteomic databases

MaxQBQ6GYP7.
PaxDbQ6GYP7.
PRIDEQ6GYP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085385; ENSMUSP00000082503; ENSMUSG00000021027. [Q6GYP7-1]
ENSMUST00000110687; ENSMUSP00000106315; ENSMUSG00000021027. [Q6GYP7-1]
GeneID56784.
KEGGmmu:56784.
UCSCuc007nou.1. mouse. [Q6GYP7-1]
uc007nov.1. mouse. [Q6GYP7-2]
uc007now.1. mouse. [Q6GYP7-5]
uc007nox.1. mouse. [Q6GYP7-4]

Organism-specific databases

CTD253959.
MGIMGI:1931050. Ralgapa1.
RougeSearch...

Phylogenomic databases

eggNOGNOG250663.
GeneTreeENSGT00390000017866.
HOVERGENHBG051842.
OMAQVFDYLC.
OrthoDBEOG7N63KR.
PhylomeDBQ6GYP7.
TreeFamTF324484.

Gene expression databases

ArrayExpressQ6GYP7.
BgeeQ6GYP7.
CleanExMM_GARNL1.
GenevestigatorQ6GYP7.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR000331. Rap_GAP_dom.
[Graphical view]
PfamPF02145. Rap_GAP. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50085. RAPGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313310.
PROQ6GYP7.
SOURCESearch...

Entry information

Entry nameRGPA1_MOUSE
AccessionPrimary (citable) accession number: Q6GYP7
Secondary accession number(s): Q6GYP6 expand/collapse secondary AC list , Q6ZQ28, Q8BNJ5, Q8C9G8, Q8CIW4, Q9JMC4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot