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Q6GYQ0

- RGPA1_HUMAN

UniProt

Q6GYQ0 - RGPA1_HUMAN

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Protein

Ral GTPase-activating protein subunit alpha-1

Gene

RALGAPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB.By similarity

GO - Molecular functioni

  1. protein heterodimerization activity Source: UniProtKB
  2. Ral GTPase activator activity Source: UniProtKB

GO - Biological processi

  1. activation of Ral GTPase activity Source: UniProtKB
  2. regulation of transcription, DNA-templated Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Ral GTPase-activating protein subunit alpha-1
Alternative name(s):
GAP-related-interacting partner to E12
Short name:
GRIPE
GTPase-activating Rap/Ran-GAP domain-like 1
Tuberin-like protein 1
p240
Gene namesi
Name:RALGAPA1
Synonyms:GARNL1, KIAA0884, TULIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:17770. RALGAPA1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1903 – 19031N → K: Has no effect on interaction with RALGAPB but causes loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA165479278.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20362036Ral GTPase-activating protein subunit alpha-1PRO_0000056753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei754 – 7541Phosphothreonine2 Publications
Modified residuei773 – 7731Phosphoserine2 Publications
Modified residuei778 – 7781Phosphothreonine1 Publication
Modified residuei797 – 7971Phosphoserine1 Publication
Modified residuei860 – 8601Phosphoserine1 Publication
Modified residuei861 – 8611Phosphoserine1 Publication
Modified residuei864 – 8641Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6GYQ0.
PaxDbiQ6GYQ0.
PRIDEiQ6GYQ0.

PTM databases

PhosphoSiteiQ6GYQ0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ6GYQ0.
CleanExiHS_GARNL1.
ExpressionAtlasiQ6GYQ0. baseline and differential.
GenevestigatoriQ6GYQ0.

Organism-specific databases

HPAiHPA000851.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi128998. 7 interactions.
IntActiQ6GYQ0. 3 interactions.
STRINGi9606.ENSP00000302647.

Structurei

3D structure databases

ProteinModelPortaliQ6GYQ0.
SMRiQ6GYQ0. Positions 1791-1956.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1796 – 2004209Rap-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1327 – 2035709Minimal domain that binds to TCF3/E12By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1716 – 174429Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi379 – 3824Poly-Ser

Sequence similaritiesi

Contains 1 Rap-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG250663.
GeneTreeiENSGT00390000017866.
HOVERGENiHBG051842.
InParanoidiQ6GYQ0.
OMAiQVFDYLC.
OrthoDBiEOG7N63KR.
PhylomeDBiQ6GYQ0.
TreeFamiTF324484.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR000331. Rap_GAP_dom.
[Graphical view]
PfamiPF02145. Rap_GAP. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50085. RAPGAP. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6GYQ0-1) [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
MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENAES IDLKQFFDQH
60 70 80 90 100
FSHIYYVFFE NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH
110 120 130 140 150
QRWQFHSIGL ILKKLLHTGN SLKIRREGVR LFLLWLQALQ NNCSKEQLWM
160 170 180 190 200
FSCLIPGFSA PQSEHGPRTL DNLINPPLNL QETQVTIEEI TPLVPPQSGD
210 220 230 240 250
KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL FSHFKKYYLP
260 270 280 290 300
YIFPNICKEN SLYHPILDIP QMRPKPHYVV IKKDAETNEA IYCTKEPFIK
310 320 330 340 350
ARVIVIRWLV SFWLEPKPHT GPHIPGMEGE VLPKNIQRAA ASLVSREESK
360 370 380 390 400
NDNADKTDRT TEPEQSHSNT STLTEREPSS SSLCSIDEEH LTDIEIVRRV
410 420 430 440 450
FSSKRSNVNF VTEIFRQAFL LPICEAAAMR KVVKVYQEWI QQEEKPLFMQ
460 470 480 490 500
EPEEIVITSS DLPCIENVTD HDISMEEGEK REEENGTNTA DHVRNSSWAK
510 520 530 540 550
NGSYQGALHN ASEEATEQNI RAGTQAVLQV FIINSSNIFL LEPANEIKNL
560 570 580 590 600
LDEHTDMCKR ILNIYRYMVV QVSMDKKTWE QMLLVLLRVT ESVLKMPSQA
610 620 630 640 650
FLQFQGKKNM TLAGRLAGPL FQTLIVAWIK ANLNVYISRE LWDDLLSVLS
660 670 680 690 700
SLTYWEELAT EWSLTMETLT KVLARNLYSL DLSDLPLDKL SEQKQKKHKG
710 720 730 740 750
KGVGHEFQKV SVDKSFSRGW SRDQPGQAPM RQRSATTTGS PGTEKARSIV
760 770 780 790 800
RQKTVDIDDA QILPRSTRVR HFSQSEETGN EVFGALNEEQ PLPRSSSTSD
810 820 830 840 850
ILEPFTVERA KVNKEDMSQK LPPLNSDIGG SSANVPDLMD EFIAERLRSG
860 870 880 890 900
NASTMTRRGS SPGSLEIPKD LPDILNKQNQ MRPIDDPGVP SEWTSPASAG
910 920 930 940 950
SSDLISSDSH SDSFSAFQYD GRKFDNFGFG TDTGVTSSAD VDSGSGHHQS
960 970 980 990 1000
AEEQEVASLT TLHIDSETSS LNQQAFSAEV ATITGSESAS PVHSPLGSRS
1010 1020 1030 1040 1050
QTPSPSTLNI DHMEQKDLQL DEKLHHSVLQ TPDDLEISEF PSECCSVMAG
1060 1070 1080 1090 1100
GTLTGWHADV ATVMWRRMLG ILGDVNSIMD PEIHAQVFDY LCELWQNLAK
1110 1120 1130 1140 1150
IRDNLGISTD NLTSPSPPVL IPPLRILTPW LFKATMLTDK YKQGKLHAYK
1160 1170 1180 1190 1200
LICNTMKRRQ DVSPNRDFLT HFYNIMHCGL LHIDQDIVNT IIKHCSPQFF
1210 1220 1230 1240 1250
SLGLPGATML IMDFIVAAGR VASSAFLNAP RVEAQVLLGS LVCFPNLYCE
1260 1270 1280 1290 1300
LPSLHPNIPD VAVSQFTDVK ELIIKTVLSS ARDEPSGPAR CVALCSLGIW
1310 1320 1330 1340 1350
ICEELVHESH HPQIKEALNV ICVSLKFTNK TVAHVACNML HMLVHYVPRL
1360 1370 1380 1390 1400
QIYQPDSPLK IIQILIATIT HLLPSTEASS YEMDKRLVVS LLLCLLDWIM
1410 1420 1430 1440 1450
ALPLKTLLQP FHATGAESDK TEKSVLNCIY KVLHGCVYGA QCFSNPRYFP
1460 1470 1480 1490 1500
MSLSDLASVD YDPFMHLESL KEPEPLHSPD SERSSKLQPV TEVKTQMQHG
1510 1520 1530 1540 1550
LISIAARTVI THLVNHLGHY PMSGGPAMLT SQVCENHDNH YSESTELSPE
1560 1570 1580 1590 1600
LFESPNIQFF VLNNTTLVSC IQIRSEENMP GGGLSAGLAS ANSNVRIIVR
1610 1620 1630 1640 1650
DLSGKYSWDS AILYGPPPVS GLSEPTSFML SLSHQEKPEE PPTSNECLED
1660 1670 1680 1690 1700
ITVKDGLSLQ FKRFRETVPT WDTIRDEEDV LDELLQYLGV TSPECLQRTG
1710 1720 1730 1740 1750
ISLNIPAPQP VCISEKQEND VINAILKQHT EEKEFVEKHF NDLNMKAVEQ
1760 1770 1780 1790 1800
DEPIPQKPQS AFYYCRLLLS ILGMNSWDKR RSFHLLKKNE KLLRELRNLD
1810 1820 1830 1840 1850
SRQCRETHKI AVFYVAEGQE DKHSILTNTG GSQAYEDFVA GLGWEVNLTN
1860 1870 1880 1890 1900
HCGFMGGLQK NKSTGLTTPY FATSTVEVIF HVSTRMPSDS DDSLTKKLRH
1910 1920 1930 1940 1950
LGNDEVHIVW SEHTRDYRRG IIPTEFGDVL IVIYPMKNHM FSIQIMKKPE
1960 1970 1980 1990 2000
VPFFGPLFDG AIVNGKVLPI MVRATAINAS RALKSLIPLY QNFYEERARY
2010 2020 2030
LQTIVQHHLE PTTFEDFAAQ VFSPAPYHHL PSDADH
Length:2,036
Mass (Da):229,832
Last modified:July 19, 2004 - v1
Checksum:i7ADF5487908C14CB
GO
Isoform 2 (identifier: Q6GYQ0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2035-2036: DH → GSYPEILPSETPTATQVDGADLASPMSPRTSKSRMSMKLRRSSGSANKS

Show »
Length:2,083
Mass (Da):234,731
Checksum:i0396D985F73CACD8
GO
Isoform 3 (identifier: Q6GYQ0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     755-755: V → VAMRSRSIGECALPSAYIRSAKSAPVLIHTSKPFLPDIVLTPLSDELS
     1036-1057: EISEFPSECCSVMAGGTLTGWH → GNISKLDIYLFSFRASVSGDHK
     1058-2036: Missing.

Note: No experimental confirmation available.

Show »
Length:1,104
Mass (Da):124,733
Checksum:iC473679777FB18DE
GO
Isoform 4 (identifier: Q6GYQ0-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1898-2036: LRHLGNDEVH...YHHLPSDADH → MESHCVAQAG...RDGVSPCWPG

Note: No experimental confirmation available.

Show »
Length:1,961
Mass (Da):221,099
Checksum:i914BB0FC44C23584
GO
Isoform 5 (identifier: Q6GYQ0-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2035-2036: DH → VERNAVIVLFLPKPPLENIGHLKAPTQRFYPVKLPQQRR

Note: No experimental confirmation available.

Show »
Length:2,073
Mass (Da):234,126
Checksum:i693F3F3BC1FB7162
GO
Isoform 6 (identifier: Q6GYQ0-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     755-755: V → VAMRSRSIGECALPSAYIRSAKSAPVLIHTSKPFLPDIVLTPLSDELS

Show »
Length:2,083
Mass (Da):234,854
Checksum:i43E1FEB75F774B33
GO
Isoform 7 (identifier: Q6GYQ0-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     812-825: VNKEDMSQKLPPLN → EAEQNATRGSTEGSVQSCNGLFWKESC

Note: No experimental confirmation available.

Show »
Length:2,049
Mass (Da):231,138
Checksum:i3556F0AB7752E829
GO

Sequence cautioni

The sequence BAC86772.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti779 – 7791G → A in BAA74907. (PubMed:10048485)Curated
Sequence conflicti1270 – 12701K → N in CAD39026. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti931 – 9311T → A.1 Publication
Corresponds to variant rs2274068 [ dbSNP | Ensembl ].
VAR_019804

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei755 – 7551V → VAMRSRSIGECALPSAYIRS AKSAPVLIHTSKPFLPDIVL TPLSDELS in isoform 3 and isoform 6. 2 PublicationsVSP_011324
Alternative sequencei812 – 82514VNKED…LPPLN → EAEQNATRGSTEGSVQSCNG LFWKESC in isoform 7. 1 PublicationVSP_054485Add
BLAST
Alternative sequencei1036 – 105722EISEF…LTGWH → GNISKLDIYLFSFRASVSGD HK in isoform 3. 1 PublicationVSP_011325Add
BLAST
Alternative sequencei1058 – 2036979Missing in isoform 3. 1 PublicationVSP_011326Add
BLAST
Alternative sequencei1898 – 2036139LRHLG…SDADH → MESHCVAQAGVQWHDLRSLQ LLPPRFKESSLLSLLSSWDY RCMPPHLSNFCIFSRDGVSP CWPG in isoform 4. 1 PublicationVSP_011327Add
BLAST
Alternative sequencei2035 – 20362DH → GSYPEILPSETPTATQVDGA DLASPMSPRTSKSRMSMKLR RSSGSANKS in isoform 2. 2 PublicationsVSP_011328
Alternative sequencei2035 – 20362DH → VERNAVIVLFLPKPPLENIG HLKAPTQRFYPVKLPQQRR in isoform 5. 1 PublicationVSP_011329

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY596970 mRNA. Translation: AAT49271.1.
AY596971 mRNA. Translation: AAT49272.1.
AB511280 mRNA. Translation: BAH83561.1.
AB020691 mRNA. Translation: BAA74907.1.
AL137818 Genomic DNA. No translation available.
AL160231 Genomic DNA. No translation available.
AL162311 Genomic DNA. No translation available.
BC042013 mRNA. Translation: AAH42013.1.
BC042045 mRNA. Translation: AAH42045.1.
BC150596 mRNA. Translation: AAI50597.1.
AL834362 mRNA. Translation: CAD39026.1.
AK126975 mRNA. Translation: BAC86772.1. Different initiation.
CCDSiCCDS32064.1. [Q6GYQ0-2]
CCDS32065.1. [Q6GYQ0-1]
CCDS61439.1. [Q6GYQ0-7]
RefSeqiNP_001269972.1. NM_001283043.1. [Q6GYQ0-7]
NP_001269973.1. NM_001283044.1. [Q6GYQ0-6]
NP_055805.1. NM_014990.1. [Q6GYQ0-1]
NP_919277.2. NM_194301.2. [Q6GYQ0-2]
XP_006720166.1. XM_006720103.1. [Q6GYQ0-6]
UniGeneiHs.113150.

Genome annotation databases

EnsembliENST00000307138; ENSP00000302647; ENSG00000174373. [Q6GYQ0-2]
ENST00000382366; ENSP00000371803; ENSG00000174373. [Q6GYQ0-7]
ENST00000389698; ENSP00000374348; ENSG00000174373. [Q6GYQ0-1]
ENST00000553892; ENSP00000451877; ENSG00000174373. [Q6GYQ0-6]
GeneIDi253959.
KEGGihsa:253959.
UCSCiuc001wti.3. human. [Q6GYQ0-1]
uc001wtj.3. human. [Q6GYQ0-2]
uc001wtk.1. human. [Q6GYQ0-3]
uc010tpv.2. human.
uc010tpw.1. human. [Q6GYQ0-6]

Polymorphism databases

DMDMi51315850.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY596970 mRNA. Translation: AAT49271.1 .
AY596971 mRNA. Translation: AAT49272.1 .
AB511280 mRNA. Translation: BAH83561.1 .
AB020691 mRNA. Translation: BAA74907.1 .
AL137818 Genomic DNA. No translation available.
AL160231 Genomic DNA. No translation available.
AL162311 Genomic DNA. No translation available.
BC042013 mRNA. Translation: AAH42013.1 .
BC042045 mRNA. Translation: AAH42045.1 .
BC150596 mRNA. Translation: AAI50597.1 .
AL834362 mRNA. Translation: CAD39026.1 .
AK126975 mRNA. Translation: BAC86772.1 . Different initiation.
CCDSi CCDS32064.1. [Q6GYQ0-2 ]
CCDS32065.1. [Q6GYQ0-1 ]
CCDS61439.1. [Q6GYQ0-7 ]
RefSeqi NP_001269972.1. NM_001283043.1. [Q6GYQ0-7 ]
NP_001269973.1. NM_001283044.1. [Q6GYQ0-6 ]
NP_055805.1. NM_014990.1. [Q6GYQ0-1 ]
NP_919277.2. NM_194301.2. [Q6GYQ0-2 ]
XP_006720166.1. XM_006720103.1. [Q6GYQ0-6 ]
UniGenei Hs.113150.

3D structure databases

ProteinModelPortali Q6GYQ0.
SMRi Q6GYQ0. Positions 1791-1956.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 128998. 7 interactions.
IntActi Q6GYQ0. 3 interactions.
STRINGi 9606.ENSP00000302647.

PTM databases

PhosphoSitei Q6GYQ0.

Polymorphism databases

DMDMi 51315850.

Proteomic databases

MaxQBi Q6GYQ0.
PaxDbi Q6GYQ0.
PRIDEi Q6GYQ0.

Protocols and materials databases

DNASUi 253959.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307138 ; ENSP00000302647 ; ENSG00000174373 . [Q6GYQ0-2 ]
ENST00000382366 ; ENSP00000371803 ; ENSG00000174373 . [Q6GYQ0-7 ]
ENST00000389698 ; ENSP00000374348 ; ENSG00000174373 . [Q6GYQ0-1 ]
ENST00000553892 ; ENSP00000451877 ; ENSG00000174373 . [Q6GYQ0-6 ]
GeneIDi 253959.
KEGGi hsa:253959.
UCSCi uc001wti.3. human. [Q6GYQ0-1 ]
uc001wtj.3. human. [Q6GYQ0-2 ]
uc001wtk.1. human. [Q6GYQ0-3 ]
uc010tpv.2. human.
uc010tpw.1. human. [Q6GYQ0-6 ]

Organism-specific databases

CTDi 253959.
GeneCardsi GC14M036008.
H-InvDB HIX0131236.
HGNCi HGNC:17770. RALGAPA1.
HPAi HPA000851.
MIMi 608884. gene.
neXtProti NX_Q6GYQ0.
PharmGKBi PA165479278.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250663.
GeneTreei ENSGT00390000017866.
HOVERGENi HBG051842.
InParanoidi Q6GYQ0.
OMAi QVFDYLC.
OrthoDBi EOG7N63KR.
PhylomeDBi Q6GYQ0.
TreeFami TF324484.

Miscellaneous databases

ChiTaRSi RALGAPA1. human.
GeneWikii GARNL1.
GenomeRNAii 253959.
NextBioi 35482065.
PROi Q6GYQ0.
SOURCEi Search...

Gene expression databases

Bgeei Q6GYQ0.
CleanExi HS_GARNL1.
ExpressionAtlasi Q6GYQ0. baseline and differential.
Genevestigatori Q6GYQ0.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR000331. Rap_GAP_dom.
[Graphical view ]
Pfami PF02145. Rap_GAP. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50085. RAPGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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), TISSUE SPECIFICITY.
  2. "Tuberous sclerosis tumor suppressor complex-like complexes act as GTPase-activating proteins for Ral GTPases."
    Shirakawa R., Fukai S., Kawato M., Higashi T., Kondo H., Ikeda T., Nakayama E., Okawa K., Nureki O., Kimura T., Kita T., Horiuchi H.
    J. Biol. Chem. 284:21580-21588(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), VARIANT ALA-931, MUTAGENESIS OF ASN-1903.
  3. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-2036 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1719-2036 (ISOFORM 5).
    Tissue: Brain and Skin.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1167-2036 (ISOFORM 4).
    Tissue: Lymph node.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1361-2036 (ISOFORM 2).
    Tissue: Brain.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. "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 THR-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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 THR-754 AND SER-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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 THR-754; SER-860; SER-861 AND SER-864, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRGPA1_HUMAN
AccessioniPrimary (citable) accession number: Q6GYQ0
Secondary accession number(s): A6NMA4
, B9EK38, C5NU19, O94960, Q6GYP9, Q6ZT23, Q86YF3, Q86YF5, Q8ND69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 102 of the entry and version 1 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3