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Q6GYQ0

- RGPA1_HUMAN

UniProt

Q6GYQ0 - RGPA1_HUMAN

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
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ6GYQ0.
    BgeeiQ6GYQ0.
    CleanExiHS_GARNL1.
    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. 5 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.
    HOVERGENiHBG051842.
    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

    MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENAES IDLKQFFDQH     50
    FSHIYYVFFE NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH 100
    QRWQFHSIGL ILKKLLHTGN SLKIRREGVR LFLLWLQALQ NNCSKEQLWM 150
    FSCLIPGFSA PQSEHGPRTL DNLINPPLNL QETQVTIEEI TPLVPPQSGD 200
    KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL FSHFKKYYLP 250
    YIFPNICKEN SLYHPILDIP QMRPKPHYVV IKKDAETNEA IYCTKEPFIK 300
    ARVIVIRWLV SFWLEPKPHT GPHIPGMEGE VLPKNIQRAA ASLVSREESK 350
    NDNADKTDRT TEPEQSHSNT STLTEREPSS SSLCSIDEEH LTDIEIVRRV 400
    FSSKRSNVNF VTEIFRQAFL LPICEAAAMR KVVKVYQEWI QQEEKPLFMQ 450
    EPEEIVITSS DLPCIENVTD HDISMEEGEK REEENGTNTA DHVRNSSWAK 500
    NGSYQGALHN ASEEATEQNI RAGTQAVLQV FIINSSNIFL LEPANEIKNL 550
    LDEHTDMCKR ILNIYRYMVV QVSMDKKTWE QMLLVLLRVT ESVLKMPSQA 600
    FLQFQGKKNM TLAGRLAGPL FQTLIVAWIK ANLNVYISRE LWDDLLSVLS 650
    SLTYWEELAT EWSLTMETLT KVLARNLYSL DLSDLPLDKL SEQKQKKHKG 700
    KGVGHEFQKV SVDKSFSRGW SRDQPGQAPM RQRSATTTGS PGTEKARSIV 750
    RQKTVDIDDA QILPRSTRVR HFSQSEETGN EVFGALNEEQ PLPRSSSTSD 800
    ILEPFTVERA KVNKEDMSQK LPPLNSDIGG SSANVPDLMD EFIAERLRSG 850
    NASTMTRRGS SPGSLEIPKD LPDILNKQNQ MRPIDDPGVP SEWTSPASAG 900
    SSDLISSDSH SDSFSAFQYD GRKFDNFGFG TDTGVTSSAD VDSGSGHHQS 950
    AEEQEVASLT TLHIDSETSS LNQQAFSAEV ATITGSESAS PVHSPLGSRS 1000
    QTPSPSTLNI DHMEQKDLQL DEKLHHSVLQ TPDDLEISEF PSECCSVMAG 1050
    GTLTGWHADV ATVMWRRMLG ILGDVNSIMD PEIHAQVFDY LCELWQNLAK 1100
    IRDNLGISTD NLTSPSPPVL IPPLRILTPW LFKATMLTDK YKQGKLHAYK 1150
    LICNTMKRRQ DVSPNRDFLT HFYNIMHCGL LHIDQDIVNT IIKHCSPQFF 1200
    SLGLPGATML IMDFIVAAGR VASSAFLNAP RVEAQVLLGS LVCFPNLYCE 1250
    LPSLHPNIPD VAVSQFTDVK ELIIKTVLSS ARDEPSGPAR CVALCSLGIW 1300
    ICEELVHESH HPQIKEALNV ICVSLKFTNK TVAHVACNML HMLVHYVPRL 1350
    QIYQPDSPLK IIQILIATIT HLLPSTEASS YEMDKRLVVS LLLCLLDWIM 1400
    ALPLKTLLQP FHATGAESDK TEKSVLNCIY KVLHGCVYGA QCFSNPRYFP 1450
    MSLSDLASVD YDPFMHLESL KEPEPLHSPD SERSSKLQPV TEVKTQMQHG 1500
    LISIAARTVI THLVNHLGHY PMSGGPAMLT SQVCENHDNH YSESTELSPE 1550
    LFESPNIQFF VLNNTTLVSC IQIRSEENMP GGGLSAGLAS ANSNVRIIVR 1600
    DLSGKYSWDS AILYGPPPVS GLSEPTSFML SLSHQEKPEE PPTSNECLED 1650
    ITVKDGLSLQ FKRFRETVPT WDTIRDEEDV LDELLQYLGV TSPECLQRTG 1700
    ISLNIPAPQP VCISEKQEND VINAILKQHT EEKEFVEKHF NDLNMKAVEQ 1750
    DEPIPQKPQS AFYYCRLLLS ILGMNSWDKR RSFHLLKKNE KLLRELRNLD 1800
    SRQCRETHKI AVFYVAEGQE DKHSILTNTG GSQAYEDFVA GLGWEVNLTN 1850
    HCGFMGGLQK NKSTGLTTPY FATSTVEVIF HVSTRMPSDS DDSLTKKLRH 1900
    LGNDEVHIVW SEHTRDYRRG IIPTEFGDVL IVIYPMKNHM FSIQIMKKPE 1950
    VPFFGPLFDG AIVNGKVLPI MVRATAINAS RALKSLIPLY QNFYEERARY 2000
    LQTIVQHHLE PTTFEDFAAQ VFSPAPYHHL PSDADH 2036
    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]
    CCDS61440.1. [Q6GYQ0-6]
    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]
    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 ]
    CCDS61440.1. [Q6GYQ0-6 ]
    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. 5 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 ]
    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.
    HOVERGENi HBG051842.
    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

    ArrayExpressi Q6GYQ0.
    Bgeei Q6GYQ0.
    CleanExi HS_GARNL1.
    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

    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 1, 2014
    This is version 101 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