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Q52LW3

- RHG29_HUMAN

UniProt

Q52LW3 - RHG29_HUMAN

Protein

Rho GTPase-activating protein 29

Gene

ARHGAP29

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (05 Feb 2008)
      Previous versions | rss
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    Functioni

    GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. May act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri612 – 65746Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. PDZ domain binding Source: MGI
    3. Rho GTPase activator activity Source: ProtInc

    GO - Biological processi

    1. positive regulation of Rho GTPase activity Source: GOC
    2. regulation of small GTPase mediated signal transduction Source: Reactome
    3. Rho protein signal transduction Source: ProtInc
    4. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GTPase-activating protein 29
    Alternative name(s):
    PTPL1-associated RhoGAP protein 1
    Rho-type GTPase-activating protein 29
    Gene namesi
    Name:ARHGAP29
    Synonyms:PARG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30207. ARHGAP29.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394548.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12611261Rho GTPase-activating protein 29PRO_0000317582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei171 – 1711PhosphoserineBy similarity
    Modified residuei176 – 1761Phosphoserine1 Publication
    Modified residuei179 – 1791Phosphoserine1 Publication
    Modified residuei190 – 1901Phosphoserine1 Publication
    Modified residuei949 – 9491Phosphoserine1 Publication
    Modified residuei1019 – 10191Phosphoserine1 Publication
    Modified residuei1146 – 11461Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ52LW3.
    PaxDbiQ52LW3.
    PRIDEiQ52LW3.

    PTM databases

    PhosphoSiteiQ52LW3.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in skeletal muscle and heart. Expressed at intermediate level in placenta, liver and pancreas. Weakly expressed in brain, lung and kidney.1 Publication

    Inductioni

    Strongly down-regulated in mantle-cell lymphomas. Up-regulated in migrating glioma cells.2 Publications

    Gene expression databases

    ArrayExpressiQ52LW3.
    BgeeiQ52LW3.
    CleanExiHS_ARHGAP29.
    GenevestigatoriQ52LW3.

    Organism-specific databases

    HPAiHPA026534.

    Interactioni

    Subunit structurei

    Interacts with PTPN13/PTPL1. Interacts with RAP2A via its coiled coil domain. Interacts with RASIP1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114806. 8 interactions.
    IntActiQ52LW3. 7 interactions.
    MINTiMINT-1465191.
    STRINGi9606.ENSP00000260526.

    Structurei

    3D structure databases

    ProteinModelPortaliQ52LW3.
    SMRiQ52LW3. Positions 193-469, 612-886.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini671 – 886216Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1258 – 12614Interaction with PTPN13/PTPL1

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili296 – 418123Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri612 – 65746Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG310169.
    HOGENOMiHOG000043077.
    HOVERGENiHBG108406.
    InParanoidiQ52LW3.
    OMAiEYSNQAR.
    PhylomeDBiQ52LW3.
    TreeFamiTF351450.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    InterProiIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF00130. C1_1. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00109. C1. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 2 hits.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q52LW3-1) [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

    MIAHKQKKTK KKRAWASGQL STDITTSEMG LKSLSSNSIF DPDYIKELVN     50
    DIRKFSHMLL YLKEAIFSDC FKEVIHIRLE ELLRVLKSIM NKHQNLNSVD 100
    LQNAAEMLTA KVKAVNFTEV NEENKNDLFQ EVFSSIETLA FTFGNILTNF 150
    LMGDVGNDSL LRLPVSRETK SFENVSVESV DSSSEKGNFS PLELDNVLLK 200
    NTDSIELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNM VKLAEATRTN 250
    IGIQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM 300
    EKQRKEIKEL WKQEQNKMLE AENALKKAKL LCMQRQDEYE KAKSSMFRAE 350
    EEHLSSSGGL AKNLNKQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR 400
    NDLENTKREI LAQLRTLVFQ CDLTLKAVTV NLFHMQHLQA ASLADSLQSL 450
    CDSAKLYDPG QEYSEFVKAT NSTEEEKVDG NVNKHLNSSQ PSGFGPANSL 500
    EDVVRLPDSS NKIEEDRCSN SADITGPSFI RSWTFGMFSD SESTGGSSES 550
    RSLDSESISP GDFHRKLPRT PSSGTMSSAD DLDEREPPSP SETGPNSLGT 600
    FKKTLMSKAA LTHKFRKLRS PTKCRDCEGI VVFQGVECEE CLLVCHRKCL 650
    ENLVIICGHQ KLPGKIHLFG AEFTQVAKKE PDGIPFILKI CASEIENRAL 700
    CLQGIYRVCG NKIKTEKLCQ ALENGMHLVD ISEFSSHDIC DVLKLYLRQL 750
    PEPFILFRLY KEFIDLAKEI QHVNEEQETK KNSLEDKKWP NMCIEINRIL 800
    LKSKDLLRQL PASNFNSLHF LIVHLKRVVD HAEENKMNSK NLGVIFGPSL 850
    IRPRPTTAPI TISSLAEYSN QARLVEFLIT YSQKIFDGSL QPQDVMCSIG 900
    VVDQGCFPKP LLSPEERDIE RSMKSLFFSS KEDIHTSESE SKIFERATSF 950
    EESERKQNAL GKCDACLSDK AQLLLDQEAE SASQKIEDGK TPKPLSLKSD 1000
    RSTNNVERHT PRTKIRPVSL PVDRLLLASP PNERNGRNMG NVNLDKFCKN 1050
    PAFEGVNRKD AATTVCSKFN GFDQQTLQKI QDKQYEQNSL TAKTTMIMPS 1100
    ALQEKGVTTS LQISGDHSIN ATQPSKPYAE PVRSVREASE RRSSDSYPLA 1150
    PVRAPRTLQP QHWTTFYKPH APIISIRGNE EKPASPSAAV PPGTDHDPHG 1200
    LVVKSMPDPD KASACPGQAT GQPKEDSEEL GLPDVNPMCQ RPRLKRMQQF 1250
    EDLEGEIPQF V 1261
    Length:1,261
    Mass (Da):142,064
    Last modified:February 5, 2008 - v2
    Checksum:i3E46445EA5DA76C8
    GO
    Isoform 2 (identifier: Q52LW3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         383-393: EEANELYKVCV → TIFFFFICKLN
         394-1261: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:393
    Mass (Da):45,194
    Checksum:i6FF8EDA79AB7061C
    GO

    Sequence cautioni

    The sequence AAH67839.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 581M → I in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti160 – 1601L → F in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti166 – 1661S → Y in AAH67839. (PubMed:15489334)Curated
    Sequence conflicti212 – 2121A → V in BAD92110. 1 PublicationCurated
    Sequence conflicti386 – 3861N → D in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti403 – 4031L → V in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti446 – 4461S → R in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti452 – 4521D → G in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti675 – 6751Q → L in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti720 – 7201Q → L in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti856 – 8561T → Q in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti991 – 9911T → A in AAB81012. (PubMed:9305890)Curated
    Sequence conflicti1190 – 11901V → C in AAB81012. (PubMed:9305890)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti552 – 5521S → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_038552
    Natural varianti1192 – 11921P → L.
    Corresponds to variant rs11165091 [ dbSNP | Ensembl ].
    VAR_049145
    Natural varianti1255 – 12551G → D.2 Publications
    Corresponds to variant rs1999272 [ dbSNP | Ensembl ].
    VAR_038553

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei383 – 39311EEANELYKVCV → TIFFFFICKLN in isoform 2. 1 PublicationVSP_031058Add
    BLAST
    Alternative sequencei394 – 1261868Missing in isoform 2. 1 PublicationVSP_031059Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90920 mRNA. Translation: AAB81012.1.
    AL162735 Genomic DNA. Translation: CAH71750.1.
    AL162735 Genomic DNA. Translation: CAH71751.1.
    CH471097 Genomic DNA. Translation: EAW73052.1.
    CH471097 Genomic DNA. Translation: EAW73051.1.
    BC022483 mRNA. Translation: AAH22483.1.
    BC067839 mRNA. Translation: AAH67839.1. Sequence problems.
    BC093741 mRNA. Translation: AAH93741.1.
    BC093767 mRNA. Translation: AAH93767.1.
    AB208873 mRNA. Translation: BAD92110.1.
    CCDSiCCDS748.1. [Q52LW3-1]
    PIRiE59430.
    RefSeqiNP_004806.3. NM_004815.3. [Q52LW3-1]
    UniGeneiHs.483238.

    Genome annotation databases

    EnsembliENST00000260526; ENSP00000260526; ENSG00000137962. [Q52LW3-1]
    ENST00000370217; ENSP00000359237; ENSG00000137962. [Q52LW3-2]
    GeneIDi9411.
    KEGGihsa:9411.
    UCSCiuc001dqj.4. human. [Q52LW3-1]
    uc001dql.3. human. [Q52LW3-2]

    Polymorphism databases

    DMDMi166977701.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90920 mRNA. Translation: AAB81012.1 .
    AL162735 Genomic DNA. Translation: CAH71750.1 .
    AL162735 Genomic DNA. Translation: CAH71751.1 .
    CH471097 Genomic DNA. Translation: EAW73052.1 .
    CH471097 Genomic DNA. Translation: EAW73051.1 .
    BC022483 mRNA. Translation: AAH22483.1 .
    BC067839 mRNA. Translation: AAH67839.1 . Sequence problems.
    BC093741 mRNA. Translation: AAH93741.1 .
    BC093767 mRNA. Translation: AAH93767.1 .
    AB208873 mRNA. Translation: BAD92110.1 .
    CCDSi CCDS748.1. [Q52LW3-1 ]
    PIRi E59430.
    RefSeqi NP_004806.3. NM_004815.3. [Q52LW3-1 ]
    UniGenei Hs.483238.

    3D structure databases

    ProteinModelPortali Q52LW3.
    SMRi Q52LW3. Positions 193-469, 612-886.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114806. 8 interactions.
    IntActi Q52LW3. 7 interactions.
    MINTi MINT-1465191.
    STRINGi 9606.ENSP00000260526.

    PTM databases

    PhosphoSitei Q52LW3.

    Polymorphism databases

    DMDMi 166977701.

    Proteomic databases

    MaxQBi Q52LW3.
    PaxDbi Q52LW3.
    PRIDEi Q52LW3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260526 ; ENSP00000260526 ; ENSG00000137962 . [Q52LW3-1 ]
    ENST00000370217 ; ENSP00000359237 ; ENSG00000137962 . [Q52LW3-2 ]
    GeneIDi 9411.
    KEGGi hsa:9411.
    UCSCi uc001dqj.4. human. [Q52LW3-1 ]
    uc001dql.3. human. [Q52LW3-2 ]

    Organism-specific databases

    CTDi 9411.
    GeneCardsi GC01M094634.
    H-InvDB HIX0021585.
    HGNCi HGNC:30207. ARHGAP29.
    HPAi HPA026534.
    MIMi 610496. gene.
    neXtProti NX_Q52LW3.
    PharmGKBi PA128394548.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310169.
    HOGENOMi HOG000043077.
    HOVERGENi HBG108406.
    InParanoidi Q52LW3.
    OMAi EYSNQAR.
    PhylomeDBi Q52LW3.
    TreeFami TF351450.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    GenomeRNAii 9411.
    NextBioi 35256.
    PROi Q52LW3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q52LW3.
    Bgeei Q52LW3.
    CleanExi HS_ARHGAP29.
    Genevestigatori Q52LW3.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    InterProi IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF00130. C1_1. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00109. C1. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 2 hits.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1."
      Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J., Heldin C.-H.
      J. Biol. Chem. 272:24333-24338(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 64-72; 221-228; 349-357; 456-468; 666-678; 943-946; 971-985; 1015-1024; 1069-1079 AND 1212-1224, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PTPN13, VARIANT ASP-1255.
      Tissue: Skeletal muscle.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Colon.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-1261 (ISOFORM 1), VARIANT ASP-1255.
      Tissue: Brain.
    6. "Glioma cell motility is associated with reduced transcription of proapoptotic and proliferation genes: a cDNA microarray analysis."
      Mariani L., Beaudry C., McDonough W.S., Hoelzinger D.B., Demuth T., Ross K.R., Berens T., Coons S.W., Watts G., Trent J.M., Wei J.S., Giese A., Berens M.E.
      J. Neurooncol. 53:161-176(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector."
      Myagmar B.-E., Umikawa M., Asato T., Taira K., Oshiro M., Hino A., Takei K., Uezato H., Kariya K.
      Biochem. Biophys. Res. Commun. 329:1046-1052(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAP2A.
    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-1019, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: INDUCTION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-179; SER-949 AND SER-1146, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-552.

    Entry informationi

    Entry nameiRHG29_HUMAN
    AccessioniPrimary (citable) accession number: Q52LW3
    Secondary accession number(s): O15463
    , Q59H86, Q5VYZ0, Q6NVX2, Q8TBI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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