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Q68EM7

- RHG17_HUMAN

UniProt

Q68EM7 - RHG17_HUMAN

Protein

Rho GTPase-activating protein 17

Gene

ARHGAP17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca2+-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1.2 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. regulation of small GTPase mediated signal transduction Source: Reactome
    2. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho GTPase-activating protein 17
    Alternative name(s):
    Rho-type GTPase-activating protein 17
    RhoGAP interacting with CIP4 homologs protein 1
    Short name:
    RICH-1
    Gene namesi
    Name:ARHGAP17
    Synonyms:RICH1
    ORF Names:MSTP066, MSTP110
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:18239. ARHGAP17.

    Subcellular locationi

    Membrane; Peripheral membrane protein. Cytoplasm. Cell junctiontight junction
    Note: Associates with membranes and concentrates at sites of cell-cell contact.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane Source: UniProtKB-SubCell
    3. tight junction Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Membrane, Tight junction

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi288 – 2881R → A: Loss of function; leading to defects in tight junction maintenance. 1 Publication

    Organism-specific databases

    PharmGKBiPA134908575.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 881881Rho GTPase-activating protein 17PRO_0000280462Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei575 – 5751Phosphoserine2 Publications
    Modified residuei679 – 6791Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ68EM7.
    PaxDbiQ68EM7.
    PRIDEiQ68EM7.

    PTM databases

    PhosphoSiteiQ68EM7.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Expressed at higher level in heart and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ68EM7.
    BgeeiQ68EM7.
    GenevestigatoriQ68EM7.

    Organism-specific databases

    HPAiHPA041703.

    Interactioni

    Subunit structurei

    Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AMOTQ4VCS52EBI-1642807,EBI-2511319
    AMOTQ4VCS5-24EBI-1642807,EBI-3891843

    Protein-protein interaction databases

    BioGridi120424. 30 interactions.
    IntActiQ68EM7. 7 interactions.
    MINTiMINT-195688.

    Structurei

    3D structure databases

    ProteinModelPortaliQ68EM7.
    SMRiQ68EM7. Positions 25-232, 246-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 246233BARPROSITE-ProRule annotationAdd
    BLAST
    Domaini252 – 442191Rho-GAPPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi753 – 76614SH3-bindingSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi521 – 816296Pro-richAdd
    BLAST

    Domaini

    The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions.1 Publication

    Sequence similaritiesi

    Contains 1 BAR domain.PROSITE-ProRule annotation
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiNOG329716.
    HOVERGENiHBG000015.
    InParanoidiQ68EM7.
    OMAiSICHHSH.
    OrthoDBiEOG7MKW5G.
    PhylomeDBiQ68EM7.
    TreeFamiTF350627.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    1.20.1270.60. 1 hit.
    InterProiIPR027267. AH/BAR-dom.
    IPR004148. BAR_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view]
    PfamiPF03114. BAR. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view]
    SMARTiSM00721. BAR. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    PROSITEiPS51021. BAR. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q68EM7-1) [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

    MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL    50
    VACFQGQHGT DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA 100
    ENQLALELSQ HEVFVEKEIV DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS 150
    VRARWNQAHK SSGTNFQGLP SKIDTLKEEM DEAGNKVEQC KDQLAADMYN 200
    FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH QDKWAEKPAF 250
    GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK 300
    AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV 350
    QDQDKKLQDL WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA 400
    IVLGPNLLWA RNEGTLAEMA AATSVHVVAV IEPIIQHADW FFPEEVEFNV 450
    SEAFVPLTTP SSNHSFHTGN DSDSGTLERK RPASMAVMEG DLVKKESFGV 500
    KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP EPPPQSSRAE 550
    SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG 600
    QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH 650
    PGGQSSSGTS QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR 700
    YSSSLSPIQA PNHPPPQPPT QATPLMHTKP NSQGPPNPMA LPSEHGLEQP 750
    SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA GGNPETAQPH AGTLPRPRPV 800
    PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS NSRVSEPHRS 850
    IFPEMHSDSA SKDVPGRILL DIDNDTESTA L 881
    Length:881
    Mass (Da):95,437
    Last modified:October 11, 2004 - v1
    Checksum:i92029DBFFEAD1001
    GO
    Isoform 2 (identifier: Q68EM7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         497-574: Missing.

    Show »
    Length:803
    Mass (Da):87,609
    Checksum:i9F42C390ACBAFADA
    GO
    Isoform 3 (identifier: Q68EM7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-273: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:608
    Mass (Da):64,267
    Checksum:i8060364C667A5535
    GO
    Isoform 4 (identifier: Q68EM7-4) [UniParc]FASTAAdd to Basket

    Also known as: RICH1B

    The sequence of this isoform differs from the canonical sequence as follows:
         215-226: LLEAQADYHRKA → ISGRKNQPLGLP
         227-881: Missing.

    Show »
    Length:226
    Mass (Da):25,760
    Checksum:iC849839D16E68AE1
    GO
    Isoform 5 (identifier: Q68EM7-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         839-881: DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → GFQNRIAASFLKCTQTQPAKTCLAASCWI

    Note: No experimental confirmation available.

    Show »
    Length:867
    Mass (Da):93,855
    Checksum:iB2797018F447B1FF
    GO
    Isoform 6 (identifier: Q68EM7-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         840-881: SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL → V

    Show »
    Length:840
    Mass (Da):90,929
    Checksum:i333F5437A7222C79
    GO
    Isoform 7 (identifier: Q68EM7-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-467: Missing.
         468-496: TGNDSDSGTLERKRPASMAVMEGDLVKKE → MCGFNTCGPMGFCLSSLLAWCVDCFFSLC

    Note: No experimental confirmation available.

    Show »
    Length:414
    Mass (Da):42,512
    Checksum:iB20A13496205E5A8
    GO

    Sequence cautioni

    The sequence AAH01241.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAQ13586.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAQ13632.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391K → E in BAB55203. (PubMed:14702039)Curated
    Sequence conflicti167 – 1671Q → R in CAC37948. (PubMed:11431473)Curated
    Sequence conflicti186 – 1861K → R in CAC37948. (PubMed:11431473)Curated
    Sequence conflicti255 – 2551E → A in BAB14506. (PubMed:14702039)Curated
    Sequence conflicti404 – 4041G → A in BAB55203. (PubMed:14702039)Curated
    Sequence conflicti575 – 5751S → C in BAC86144. (PubMed:14702039)Curated
    Sequence conflicti855 – 8551M → V in BAB55203. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 467467Missing in isoform 7. 1 PublicationVSP_023682Add
    BLAST
    Alternative sequencei1 – 273273Missing in isoform 3. 1 PublicationVSP_023683Add
    BLAST
    Alternative sequencei215 – 22612LLEAQ…YHRKA → ISGRKNQPLGLP in isoform 4. 1 PublicationVSP_023684Add
    BLAST
    Alternative sequencei227 – 881655Missing in isoform 4. 1 PublicationVSP_023685Add
    BLAST
    Alternative sequencei468 – 49629TGNDS…LVKKE → MCGFNTCGPMGFCLSSLLAW CVDCFFSLC in isoform 7. 1 PublicationVSP_023686Add
    BLAST
    Alternative sequencei497 – 57478Missing in isoform 2. 2 PublicationsVSP_023687Add
    BLAST
    Alternative sequencei839 – 88143DSNSR…ESTAL → GFQNRIAASFLKCTQTQPAK TCLAASCWI in isoform 5. 1 PublicationVSP_023688Add
    BLAST
    Alternative sequencei840 – 88142SNSRV…ESTAL → V in isoform 6. 1 PublicationVSP_023689Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ306731 mRNA. Translation: CAC37948.1.
    AJ306732 mRNA. Translation: CAC37949.1.
    AK001170 mRNA. No translation available.
    AK023281 mRNA. Translation: BAB14506.1.
    AK027567 mRNA. Translation: BAB55203.1.
    AK125358 mRNA. Translation: BAC86144.1.
    AK291691 mRNA. Translation: BAF84380.1.
    AL833975 mRNA. Translation: CAD38819.1.
    BC001241 mRNA. Translation: AAH01241.1. Different initiation.
    BC080195 mRNA. Translation: AAH80195.1.
    AF163257 mRNA. Translation: AAQ13586.1. Different initiation.
    AF173885 mRNA. Translation: AAQ13632.1. Different initiation.
    CCDSiCCDS32408.1. [Q68EM7-2]
    CCDS32409.1. [Q68EM7-1]
    PIRiF59433.
    RefSeqiNP_001006635.1. NM_001006634.2. [Q68EM7-1]
    NP_060524.4. NM_018054.5. [Q68EM7-2]
    XP_005255471.1. XM_005255414.1. [Q68EM7-6]
    UniGeneiHs.373793.

    Genome annotation databases

    EnsembliENST00000289968; ENSP00000289968; ENSG00000140750. [Q68EM7-1]
    ENST00000303665; ENSP00000303130; ENSG00000140750. [Q68EM7-2]
    GeneIDi55114.
    KEGGihsa:55114.
    UCSCiuc002dmy.3. human. [Q68EM7-7]
    uc002dna.3. human. [Q68EM7-1]
    uc002dnc.3. human. [Q68EM7-2]
    uc002dng.1. human. [Q68EM7-4]

    Polymorphism databases

    DMDMi74736331.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ306731 mRNA. Translation: CAC37948.1 .
    AJ306732 mRNA. Translation: CAC37949.1 .
    AK001170 mRNA. No translation available.
    AK023281 mRNA. Translation: BAB14506.1 .
    AK027567 mRNA. Translation: BAB55203.1 .
    AK125358 mRNA. Translation: BAC86144.1 .
    AK291691 mRNA. Translation: BAF84380.1 .
    AL833975 mRNA. Translation: CAD38819.1 .
    BC001241 mRNA. Translation: AAH01241.1 . Different initiation.
    BC080195 mRNA. Translation: AAH80195.1 .
    AF163257 mRNA. Translation: AAQ13586.1 . Different initiation.
    AF173885 mRNA. Translation: AAQ13632.1 . Different initiation.
    CCDSi CCDS32408.1. [Q68EM7-2 ]
    CCDS32409.1. [Q68EM7-1 ]
    PIRi F59433.
    RefSeqi NP_001006635.1. NM_001006634.2. [Q68EM7-1 ]
    NP_060524.4. NM_018054.5. [Q68EM7-2 ]
    XP_005255471.1. XM_005255414.1. [Q68EM7-6 ]
    UniGenei Hs.373793.

    3D structure databases

    ProteinModelPortali Q68EM7.
    SMRi Q68EM7. Positions 25-232, 246-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120424. 30 interactions.
    IntActi Q68EM7. 7 interactions.
    MINTi MINT-195688.

    PTM databases

    PhosphoSitei Q68EM7.

    Polymorphism databases

    DMDMi 74736331.

    Proteomic databases

    MaxQBi Q68EM7.
    PaxDbi Q68EM7.
    PRIDEi Q68EM7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000289968 ; ENSP00000289968 ; ENSG00000140750 . [Q68EM7-1 ]
    ENST00000303665 ; ENSP00000303130 ; ENSG00000140750 . [Q68EM7-2 ]
    GeneIDi 55114.
    KEGGi hsa:55114.
    UCSCi uc002dmy.3. human. [Q68EM7-7 ]
    uc002dna.3. human. [Q68EM7-1 ]
    uc002dnc.3. human. [Q68EM7-2 ]
    uc002dng.1. human. [Q68EM7-4 ]

    Organism-specific databases

    CTDi 55114.
    GeneCardsi GC16M024931.
    HGNCi HGNC:18239. ARHGAP17.
    HPAi HPA041703.
    MIMi 608293. gene.
    neXtProti NX_Q68EM7.
    PharmGKBi PA134908575.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG329716.
    HOVERGENi HBG000015.
    InParanoidi Q68EM7.
    OMAi SICHHSH.
    OrthoDBi EOG7MKW5G.
    PhylomeDBi Q68EM7.
    TreeFami TF350627.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.

    Miscellaneous databases

    ChiTaRSi ARHGAP17. human.
    GenomeRNAii 55114.
    NextBioi 58744.
    PROi Q68EM7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q68EM7.
    Bgeei Q68EM7.
    Genevestigatori Q68EM7.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    1.20.1270.60. 1 hit.
    InterProi IPR027267. AH/BAR-dom.
    IPR004148. BAR_dom.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    [Graphical view ]
    Pfami PF03114. BAR. 1 hit.
    PF00620. RhoGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00721. BAR. 1 hit.
    SM00324. RhoGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    PROSITEi PS51021. BAR. 1 hit.
    PS50238. RHOGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1."
      Richnau N., Aspenstroem P.
      J. Biol. Chem. 276:35060-35070(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, MUTAGENESIS OF ARG-288.
    2. "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] (ISOFORMS 1; 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5).
      Tissue: Placenta and Teratocarcinoma.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Brain.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6).
      Tissue: Cervix and Eye.
    5. Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881.
      Tissue: Aorta.
    6. "Identification of EPI64, a TBC/rabGAP domain-containing microvillar protein that binds to the first PDZ domain of EBP50 and E3KARP."
      Reczek D., Bretscher A.
      J. Cell Biol. 153:191-206(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC9A3R1.
    7. "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells."
      Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M., Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K., Starostine A., Metalnikov P., Pawson T.
      Cell 125:535-548(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, INTERACTION WITH AMOT; MPP5; INADL; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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 THR-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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 SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRHG17_HUMAN
    AccessioniPrimary (citable) accession number: Q68EM7
    Secondary accession number(s): A8K6M6
    , Q6ZUS4, Q7Z2F2, Q8NDG2, Q96KS2, Q96KS3, Q96SS8, Q9BVF6, Q9H8U5, Q9NW54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 99 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3