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Q15438

- CYH1_HUMAN

UniProt

Q15438 - CYH1_HUMAN

Protein

Cytohesin-1

Gene

CYTH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei281 – 2811Phosphatidylinositol 3,4,5-trisphosphateBy similarity
    Binding sitei292 – 2921Phosphatidylinositol 3,4,5-trisphosphateBy similarity
    Binding sitei302 – 3021Phosphatidylinositol 3,4,5-trisphosphateBy similarity
    Binding sitei351 – 3511Phosphatidylinositol 3,4,5-trisphosphateBy similarity

    GO - Molecular functioni

    1. ARF guanyl-nucleotide exchange factor activity Source: UniProtKB
    2. lipid binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. establishment of epithelial cell polarity Source: Ensembl
    2. positive regulation of GTPase activity Source: GOC
    3. regulation of ARF protein signal transduction Source: InterPro
    4. regulation of cell adhesion Source: MGI
    5. vesicle-mediated transport Source: ProtInc

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytohesin-1
    Alternative name(s):
    PH, SEC7 and coiled-coil domain-containing protein 1
    SEC7 homolog B2-1
    Gene namesi
    Name:CYTH1
    Synonyms:D17S811E, PSCD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9501. CYTH1.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytosol By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: UniProtKB
    3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    4. plasma membrane Source: UniProtKB
    5. tight junction Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571E → A or K: Reduces guanine exchange factor activity by over 90%. 1 Publication
    Mutagenesisi187 – 1871Y → A: Reduces guanine exchange factor activity by over 90%. 1 Publication
    Mutagenesisi195 – 1951M → A: Reduces guanine exchange factor activity by over 90%. 1 Publication

    Organism-specific databases

    PharmGKBiPA164718528.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398Cytohesin-1PRO_0000120194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15438.
    PaxDbiQ15438.
    PRIDEiQ15438.

    PTM databases

    PhosphoSiteiQ15438.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ15438.
    BgeeiQ15438.
    CleanExiHS_CYTH1.
    GenevestigatoriQ15438.

    Organism-specific databases

    HPAiHPA047498.

    Interactioni

    Subunit structurei

    Interacts with TRIM23 and CYTIP.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CYTIPO607592EBI-997830,EBI-997814

    Protein-protein interaction databases

    BioGridi114688. 12 interactions.
    IntActiQ15438. 3 interactions.
    MINTiMINT-3031502.
    STRINGi9606.ENSP00000354398.

    Structurei

    Secondary structure

    1
    398
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi64 – 7512
    Helixi77 – 8610
    Helixi94 – 10310
    Helixi109 – 1168
    Helixi121 – 13313
    Turni137 – 1393
    Helixi141 – 15010
    Helixi158 – 17518
    Helixi183 – 20119
    Beta strandi203 – 2053
    Helixi211 – 2177
    Turni218 – 2214
    Helixi229 – 24113
    Beta strandi246 – 2483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BC9NMR-A58-256[»]
    4A4PX-ray2.00A/B63-248[»]
    ProteinModelPortaliQ15438.
    SMRiQ15438. Positions 58-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15438.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 202130SEC7PROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 377118PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2779Phosphatidylinositol 3,4,5-trisphosphate bindingBy similarity
    Regioni388 – 3969C-terminal autoinhibitory regionBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili10 – 6758Sequence AnalysisAdd
    BLAST

    Domaini

    Binds via its PH domain to the inositol head group of phosphatidylinositol 3,4,5-trisphosphate.By similarity
    Autoinhibited by its C-terminal basic region.By similarity

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 SEC7 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5307.
    HOGENOMiHOG000253023.
    HOVERGENiHBG002647.
    OMAiVGLHEFT.
    OrthoDBiEOG7RBZ9C.
    PhylomeDBiQ15438.
    TreeFamiTF352091.

    Family and domain databases

    Gene3Di1.10.1000.11. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR023394. Sec7_alpha_orthog.
    IPR000904. Sec7_dom.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF01369. Sec7. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00222. Sec7. 1 hit.
    [Graphical view]
    SUPFAMiSSF48425. SSF48425. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS50190. SEC7. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15438-1) [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

    MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN    50
    LGSTEERKNM QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF 100
    LYKGEGLNKT AIGDYLGERD EFNIQVLHAF VELHEFTDLN LVQALRQFLW 150
    SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF QSTDTCYVLS FAIIMLNTSL 200
    HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK NEPFKIPEDD 250
    GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE 300
    PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG 350
    NHTVYRISAP TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH 398
    Length:398
    Mass (Da):46,413
    Last modified:November 1, 1996 - v1
    Checksum:i067FEE0FEA7A4C86
    GO
    Isoform 2 (identifier: Q15438-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:397
    Mass (Da):46,356
    Checksum:iCBD984BC348E6B15
    GO
    Isoform 3 (identifier: Q15438-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:339
    Mass (Da):39,470
    Checksum:iC08318AD7469BD02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti353 – 3619TVYRISAPT → MFTGSQLRR in AAF37737. (PubMed:15489334)Curated
    Sequence conflicti353 – 3619TVYRISAPT → MFTGSQLRR in AAF37738. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5959Missing in isoform 3. 1 PublicationVSP_055884Add
    BLAST
    Alternative sequencei273 – 2731Missing in isoform 2. CuratedVSP_006034

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85169 mRNA. Translation: AAA36602.1.
    AK293894 mRNA. Translation: BAH11620.1.
    AK316277 mRNA. Translation: BAH14648.1.
    AC022966 Genomic DNA. No translation available.
    AC099804 Genomic DNA. No translation available.
    BC038385 mRNA. Translation: AAH38385.1.
    BC050452 mRNA. Translation: AAH50452.1.
    AF125362
    , AF125350, AF125351, AF125352, AF125353, AF125354, AF125355, AF125356, AF125357, AF125359, AF125360, AF125361 Genomic DNA. Translation: AAF37737.1.
    AF125362
    , AF125350, AF125351, AF125352, AF125353, AF125354, AF125355, AF125356, AF125357, AF125358, AF125359, AF125360, AF125361 Genomic DNA. Translation: AAF37738.1.
    CCDSiCCDS32754.1. [Q15438-2]
    CCDS42392.2. [Q15438-1]
    PIRiS24168.
    RefSeqiNP_004753.1. NM_004762.3. [Q15438-1]
    NP_059430.2. NM_017456.3. [Q15438-2]
    UniGeneiHs.191215.

    Genome annotation databases

    EnsembliENST00000361101; ENSP00000354398; ENSG00000108669. [Q15438-1]
    ENST00000446868; ENSP00000389095; ENSG00000108669. [Q15438-1]
    ENST00000585509; ENSP00000465940; ENSG00000108669. [Q15438-3]
    ENST00000589297; ENSP00000466512; ENSG00000108669. [Q15438-3]
    ENST00000591455; ENSP00000465665; ENSG00000108669. [Q15438-2]
    GeneIDi9267.
    KEGGihsa:9267.
    UCSCiuc002jvw.3. human. [Q15438-2]
    uc010wtw.1. human. [Q15438-1]

    Polymorphism databases

    DMDMi2498175.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85169 mRNA. Translation: AAA36602.1 .
    AK293894 mRNA. Translation: BAH11620.1 .
    AK316277 mRNA. Translation: BAH14648.1 .
    AC022966 Genomic DNA. No translation available.
    AC099804 Genomic DNA. No translation available.
    BC038385 mRNA. Translation: AAH38385.1 .
    BC050452 mRNA. Translation: AAH50452.1 .
    AF125362
    , AF125350 , AF125351 , AF125352 , AF125353 , AF125354 , AF125355 , AF125356 , AF125357 , AF125359 , AF125360 , AF125361 Genomic DNA. Translation: AAF37737.1 .
    AF125362
    , AF125350 , AF125351 , AF125352 , AF125353 , AF125354 , AF125355 , AF125356 , AF125357 , AF125358 , AF125359 , AF125360 , AF125361 Genomic DNA. Translation: AAF37738.1 .
    CCDSi CCDS32754.1. [Q15438-2 ]
    CCDS42392.2. [Q15438-1 ]
    PIRi S24168.
    RefSeqi NP_004753.1. NM_004762.3. [Q15438-1 ]
    NP_059430.2. NM_017456.3. [Q15438-2 ]
    UniGenei Hs.191215.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BC9 NMR - A 58-256 [» ]
    4A4P X-ray 2.00 A/B 63-248 [» ]
    ProteinModelPortali Q15438.
    SMRi Q15438. Positions 58-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114688. 12 interactions.
    IntActi Q15438. 3 interactions.
    MINTi MINT-3031502.
    STRINGi 9606.ENSP00000354398.

    PTM databases

    PhosphoSitei Q15438.

    Polymorphism databases

    DMDMi 2498175.

    Proteomic databases

    MaxQBi Q15438.
    PaxDbi Q15438.
    PRIDEi Q15438.

    Protocols and materials databases

    DNASUi 9267.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361101 ; ENSP00000354398 ; ENSG00000108669 . [Q15438-1 ]
    ENST00000446868 ; ENSP00000389095 ; ENSG00000108669 . [Q15438-1 ]
    ENST00000585509 ; ENSP00000465940 ; ENSG00000108669 . [Q15438-3 ]
    ENST00000589297 ; ENSP00000466512 ; ENSG00000108669 . [Q15438-3 ]
    ENST00000591455 ; ENSP00000465665 ; ENSG00000108669 . [Q15438-2 ]
    GeneIDi 9267.
    KEGGi hsa:9267.
    UCSCi uc002jvw.3. human. [Q15438-2 ]
    uc010wtw.1. human. [Q15438-1 ]

    Organism-specific databases

    CTDi 9267.
    GeneCardsi GC17M076670.
    HGNCi HGNC:9501. CYTH1.
    HPAi HPA047498.
    MIMi 182115. gene.
    neXtProti NX_Q15438.
    PharmGKBi PA164718528.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5307.
    HOGENOMi HOG000253023.
    HOVERGENi HBG002647.
    OMAi VGLHEFT.
    OrthoDBi EOG7RBZ9C.
    PhylomeDBi Q15438.
    TreeFami TF352091.

    Miscellaneous databases

    ChiTaRSi CYTH1. human.
    EvolutionaryTracei Q15438.
    GeneWikii CYTH1.
    GenomeRNAii 9267.
    NextBioi 34739.
    PROi Q15438.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15438.
    Bgeei Q15438.
    CleanExi HS_CYTH1.
    Genevestigatori Q15438.

    Family and domain databases

    Gene3Di 1.10.1000.11. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR023394. Sec7_alpha_orthog.
    IPR000904. Sec7_dom.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF01369. Sec7. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00222. Sec7. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48425. SSF48425. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS50190. SEC7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with homology to yeast SEC7."
      Liu L., Pohajdak B.
      Biochim. Biophys. Acta 1132:75-78(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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] (ISOFORM 3).
      Tissue: Cerebellum.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Skin and Testis.
    5. "Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors."
      Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K., Kirby M., Moss J., Vaughan M.
      J. Biol. Chem. 275:3221-3230(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-398, FUNCTION, ALTERNATIVE SPLICING.
    6. "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)."
      Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J., Vaughan M.
      J. Biol. Chem. 275:21331-21339(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM23.
    7. Cited for: INTERACTION WITH CYTIP.
    8. "The Arl4 family of small G proteins can recruit the cytohesin Arf6 exchange factors to the plasma membrane."
      Hofmann I., Thompson A., Sanderson C.M., Munro S.
      Curr. Biol. 17:711-716(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1."
      Betz S.F., Schnuchel A., Wang H., Olejniczak E.T., Meadows R.P., Lipsky B.P., Harris E.A., Staunton D.E., Fesik S.W.
      Proc. Natl. Acad. Sci. U.S.A. 95:7909-7914(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 58-256, FUNCTION, MUTAGENESIS OF GLU-157; TYR-187 AND MET-195.

    Entry informationi

    Entry nameiCYH1_HUMAN
    AccessioniPrimary (citable) accession number: Q15438
    Secondary accession number(s): A6NFW7
    , B7Z1T4, Q9P123, Q9P124
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 138 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3