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P08729

- K2C7_HUMAN

UniProt

P08729 - K2C7_HUMAN

Protein

Keratin, type II cytoskeletal 7

Gene

KRT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 5 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei343 – 3431Stutter

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Keratin, type II cytoskeletal 7
    Alternative name(s):
    Cytokeratin-7
    Short name:
    CK-7
    Keratin-7
    Short name:
    K7
    Sarcolectin
    Type-II keratin Kb7
    Gene namesi
    Name:KRT7
    Synonyms:SCL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6445. KRT7.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intermediate filament Source: UniProtKB
    3. keratin filament Source: InterPro
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Intermediate filament, Keratin

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30233.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 469468Keratin, type II cytoskeletal 7PRO_0000063725Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei20 – 201Dimethylated arginine; alternate1 Publication
    Modified residuei20 – 201Omega-N-methylarginine; alternate1 Publication
    Modified residuei179 – 1791N6-acetyllysine1 Publication
    Modified residuei252 – 2521Phosphoserine1 Publication
    Modified residuei254 – 2541Phosphoserine1 Publication

    Post-translational modificationi

    Arg-20 is dimethylated, probably to asymmetric dimethylarginine.

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP08729.
    PaxDbiP08729.
    PRIDEiP08729.

    2D gel databases

    SWISS-2DPAGEP08729.

    PTM databases

    PhosphoSiteiP08729.

    Expressioni

    Tissue specificityi

    Expressed in cultured epidermal, bronchial and mesothelial cells but absent in colon, ectocervix and liver. Observed throughout the glandular cells in the junction between stomach and esophagus but is absent in the esophagus.2 Publications

    Inductioni

    Up-regulated by retinoic acid.1 Publication

    Gene expression databases

    BgeeiP08729.
    CleanExiHS_KRT7.
    GenevestigatoriP08729.

    Organism-specific databases

    HPAiCAB000028.
    HPA007272.

    Interactioni

    Subunit structurei

    Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10 and with HPV16 E7. Interacts with GPER1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF3AQ141523EBI-297833,EBI-366617

    Protein-protein interaction databases

    BioGridi110053. 10 interactions.
    IntActiP08729. 6 interactions.
    MINTiMINT-256895.
    STRINGi9606.ENSP00000329243.

    Structurei

    3D structure databases

    ProteinModelPortaliP08729.
    SMRiP08729. Positions 88-240, 256-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 9089HeadAdd
    BLAST
    Regioni90 – 12637Coil 1AAdd
    BLAST
    Regioni91 – 399309RodAdd
    BLAST
    Regioni92 – 976Interaction with HPV16 E7
    Regioni127 – 14418Linker 1Add
    BLAST
    Regioni145 – 23692Coil 1BAdd
    BLAST
    Regioni237 – 26024Linker 12Add
    BLAST
    Regioni261 – 399139Coil 2Add
    BLAST
    Regioni400 – 46970TailAdd
    BLAST

    Sequence similaritiesi

    Belongs to the intermediate filament family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG145985.
    HOGENOMiHOG000230976.
    HOVERGENiHBG013015.
    InParanoidiP08729.
    KOiK07605.
    OMAiMSIHFSS.
    OrthoDBiEOG7FV3Q8.
    PhylomeDBiP08729.
    TreeFamiTF317854.

    Family and domain databases

    InterProiIPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR003054. Keratin_II.
    IPR009053. Prefoldin.
    [Graphical view]
    PANTHERiPTHR23239. PTHR23239. 1 hit.
    PfamiPF00038. Filament. 1 hit.
    [Graphical view]
    PRINTSiPR01276. TYPE2KERATIN.
    SUPFAMiSSF46579. SSF46579. 1 hit.
    PROSITEiPS00226. IF. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08729-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA    50
    VRSAYGGPVG AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN 100
    KFASFIDKVR FLEQQNKLLE TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG 150
    QLEALQVDGG RLEAELRSMQ DVVEDFKNKY EDEINHRTAA ENEFVVLKKD 200
    VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI SDTSVVLSMD 250
    NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD 300
    LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA 350
    RAKQEELEAA LQRGKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE 400
    SRLAGDGVGA VNISVMNSTG GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG 450
    LLKAYSIRTA SASRRSARD 469
    Length:469
    Mass (Da):51,386
    Last modified:January 11, 2011 - v5
    Checksum:i070CBE8F66A62497
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791D → G in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti83 – 842SL → FS in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti97 – 971T → A in CAA26956. (PubMed:2415537)Curated
    Sequence conflicti97 – 971T → A in CAA31695. (PubMed:2459129)Curated
    Sequence conflicti155 – 1551L → M in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti164 – 1641A → Q in CAA26956. (PubMed:2415537)Curated
    Sequence conflicti164 – 1641A → Q in CAA31695. (PubMed:2459129)Curated
    Sequence conflicti164 – 1641A → Q in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti165 – 1651E → G in CAA26956. (PubMed:2415537)Curated
    Sequence conflicti165 – 1651E → G in CAA31695. (PubMed:2459129)Curated
    Sequence conflicti165 – 1651E → G in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti168 – 1681S → T in CAA26956. (PubMed:2415537)Curated
    Sequence conflicti168 – 1681S → T in CAA31695. (PubMed:2459129)Curated
    Sequence conflicti168 – 1681S → T in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti342 – 3421R → C in CAA26956. (PubMed:2415537)Curated
    Sequence conflicti342 – 3421R → C in CAA31695. (PubMed:2459129)Curated
    Sequence conflicti411 – 4111V → A in CAB41416. (PubMed:10492017)Curated
    Sequence conflicti467 – 4671A → T in CAB41416. (PubMed:10492017)Curated

    Mass spectrometryi

    Molecular mass is 51203.48 Da from positions 2 - 469. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti186 – 1861H → R.6 Publications
    Corresponds to variant rs6580870 [ dbSNP | Ensembl ].
    VAR_060731
    Natural varianti364 – 3641G → A.5 Publications
    Corresponds to variant rs2608009 [ dbSNP | Ensembl ].
    VAR_016321

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03212 mRNA. Translation: CAA26956.2. Sequence problems.
    X13320
    , X13346, X13347, X13348, X13349, X13350, X13351, X13352, X13353 Genomic DNA. Translation: CAA31695.1.
    AJ238246 mRNA. Translation: CAB41416.1.
    AF509887 mRNA. Translation: AAN64031.1.
    AF509892, AF509891 Genomic DNA. Translation: AAN64035.1.
    AC007338 Genomic DNA. No translation available.
    AC007494 Genomic DNA. No translation available.
    BC002700 mRNA. Translation: AAH02700.1.
    CCDSiCCDS8822.1.
    PIRiB24177.
    S05602.
    RefSeqiNP_005547.3. NM_005556.3.
    UniGeneiHs.411501.
    Hs.670221.

    Genome annotation databases

    EnsembliENST00000331817; ENSP00000329243; ENSG00000135480.
    GeneIDi3855.
    KEGGihsa:3855.
    UCSCiuc001saa.1. human.

    Polymorphism databases

    DMDMi317373583.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03212 mRNA. Translation: CAA26956.2 . Sequence problems.
    X13320
    , X13346 , X13347 , X13348 , X13349 , X13350 , X13351 , X13352 , X13353 Genomic DNA. Translation: CAA31695.1 .
    AJ238246 mRNA. Translation: CAB41416.1 .
    AF509887 mRNA. Translation: AAN64031.1 .
    AF509892 , AF509891 Genomic DNA. Translation: AAN64035.1 .
    AC007338 Genomic DNA. No translation available.
    AC007494 Genomic DNA. No translation available.
    BC002700 mRNA. Translation: AAH02700.1 .
    CCDSi CCDS8822.1.
    PIRi B24177.
    S05602.
    RefSeqi NP_005547.3. NM_005556.3.
    UniGenei Hs.411501.
    Hs.670221.

    3D structure databases

    ProteinModelPortali P08729.
    SMRi P08729. Positions 88-240, 256-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110053. 10 interactions.
    IntActi P08729. 6 interactions.
    MINTi MINT-256895.
    STRINGi 9606.ENSP00000329243.

    PTM databases

    PhosphoSitei P08729.

    Polymorphism databases

    DMDMi 317373583.

    2D gel databases

    SWISS-2DPAGE P08729.

    Proteomic databases

    MaxQBi P08729.
    PaxDbi P08729.
    PRIDEi P08729.

    Protocols and materials databases

    DNASUi 3855.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331817 ; ENSP00000329243 ; ENSG00000135480 .
    GeneIDi 3855.
    KEGGi hsa:3855.
    UCSCi uc001saa.1. human.

    Organism-specific databases

    CTDi 3855.
    GeneCardsi GC12P052626.
    H-InvDB HIX0010643.
    HIX0079487.
    HGNCi HGNC:6445. KRT7.
    HPAi CAB000028.
    HPA007272.
    MIMi 148059. gene.
    neXtProti NX_P08729.
    PharmGKBi PA30233.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145985.
    HOGENOMi HOG000230976.
    HOVERGENi HBG013015.
    InParanoidi P08729.
    KOi K07605.
    OMAi MSIHFSS.
    OrthoDBi EOG7FV3Q8.
    PhylomeDBi P08729.
    TreeFami TF317854.

    Miscellaneous databases

    ChiTaRSi KRT7. human.
    GeneWikii Keratin_7.
    GenomeRNAii 3855.
    NextBioi 15169.
    PROi P08729.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08729.
    CleanExi HS_KRT7.
    Genevestigatori P08729.

    Family and domain databases

    InterProi IPR001664. IF.
    IPR018039. Intermediate_filament_CS.
    IPR003054. Keratin_II.
    IPR009053. Prefoldin.
    [Graphical view ]
    PANTHERi PTHR23239. PTHR23239. 1 hit.
    Pfami PF00038. Filament. 1 hit.
    [Graphical view ]
    PRINTSi PR01276. TYPE2KERATIN.
    SUPFAMi SSF46579. SSF46579. 1 hit.
    PROSITEi PS00226. IF. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and expression of a human type II mesothelial keratin."
      Glass C., Kim K.H., Fuchs E.
      J. Cell Biol. 101:2366-2373(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-186 AND ALA-364.
      Tissue: Mesothelium.
    2. "Isolation, sequence, and differential expression of a human K7 gene in simple epithelial cells."
      Glass C., Fuchs E.
      J. Cell Biol. 107:1337-1350(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, VARIANTS ARG-186 AND ALA-364.
    3. "Sarcolectin (SCL): structure and expression of the recombinant molecule."
      Kaba A., Jiang P., Chany-Fournier F., Chany C.
      Biochimie 81:709-715(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ARG-186 AND ALA-364.
      Tissue: Placenta.
    4. "Cloning of human, murine, and marsupial keratin 7 and a survey of K7 expression in the mouse."
      Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B., McLean W.H.I.
      Biochem. Biophys. Res. Commun. 297:818-827(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANTS ARG-186 AND ALA-364.
      Tissue: Keratinocyte.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS ARG-186 AND ALA-364.
      Tissue: Pancreas.
    7. Cited for: PROTEIN SEQUENCE OF 2-48; 53-96; 102-110; 123-130; 137-161; 178-208; 215-273; 277-296; 306-313; 318-326; 330-348; 352-363 AND 374-402, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-20, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Ovarian carcinoma.
    8. "Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7."
      Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.
      J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3S10.
    9. "Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)-globin and human cytokeratin 7."
      Kanduc D.
      J. Virol. 76:7040-7048(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HPV16 E7.
    10. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    11. "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-2 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "G protein-coupled estrogen receptor 1/G protein-coupled receptor 30 localizes in the plasma membrane and traffics intracellularly on cytokeratin intermediate filaments."
      Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.
      Mol. Pharmacol. 79:400-410(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPER1.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiK2C7_HUMAN
    AccessioniPrimary (citable) accession number: P08729
    Secondary accession number(s): Q92676, Q9BUD8, Q9Y3R7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 163 of the entry and version 5 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

    Miscellaneous

    There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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