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Q9Y6J0

- CABIN_HUMAN

UniProt

Q9Y6J0 - CABIN_HUMAN

Protein

Calcineurin-binding protein cabin-1

Gene

CABIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes.2 Publications

    GO - Molecular functioni

    1. protein phosphatase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: UniProtKB
    2. chromatin modification Source: UniProtKB-KW
    3. DNA replication-independent nucleosome assembly Source: UniProt
    4. negative regulation of catalytic activity Source: GOC

    Keywords - Molecular functioni

    Chromatin regulator

    Enzyme and pathway databases

    ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcineurin-binding protein cabin-1
    Alternative name(s):
    Calcineurin inhibitor
    Short name:
    CAIN
    Gene namesi
    Name:CABIN1
    Synonyms:KIAA0330
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:24187. CABIN1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. aggresome Source: HPA
    2. cytoplasm Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2172 – 21721L → A, K or W: Abrogates binding to MEF2B. 1 Publication

    Organism-specific databases

    PharmGKBiPA164717549.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22202220Calcineurin-binding protein cabin-1PRO_0000106275Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661Phosphoserine1 Publication
    Modified residuei1439 – 14391Phosphoserine1 Publication
    Modified residuei2151 – 21511Phosphothreonine1 Publication
    Modified residuei2154 – 21541Phosphothreonine1 Publication

    Post-translational modificationi

    Activated through PKC-mediated hyperphosphorylation. Phosphorylation by the DNA damage kinases ATM and CHK2 enhances ubiquitination.4 Publications
    Upon genotoxic stress, ubiquitination by the DCX(DDB2) E3 ubiquitin-protein ligase complex targets CABIN1 for proteasomal degradation, leading to the release of p53/TP53.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y6J0.
    PaxDbiQ9Y6J0.
    PRIDEiQ9Y6J0.

    PTM databases

    PhosphoSiteiQ9Y6J0.

    Expressioni

    Tissue specificityi

    Widely expressed in different tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y6J0.
    BgeeiQ9Y6J0.
    CleanExiHS_CABIN1.
    GenevestigatoriQ9Y6J0.

    Organism-specific databases

    HPAiHPA043296.

    Interactioni

    Subunit structurei

    Component of a complex that includes at least ASF1A, CABIN1, HIRA, histone H3.3 and UBN1. Interacts with calcineurin. Interacts with MEF2B.3 Publications

    Protein-protein interaction databases

    BioGridi117070. 20 interactions.
    IntActiQ9Y6J0. 1 interaction.
    MINTiMINT-2824170.
    STRINGi9606.ENSP00000263119.

    Structurei

    Secondary structure

    1
    2220
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2166 – 217712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N6JX-ray2.20G2156-2190[»]
    ProteinModelPortaliQ9Y6J0.
    SMRiQ9Y6J0. Positions 168-198, 615-644, 1057-1100.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6J0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati36 – 6934TPR 1Add
    BLAST
    Repeati90 – 12334TPR 2Add
    BLAST
    Repeati125 – 15733TPR 3Add
    BLAST
    Repeati615 – 64834TPR 4Add
    BLAST
    Repeati1055 – 108834TPR 5Add
    BLAST
    Repeati1106 – 113934TPR 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2116 – 215338Required for interaction with calcineurinBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 6 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiNOG84755.
    HOGENOMiHOG000111281.
    HOVERGENiHBG050758.
    InParanoidiQ9Y6J0.
    KOiK17613.
    OMAiAEPTCSQ.
    OrthoDBiEOG7R56RQ.
    PhylomeDBiQ9Y6J0.
    TreeFamiTF323227.

    Family and domain databases

    Gene3Di1.25.40.10. 3 hits.
    InterProiIPR015134. MEF2_binding.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF09047. MEF2_binding. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 4 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 4 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6J0-1) [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

    MIRIAALNAS STIEDDHEGS FKSHKTQTKE AQEAEAFALY HKALDLQKHD     50
    RFEESAKAYH ELLEASLLRE AVSSGDEKEG LKHPGLILKY STYKNLAQLA 100
    AQREDLETAM EFYLEAVMLD STDVNLWYKI GHVALRLIRI PLARHAFEEG 150
    LRCNPDHWPC LDNLITVLYT LSDYTTCLYF ICKALEKDCR YSKGLVLKEK 200
    IFEEQPCLRK DSLRMFLKCD MSIHDVSVSA AETQAIVDEA LGLRKKRQAL 250
    IVREKEPDLK LVQPIPFFTW KCLGESLLAM YNHLTTCEPP RPSLGKRIDL 300
    SDYQDPSQPL ESSMVVTPVN VIQPSTVSTN PAVAVAEPVV SYTSVATTSF 350
    PLHSPGLLET GAPVGDISGG DKSKKGVKRK KISEESGETA KRRSARVRNT 400
    KCKKEEKVDF QELLMKFLPS RLRKLDPEEE DDSFNNYEVQ SEAKLESFPS 450
    IGPQRLSFDS ATFMESEKQD VHEFLLENLT NGGILELMMR YLKAMGHKFL 500
    VRWPPGLAEV VLSVYHSWRR HSTSLPNPLL RDCSNKHIKD MMLMSLSCME 550
    LQLDQWLLTK GRSSAVSPRN CPAGMVNGRF GPDFPGTHCL GDLLQLSFAS 600
    SQRDLFEDGW LEFVVRVYWL KARFLALQGD MEQALENYDI CTEMLQSSTA 650
    IQVEAGAERR DIVIRLPNLH NDSVVSLEEI DKNLKSLERC QSLEEIQRLY 700
    EAGDYKAVVH LLRPTLCTSG FDRAKHLEFM TSIPERPAQL LLLQDSLLRL 750
    KDYRQCFECS DVALNEAVQQ MVNSGEAAAK EEWVATVTQL LMGIEQALSA 800
    DSSGSILKVS SSTTGLVRLT NNLIQVIDCS MAVQEEAKEP HVSSVLPWII 850
    LHRIIWQEED TFHSLCHQQQ LQNPAEEGMS ETPMLPSSLM LLNTAHEYLG 900
    RRSWCCNSDG ALLRFYVRVL QKELAASTSE DTHPYKEELE TALEQCFYCL 950
    YSFPSKKSKA RYLEEHSAQQ VDLIWEDALF MFEYFKPKTL PEFDSYKTST 1000
    VSADLANLLK RIATIVPRTE RPALSLDKVS AYIEGTSTEV PCLPEGADPS 1050
    PPVVNELYYL LADYHFKNKE QSKAIKFYMH DICICPNRFD SWAGMALARA 1100
    SRIQDKLNSN ELKSDGPIWK HATPVLNCFR RALEIDSSNL SLWIEYGTMS 1150
    YALHSFASRQ LKQWRGELPP ELVQQMEGRR DSMLETAKHC FTSAARCEGD 1200
    GDEEEWLIHY MLGKVAEKQQ QPPTVYLLHY RQAGHYLHEE AARYPKKIHY 1250
    HNPPELAMEA LEVYFRLHAS ILKLLGKPDS GVGAEVLVNF MKEAAEGPFA 1300
    RGEEKNTPKA SEKEKACLVD EDSHSSAGTL PGPGASLPSS SGPGLTSPPY 1350
    TATPIDHDYV KCKKPHQQAT PDDRSQDSTA VALSDSSSTQ DFFNEPTSLL 1400
    EGSRKSYTEK RLPILSSQAG ATGKDLQGAT EERGKNEESL ESTEGFRAAE 1450
    QGVQKPAAET PASACIPGKP SASTPTLWDG KKRGDLPGEP VAFPQGLPAG 1500
    AEEQRQFLTE QCIASFRLCL SRFPQHYKSL YRLAFLYTYS KTHRNLQWAR 1550
    DVLLGSSIPW QQLQHMPAQG LFCERNKTNF FNGIWRIPVD EIDRPGSFAW 1600
    HMNRSIVLLL KVLAQLRDHS TLLKVSSMLQ RTPDQGKKYL RDADRQVLAQ 1650
    RAFILTVKVL EDTLSELAEG SERPGPKVCG LPGARMTTDV SHKASPEDGQ 1700
    EGLPQPKKPP LADGSGPGPE PGGKVGLLNH RPVAMDAGDS ADQSGERKDK 1750
    ESPRAGPTEP MDTSEATVCH SDLERTPPLL PGRPARDRGP ESRPTELSLE 1800
    ELSISARQQP TPLTPAQPAP APAPATTTGT RAGGHPEEPL SRLSRKRKLL 1850
    EDTESGKTLL LDAYRVWQQG QKGVAYDLGR VERIMSETYM LIKQVDEEAA 1900
    LEQAVKFCQV HLGAAAQRQA SGDTPTTPKH PKDSRENFFP VTVVPTAPDP 1950
    VPADSVQRPS DAHTKPRPAL AAATTIITCP PSASASTLDQ SKDPGPPRPH 2000
    RPEATPSMAS LGPEGEELAR VAEGTSFPPQ EPRHSPQVKM APTSSPAEPH 2050
    CWPAEAALGT GAEPTCSQEG KLRPEPRRDG EAQEAASETQ PLSSPPTAAS 2100
    SKAPSSGSAQ PPEGHPGKPE PSRAKSRPLP NMPKLVIPSA ATKFPPEITV 2150
    TPPTPTLLSP KGSISEETKQ KLKSAILSAQ SAANVRKESL CQPALEVLET 2200
    SSQESSLESE TDEDDDYMDI 2220
    Length:2,220
    Mass (Da):246,352
    Last modified:November 1, 1999 - v1
    Checksum:iBA4AD1741056C233
    GO
    Isoform 2 (identifier: Q9Y6J0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         220-269: Missing.
         1344-1372: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:2,141
    Mass (Da):237,574
    Checksum:i3F14AC67988BE2E5
    GO

    Sequence cautioni

    The sequence BAA20788.2 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561A → T.
    Corresponds to variant rs5760185 [ dbSNP | Ensembl ].
    VAR_052607
    Natural varianti225 – 2251D → N.
    Corresponds to variant rs17004823 [ dbSNP | Ensembl ].
    VAR_052608
    Natural varianti517 – 5171S → R.
    Corresponds to variant rs9624393 [ dbSNP | Ensembl ].
    VAR_052609
    Natural varianti660 – 6601R → S.
    Corresponds to variant rs9624395 [ dbSNP | Ensembl ].
    VAR_052610
    Natural varianti853 – 8531R → Q.1 Publication
    Corresponds to variant rs17854874 [ dbSNP | Ensembl ].
    VAR_052611
    Natural varianti921 – 9211Q → E.
    Corresponds to variant rs12166151 [ dbSNP | Ensembl ].
    VAR_052612

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei220 – 26950Missing in isoform 2. 1 PublicationVSP_054161Add
    BLAST
    Alternative sequencei1344 – 137229Missing in isoform 2. 1 PublicationVSP_054162Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072441 mRNA. Translation: AAD40846.1.
    AP000351 Genomic DNA. No translation available.
    AP000352 Genomic DNA. No translation available.
    AP000353 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59639.1.
    BC054497 mRNA. Translation: AAH54497.1.
    Z92546 Genomic DNA. Translation: CAB62954.1.
    AB002328 mRNA. Translation: BAA20788.2. Different initiation.
    CCDSiCCDS13823.1. [Q9Y6J0-1]
    RefSeqiNP_001186210.1. NM_001199281.1. [Q9Y6J0-1]
    NP_001188358.1. NM_001201429.1.
    NP_036427.1. NM_012295.3. [Q9Y6J0-1]
    UniGeneiHs.517478.

    Genome annotation databases

    EnsembliENST00000263119; ENSP00000263119; ENSG00000099991. [Q9Y6J0-1]
    ENST00000398319; ENSP00000381364; ENSG00000099991. [Q9Y6J0-1]
    ENST00000405822; ENSP00000384694; ENSG00000099991. [Q9Y6J0-2]
    GeneIDi23523.
    KEGGihsa:23523.
    UCSCiuc002zzi.1. human. [Q9Y6J0-1]
    uc002zzj.1. human.

    Polymorphism databases

    DMDMi6685261.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072441 mRNA. Translation: AAD40846.1 .
    AP000351 Genomic DNA. No translation available.
    AP000352 Genomic DNA. No translation available.
    AP000353 Genomic DNA. No translation available.
    CH471095 Genomic DNA. Translation: EAW59639.1 .
    BC054497 mRNA. Translation: AAH54497.1 .
    Z92546 Genomic DNA. Translation: CAB62954.1 .
    AB002328 mRNA. Translation: BAA20788.2 . Different initiation.
    CCDSi CCDS13823.1. [Q9Y6J0-1 ]
    RefSeqi NP_001186210.1. NM_001199281.1. [Q9Y6J0-1 ]
    NP_001188358.1. NM_001201429.1.
    NP_036427.1. NM_012295.3. [Q9Y6J0-1 ]
    UniGenei Hs.517478.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N6J X-ray 2.20 G 2156-2190 [» ]
    ProteinModelPortali Q9Y6J0.
    SMRi Q9Y6J0. Positions 168-198, 615-644, 1057-1100.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117070. 20 interactions.
    IntActi Q9Y6J0. 1 interaction.
    MINTi MINT-2824170.
    STRINGi 9606.ENSP00000263119.

    PTM databases

    PhosphoSitei Q9Y6J0.

    Polymorphism databases

    DMDMi 6685261.

    Proteomic databases

    MaxQBi Q9Y6J0.
    PaxDbi Q9Y6J0.
    PRIDEi Q9Y6J0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263119 ; ENSP00000263119 ; ENSG00000099991 . [Q9Y6J0-1 ]
    ENST00000398319 ; ENSP00000381364 ; ENSG00000099991 . [Q9Y6J0-1 ]
    ENST00000405822 ; ENSP00000384694 ; ENSG00000099991 . [Q9Y6J0-2 ]
    GeneIDi 23523.
    KEGGi hsa:23523.
    UCSCi uc002zzi.1. human. [Q9Y6J0-1 ]
    uc002zzj.1. human.

    Organism-specific databases

    CTDi 23523.
    GeneCardsi GC22P024407.
    HGNCi HGNC:24187. CABIN1.
    HPAi HPA043296.
    MIMi 604251. gene.
    neXtProti NX_Q9Y6J0.
    PharmGKBi PA164717549.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG84755.
    HOGENOMi HOG000111281.
    HOVERGENi HBG050758.
    InParanoidi Q9Y6J0.
    KOi K17613.
    OMAi AEPTCSQ.
    OrthoDBi EOG7R56RQ.
    PhylomeDBi Q9Y6J0.
    TreeFami TF323227.

    Enzyme and pathway databases

    Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

    Miscellaneous databases

    EvolutionaryTracei Q9Y6J0.
    GeneWikii CABIN1.
    GenomeRNAii 23523.
    NextBioi 35518161.
    PROi Q9Y6J0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6J0.
    Bgeei Q9Y6J0.
    CleanExi HS_CABIN1.
    Genevestigatori Q9Y6J0.

    Family and domain databases

    Gene3Di 1.25.40.10. 3 hits.
    InterProi IPR015134. MEF2_binding.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF09047. MEF2_binding. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 4 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 4 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cabin 1, a negative regulator for calcineurin signaling in T lymphocytes."
      Sun L., Youn H.-D., Loh C., Stolow M., He W., Liu J.O.
      Immunity 8:703-711(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CALCINEURIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
      Tissue: Kidney.
    2. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [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] (ISOFORM 2), VARIANT GLN-853.
      Tissue: Testis.
    5. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-2220 (ISOFORM 1).
      Tissue: Brain.
    6. "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis."
      Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.
      Cell 116:51-61(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH ASF1A; HIRA; HISTONE H3.3 AND UBN1.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "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-2151 AND THR-2154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-66 AND SER-1439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Phosphorylation and ubiquitination-dependent degradation of CABIN1 releases p53 for transactivation upon genotoxic stress."
      Choi S.Y., Jang H., Roe J.S., Kim S.T., Cho E.J., Youn H.D.
      Nucleic Acids Res. 41:2180-2190(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ATM AND CHK2, UBIQUITINATION.
    11. "Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2."
      Han A., Pan F., Stroud J.C., Youn H.-D., Liu J.O., Chen L.
      Nature 422:730-734(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2156-2190 IN COMPLEX WITH MEF2B AND DNA, MUTAGENESIS OF LEU-2172.

    Entry informationi

    Entry nameiCABIN_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6J0
    Secondary accession number(s): G5E9F3, Q6PHY0, Q9Y460
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 136 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 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3