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Q9Y6J0

- CABIN_HUMAN

UniProt

Q9Y6J0 - CABIN_HUMAN

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Protein

Calcineurin-binding protein cabin-1

Gene
CABIN1, KIAA0330
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
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.

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.2 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.

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 calcineurin By similarityAdd
BLAST

Sequence similaritiesi

Contains 6 TPR repeats.

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. VSP_054161Add
BLAST
Alternative sequencei1344 – 137229Missing in isoform 2. VSP_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.
ENST00000398319; ENSP00000381364; ENSG00000099991.
ENST00000405822; ENSP00000384694; ENSG00000099991.
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 .
ENST00000398319 ; ENSP00000381364 ; ENSG00000099991 .
ENST00000405822 ; ENSP00000384694 ; ENSG00000099991 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 135 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

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