Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y6J0 (CABIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcineurin-binding protein cabin-1
Alternative name(s):
Calcineurin inhibitor
Short name=CAIN
Gene names
Name:CABIN1
Synonyms:KIAA0330
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6

Subunit structure

Component of a complex that includes at least ASF1A, CABIN1, HIRA, histone H3.3 and UBN1. Interacts with calcineurin. Interacts with MEF2B. Ref.1 Ref.6

Subcellular location

Nucleus Ref.1.

Tissue specificity

Widely expressed in different tissues. Ref.1

Post-translational modification

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.

Sequence similarities

Contains 6 TPR repeats.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6J0-1)

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.
Isoform 2 (identifier: Q9Y6J0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     220-269: Missing.
     1344-1372: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22202220Calcineurin-binding protein cabin-1
PRO_0000106275

Regions

Repeat36 – 6934TPR 1
Repeat90 – 12334TPR 2
Repeat125 – 15733TPR 3
Repeat615 – 64834TPR 4
Repeat1055 – 108834TPR 5
Repeat1106 – 113934TPR 6
Region2116 – 215338Required for interaction with calcineurin By similarity

Amino acid modifications

Modified residue661Phosphoserine Ref.9
Modified residue14391Phosphoserine Ref.9
Modified residue21511Phosphothreonine Ref.8
Modified residue21541Phosphothreonine Ref.8

Natural variations

Alternative sequence220 – 26950Missing in isoform 2.
VSP_054161
Alternative sequence1344 – 137229Missing in isoform 2.
VSP_054162
Natural variant561A → T.
Corresponds to variant rs5760185 [ dbSNP | Ensembl ].
VAR_052607
Natural variant2251D → N.
Corresponds to variant rs17004823 [ dbSNP | Ensembl ].
VAR_052608
Natural variant5171S → R.
Corresponds to variant rs9624393 [ dbSNP | Ensembl ].
VAR_052609
Natural variant6601R → S.
Corresponds to variant rs9624395 [ dbSNP | Ensembl ].
VAR_052610
Natural variant8531R → Q. Ref.4
Corresponds to variant rs17854874 [ dbSNP | Ensembl ].
VAR_052611
Natural variant9211Q → E.
Corresponds to variant rs12166151 [ dbSNP | Ensembl ].
VAR_052612

Experimental info

Mutagenesis21721L → A, K or W: Abrogates binding to MEF2B. Ref.11

Secondary structure

... 2220
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: BA4AD1741056C233

FASTA2,220246,352
        10         20         30         40         50         60 
MIRIAALNAS STIEDDHEGS FKSHKTQTKE AQEAEAFALY HKALDLQKHD RFEESAKAYH 

        70         80         90        100        110        120 
ELLEASLLRE AVSSGDEKEG LKHPGLILKY STYKNLAQLA AQREDLETAM EFYLEAVMLD 

       130        140        150        160        170        180 
STDVNLWYKI GHVALRLIRI PLARHAFEEG LRCNPDHWPC LDNLITVLYT LSDYTTCLYF 

       190        200        210        220        230        240 
ICKALEKDCR YSKGLVLKEK IFEEQPCLRK DSLRMFLKCD MSIHDVSVSA AETQAIVDEA 

       250        260        270        280        290        300 
LGLRKKRQAL IVREKEPDLK LVQPIPFFTW KCLGESLLAM YNHLTTCEPP RPSLGKRIDL 

       310        320        330        340        350        360 
SDYQDPSQPL ESSMVVTPVN VIQPSTVSTN PAVAVAEPVV SYTSVATTSF PLHSPGLLET 

       370        380        390        400        410        420 
GAPVGDISGG DKSKKGVKRK KISEESGETA KRRSARVRNT KCKKEEKVDF QELLMKFLPS 

       430        440        450        460        470        480 
RLRKLDPEEE DDSFNNYEVQ SEAKLESFPS IGPQRLSFDS ATFMESEKQD VHEFLLENLT 

       490        500        510        520        530        540 
NGGILELMMR YLKAMGHKFL VRWPPGLAEV VLSVYHSWRR HSTSLPNPLL RDCSNKHIKD 

       550        560        570        580        590        600 
MMLMSLSCME LQLDQWLLTK GRSSAVSPRN CPAGMVNGRF GPDFPGTHCL GDLLQLSFAS 

       610        620        630        640        650        660 
SQRDLFEDGW LEFVVRVYWL KARFLALQGD MEQALENYDI CTEMLQSSTA IQVEAGAERR 

       670        680        690        700        710        720 
DIVIRLPNLH NDSVVSLEEI DKNLKSLERC QSLEEIQRLY EAGDYKAVVH LLRPTLCTSG 

       730        740        750        760        770        780 
FDRAKHLEFM TSIPERPAQL LLLQDSLLRL KDYRQCFECS DVALNEAVQQ MVNSGEAAAK 

       790        800        810        820        830        840 
EEWVATVTQL LMGIEQALSA DSSGSILKVS SSTTGLVRLT NNLIQVIDCS MAVQEEAKEP 

       850        860        870        880        890        900 
HVSSVLPWII LHRIIWQEED TFHSLCHQQQ LQNPAEEGMS ETPMLPSSLM LLNTAHEYLG 

       910        920        930        940        950        960 
RRSWCCNSDG ALLRFYVRVL QKELAASTSE DTHPYKEELE TALEQCFYCL YSFPSKKSKA 

       970        980        990       1000       1010       1020 
RYLEEHSAQQ VDLIWEDALF MFEYFKPKTL PEFDSYKTST VSADLANLLK RIATIVPRTE 

      1030       1040       1050       1060       1070       1080 
RPALSLDKVS AYIEGTSTEV PCLPEGADPS PPVVNELYYL LADYHFKNKE QSKAIKFYMH 

      1090       1100       1110       1120       1130       1140 
DICICPNRFD SWAGMALARA SRIQDKLNSN ELKSDGPIWK HATPVLNCFR RALEIDSSNL 

      1150       1160       1170       1180       1190       1200 
SLWIEYGTMS YALHSFASRQ LKQWRGELPP ELVQQMEGRR DSMLETAKHC FTSAARCEGD 

      1210       1220       1230       1240       1250       1260 
GDEEEWLIHY MLGKVAEKQQ QPPTVYLLHY RQAGHYLHEE AARYPKKIHY HNPPELAMEA 

      1270       1280       1290       1300       1310       1320 
LEVYFRLHAS ILKLLGKPDS GVGAEVLVNF MKEAAEGPFA RGEEKNTPKA SEKEKACLVD 

      1330       1340       1350       1360       1370       1380 
EDSHSSAGTL PGPGASLPSS SGPGLTSPPY TATPIDHDYV KCKKPHQQAT PDDRSQDSTA 

      1390       1400       1410       1420       1430       1440 
VALSDSSSTQ DFFNEPTSLL EGSRKSYTEK RLPILSSQAG ATGKDLQGAT EERGKNEESL 

      1450       1460       1470       1480       1490       1500 
ESTEGFRAAE QGVQKPAAET PASACIPGKP SASTPTLWDG KKRGDLPGEP VAFPQGLPAG 

      1510       1520       1530       1540       1550       1560 
AEEQRQFLTE QCIASFRLCL SRFPQHYKSL YRLAFLYTYS KTHRNLQWAR DVLLGSSIPW 

      1570       1580       1590       1600       1610       1620 
QQLQHMPAQG LFCERNKTNF FNGIWRIPVD EIDRPGSFAW HMNRSIVLLL KVLAQLRDHS 

      1630       1640       1650       1660       1670       1680 
TLLKVSSMLQ RTPDQGKKYL RDADRQVLAQ RAFILTVKVL EDTLSELAEG SERPGPKVCG 

      1690       1700       1710       1720       1730       1740 
LPGARMTTDV SHKASPEDGQ EGLPQPKKPP LADGSGPGPE PGGKVGLLNH RPVAMDAGDS 

      1750       1760       1770       1780       1790       1800 
ADQSGERKDK ESPRAGPTEP MDTSEATVCH SDLERTPPLL PGRPARDRGP ESRPTELSLE 

      1810       1820       1830       1840       1850       1860 
ELSISARQQP TPLTPAQPAP APAPATTTGT RAGGHPEEPL SRLSRKRKLL EDTESGKTLL 

      1870       1880       1890       1900       1910       1920 
LDAYRVWQQG QKGVAYDLGR VERIMSETYM LIKQVDEEAA LEQAVKFCQV HLGAAAQRQA 

      1930       1940       1950       1960       1970       1980 
SGDTPTTPKH PKDSRENFFP VTVVPTAPDP VPADSVQRPS DAHTKPRPAL AAATTIITCP 

      1990       2000       2010       2020       2030       2040 
PSASASTLDQ SKDPGPPRPH RPEATPSMAS LGPEGEELAR VAEGTSFPPQ EPRHSPQVKM 

      2050       2060       2070       2080       2090       2100 
APTSSPAEPH CWPAEAALGT GAEPTCSQEG KLRPEPRRDG EAQEAASETQ PLSSPPTAAS 

      2110       2120       2130       2140       2150       2160 
SKAPSSGSAQ PPEGHPGKPE PSRAKSRPLP NMPKLVIPSA ATKFPPEITV TPPTPTLLSP 

      2170       2180       2190       2200       2210       2220 
KGSISEETKQ KLKSAILSAQ SAANVRKESL CQPALEVLET SSQESSLESE TDEDDDYMDI 

« Hide

Isoform 2 [UniParc].

Checksum: 3F14AC67988BE2E5
Show »

FASTA2,141237,574

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001186210.1. NM_001199281.1.
NP_001188358.1. NM_001201429.1.
NP_036427.1. NM_012295.3.
UniGeneHs.517478.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N6JX-ray2.20G2156-2190[»]
ProteinModelPortalQ9Y6J0.
SMRQ9Y6J0. Positions 38-190, 1060-1151, 1187-1233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117070. 20 interactions.
IntActQ9Y6J0. 1 interaction.
MINTMINT-2824170.
STRING9606.ENSP00000263119.

PTM databases

PhosphoSiteQ9Y6J0.

Polymorphism databases

DMDM6685261.

Proteomic databases

PaxDbQ9Y6J0.
PRIDEQ9Y6J0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263119; ENSP00000263119; ENSG00000099991.
ENST00000398319; ENSP00000381364; ENSG00000099991.
ENST00000405822; ENSP00000384694; ENSG00000099991.
GeneID23523.
KEGGhsa:23523.
UCSCuc002zzi.1. human.

Organism-specific databases

CTD23523.
GeneCardsGC22P024407.
HGNCHGNC:24187. CABIN1.
HPAHPA043296.
MIM604251. gene.
neXtProtNX_Q9Y6J0.
PharmGKBPA164717549.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG84755.
HOGENOMHOG000111281.
HOVERGENHBG050758.
InParanoidQ9Y6J0.
KOK17613.
OMAAEPTCSQ.
OrthoDBEOG7R56RQ.
PhylomeDBQ9Y6J0.
TreeFamTF323227.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ9Y6J0.
BgeeQ9Y6J0.
CleanExHS_CABIN1.
GenevestigatorQ9Y6J0.

Family and domain databases

Gene3D1.25.40.10. 3 hits.
InterProIPR015134. MEF2_binding.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF09047. MEF2_binding. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS50005. TPR. 4 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y6J0.
GeneWikiCABIN1.
GenomeRNAi23523.
NextBio45981.
PROQ9Y6J0.
SOURCESearch...

Entry information

Entry nameCABIN_HUMAN
AccessionPrimary (citable) accession number: Q9Y6J0
Secondary accession number(s): G5E9F3, Q6PHY0, Q9Y460
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM