Q9Y6J0 (CABIN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calcineurin-binding protein cabin-1

Alternative name(s):
Calcineurin inhibitor
Short name=CAIN

Gene names

Name:	CABIN1
Synonyms:	KIAA0330

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2220 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.4
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.4
Subcellular location	Nucleus Ref.1.
Tissue specificity	Widely expressed in different tissues. Ref.1
Post-translational modification	Activated through PKC-mediated hyperphosphorylation.
Sequence similarities	Contains 6 TPR repeats.
Sequence caution	The sequence BAA20788.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat TPR repeat
Molecular function	Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Non-traceable author statement Ref.1. Source: UniProtKB chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	aggresome Inferred from direct assay. Source: HPA cytoplasm Inferred from direct assay. Source: HPA nucleus Non-traceable author statement. Source: UniProtKB
Molecular_function	protein phosphatase inhibitor activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2220

2220

Calcineurin-binding protein cabin-1

PRO_0000106275

Regions

Repeat

36 – 69

34

TPR 1

Repeat

90 – 123

34

TPR 2

Repeat

125 – 157

33

TPR 3

Repeat

615 – 648

34

TPR 4

Repeat

1055 – 1088

34

TPR 5

Repeat

1106 – 1139

34

TPR 6

Region

2116 – 2153

38

Required for interaction with calcineurin By similarity

Amino acid modifications

Modified residue

66

1

Phosphoserine Ref.7

Modified residue

1439

1

Phosphoserine Ref.7

Modified residue

2151

1

Phosphothreonine Ref.6

Modified residue

2154

1

Phosphothreonine Ref.6

Natural variations

Natural variant

56

1

A → T.
Corresponds to variant rs5760185 [ dbSNP | Ensembl ].

VAR_052607

Natural variant

225

1

D → N.
Corresponds to variant rs17004823 [ dbSNP | Ensembl ].

VAR_052608

Natural variant

517

1

S → R.
Corresponds to variant rs9624393 [ dbSNP | Ensembl ].

VAR_052609

Natural variant

660

1

R → S.
Corresponds to variant rs9624395 [ dbSNP | Ensembl ].

VAR_052610

Natural variant

853

1

R → Q.
Corresponds to variant rs17854874 [ dbSNP | Ensembl ].

VAR_052611

Natural variant

921

1

Q → E.
Corresponds to variant rs12166151 [ dbSNP | Ensembl ].

VAR_052612

Experimental info

Mutagenesis

2172

1

L → A, K or W: Abrogates binding to MEF2B. Ref.8

Secondary structure

1

.

.

.

2220

Helix Strand Turn

Details...

Helix

2166 – 2177

12

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6J0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: BA4AD1741056C233	FASTA	2,220	246,352
	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

References

	« Hide 'large scale' referencesShow '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], 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]	"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. Tissue: Brain.
[4]	"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.
[5]	"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.
[6]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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, MASS SPECTROMETRY.
[8]	"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.
AP000352 Genomic DNA. No translation available.
AP000353 Genomic DNA. No translation available.
Z92546 Genomic DNA. Translation: CAB62954.1.
AB002328 mRNA. Translation: BAA20788.2. Different initiation.

IPI

IPI00002355.

RefSeq

NP_001186210.1. NM_001199281.1.
NP_001188358.1. NM_001201429.1.
NP_036427.1. NM_012295.3.

UniGene

Hs.517478.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1N6J	X-ray	2.20	G	2156-2190	[»]

ProteinModelPortal

Q9Y6J0.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000263119.

PTM databases

PhosphoSite

Q9Y6J0.

Polymorphism databases

DMDM

6685261.

Proteomic databases

PaxDb

Q9Y6J0.

PRIDE

Q9Y6J0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263119; ENSP00000263119; ENSG00000099991.
ENST00000398319; ENSP00000381364; ENSG00000099991.

GeneID

23523.

KEGG

hsa:23523.

UCSC

uc002zzi.1. human.

Organism-specific databases

CTD

23523.

GeneCards

GC22P024407.

HGNC

HGNC:24187. CABIN1.

HPA

HPA043296.

MIM

604251. gene.

neXtProt

NX_Q9Y6J0.

PharmGKB

PA164717549.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG84755.

HOGENOM

HOG000111281.

HOVERGEN

HBG050758.

InParanoid

Q9Y6J0.

OMA

AEPTCSQ.

OrthoDB

EOG4NZTSB.

PhylomeDB

Q9Y6J0.

Enzyme and pathway databases

Pathway_Interaction_DB

tcrcalciumpathway. Calcium signaling in the CD4+ TCR pathway.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.

Gene expression databases

ArrayExpress

Q9Y6J0.

Bgee

Q9Y6J0.

CleanEx

HS_CABIN1.

Genevestigator

Q9Y6J0.

GermOnline

ENSG00000099991. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.10. 3 hits.

InterPro

IPR015134. MEF2_binding.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Pfam

PF09047. MEF2_binding. 1 hit.
[Graphical view]

SMART

SM00028. TPR. 4 hits.
[Graphical view]

PROSITE

PS50005. TPR. 4 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Y6J0.

GenomeRNAi

23523.

NextBio

45981.

SOURCE

Search...

Entry information

Entry name

CABIN_HUMAN

Accession

Primary (citable) accession number: Q9Y6J0
Secondary accession number(s): Q9Y460

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.