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Q8CGB3 (UACA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Uveal autoantigen with coiled-coil domains and ankyrin repeats
Alternative name(s):
Nuclear membrane-binding protein
Short name=Nucling
Gene names
Name:Uaca
Synonyms:Kiaa1561
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1411 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates APAF1 expression and plays an important role in the regulation of stress-induced apoptosis. Promotes apoptosis by regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3 down-regulation and NF-kappa-B inactivation. Regulates the redistribution of APAF1 into the nucleus after proapoptotic stress. Down-regulates the expression of LGALS3 by inhibiting NFKB1. Ref.5 Ref.6

Modulates isoactin dynamics to regulate the morphological alterations required for cell growth and motility. Interaction with ARF6 may modulate cell shape and motility after injury By similarity. Ref.5 Ref.6

Subunit structure

Component of the apoptosome complex, composed of APAF1, pro-caspase-9 and UACA. In the complex, it probably interacts directly with APAF1. Interacts with LGALS3, ARF6 and ACTB. Ref.5 Ref.6

Subcellular location

Nucleus. Cytoplasm. Cytoplasmcytoskeleton. Note: Expressed diffusely in cytoplasm. Ref.1

Tissue specificity

Highly expressed in heart, liver, kidney and testis. Weakly expressed in lung and skeletal muscle. Not expressed in brain and spleen. Ref.1

Developmental stage

First detected at the E9.5 stage in heart at the edge of both sides of the common ventricular chamber and is then progressively increased and restricted to the myocardial wall of left common ventricular chamber of heart. Ref.1

Induction

Up-regulated during cardiomyogenic differentiation. By apoptotic stress in a dose-dependent manner. Ref.1

Disruption phenotype

Mice show a high incidence of inflammatory lesions in preputial glands. Cells around the lesions showed resistance to apoptosis. Ref.6

Sequence similarities

Contains 6 ANK repeats.

Sequence caution

The sequence BAC78213.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAD32481.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Coiled coil
Repeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processintrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype Ref.5. Source: MGI

intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from mutant phenotype Ref.5. Source: MGI

negative regulation of NF-kappaB import into nucleus

Inferred from mutant phenotype Ref.6. Source: MGI

negative regulation of inflammatory response

Inferred from mutant phenotype Ref.6. Source: MGI

positive regulation of apoptotic process

Inferred from direct assay Ref.5. Source: MGI

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.5. Source: MGI

positive regulation of protein import into nucleus

Inferred from mutant phenotype Ref.5. Source: MGI

response to UV

Inferred from mutant phenotype Ref.5. Source: MGI

   Cellular_componentapoptosome

Inferred from direct assay Ref.5. Source: MGI

cytoplasm

Inferred from direct assay Ref.1Ref.6. Source: MGI

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.5. Source: MGI

membrane

Inferred from direct assay Ref.1. Source: MGI

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from direct assay Ref.1Ref.6. Source: MGI

nucleus

Inferred from direct assay Ref.5. Source: MGI

perinuclear region of cytoplasm

Inferred from direct assay Ref.5. Source: MGI

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CGB3-1)

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: Q8CGB3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-398: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8CGB3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     264-264: G → GGG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14111411Uveal autoantigen with coiled-coil domains and ankyrin repeats
PRO_0000231651

Regions

Repeat69 – 9830ANK 1
Repeat102 – 13130ANK 2
Repeat135 – 16430ANK 3
Repeat168 – 19730ANK 4
Repeat201 – 23030ANK 5
Repeat234 – 26330ANK 6
Coiled coil299 – 37981 Potential
Coiled coil442 – 624183 Potential
Coiled coil652 – 1380729 Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2801Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 398398Missing in isoform 2.
VSP_017874
Alternative sequence2641G → GGG in isoform 3.
VSP_017875

Experimental info

Sequence conflict1441V → A in AAH42415. Ref.3
Sequence conflict3531P → L in AAH42415. Ref.3
Sequence conflict7571R → K in AAH42415. Ref.3
Sequence conflict7781A → T in AAH42415. Ref.3

Sequences

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

Last modified April 4, 2006. Version 2.
Checksum: 0809D2DE9732F879

FASTA1,411160,813
        10         20         30         40         50         60 
MKSLKSRLWK QDAPGPTSPS SPTAVASTQS AEWNKYDDRL MKAAERGDVE KVSSILAKKG 

        70         80         90        100        110        120 
VHPGKLDVEG RSAFHVVASK GNLECLNAIL THGIDVATRD SAGRNALHLA AKYGHALCLQ 

       130        140        150        160        170        180 
KLLQYNCPTE HVDLQGRTAL HDAVMADCPS SIQLLCDHGA SVNAKDIDGR TPLVLATQMC 

       190        200        210        220        230        240 
RPTICQLLID RGADVNSRDK QNRTALMLGC EYGCRDAVEV LVKNGADLTL LDALGHDSSY 

       250        260        270        280        290        300 
YARIGDNLDI LNLLKTASEN TNKGRELWRK GPPLQQRNLS HTQDEGSVKS TQREQREPHS 

       310        320        330        340        350        360 
FQDLEIENED LREKLRKIQQ EQRILLDKVN GLQLQLNEEV MVADDLESER EKPKSLLAAK 

       370        380        390        400        410        420 
EKQHEESLRT IEALKNRFKY FESDHPGPGS YPSNRKEDML HKQGQMYTTE PQCASPGIPP 

       430        440        450        460        470        480 
HMHSRSMLRP LELSLPSQTS YSENEILKKE LETLRTYYDS AKQDRLKFQN ELAHKVAECK 

       490        500        510        520        530        540 
ALALECERVK EDSDEQIKQL EDALKDVQKR MYESEGKVKQ MQTHFLALKE HLTNEAATGS 

       550        560        570        580        590        600 
HRIIEELREQ LKDLKGKYEG ASAEVGKLRS QIKQSEMLVG EFKRDEGRLV EENKRLQKEC 

       610        620        630        640        650        660 
GTCEVELERR GRRVVELEGQ LKELGAKLAL SVPTEKFESM KSSLSNDINE KVKRLAEVGR 

       670        680        690        700        710        720 
DYESAQGEIR QLKRDLESVR AQHIRPEEHE QLRSRLEQKS GELGKKVSEL TLKNQTLQKD 

       730        740        750        760        770        780 
VEKLHADNKL LNQQVHSLTV EMKTRYVPLR VSEEMKRSHD VNVEDLNKKL SEATQRYAEK 

       790        800        810        820        830        840 
KQEAERLLAE NDKLTKNVSR LEAVFVAPEK HEKELMGLKS NIAELKKQLS ELNKKCGEGQ 

       850        860        870        880        890        900 
EKIRALMSEN SSLKKTLSSQ YVPAKTHEEV KASLNSTVEK TNRALLEAKK RFDDTSQEVS 

       910        920        930        940        950        960 
KLRDENEVLR RNLENVQNQM KADYVSLEEH SRRMSTVSQS LKEAQEANAA ILADHRQGQE 

       970        980        990       1000       1010       1020 
EIVSLHAEIK AQKKELDTIQ ECIKLKYAPL ARLEECERKF KATEKGLKEQ LSEQTHKCRQ 

      1030       1040       1050       1060       1070       1080 
RDEEVKKGKQ ENERLRADLA ALQKELQDRN ALAEEAREAE RALSGKADEL SKQLKDLSQK 

      1090       1100       1110       1120       1130       1140 
YSDVKSEREK LVEEKAKQAS EILAAQNLLQ KQPVPLEQVE ALKKSLNGTI EQLKEELRSK 

      1150       1160       1170       1180       1190       1200 
QRCLEREQQT VSQLQQLLEN QKNSSVTLAE HLKLKEALEK EVGIMKASLR EKEEESQKKT 

      1210       1220       1230       1240       1250       1260 
KEVSKLQTEV QTTKQALKNL ETREVVDMSK YKATKNDLET QISNLNDKLA SLNRKYDQAC 

      1270       1280       1290       1300       1310       1320 
EEKVSAKDEK ELLHLSIEQE IRDQKERCDK SLTTIMELQQ RIQESAKQIE AKDNKITELL 

      1330       1340       1350       1360       1370       1380 
NDVERLKQAL NGLSQLTYSS GSPTKRQSQL VDTLQQRVRD LQQQLADADR QHQEVIAIYR 

      1390       1400       1410 
THLLSAAQGH MDEDVQAALL QIIQMRQGLV C 

« Hide

Isoform 2 [UniParc].

Checksum: 13DDD2313B8FED0F
Show »

FASTA1,013116,517
Isoform 3 [UniParc].

Checksum: 89FA7474FDE59D5C
Show »

FASTA1,413160,927

References

« Hide 'large scale' references
[1]"Identification of a novel, embryonal carcinoma cell-associated molecule, nucling, that is up-regulated during cardiac muscle differentiation."
Sakai T., Liu L., Shishido Y., Fukui K.
J. Biochem. 133:429-436(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
Strain: 129.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryonic intestine.
[3]"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 3).
Strain: FVB/N.
Tissue: Mammary gland and Salivary gland.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-306.
Strain: C57BL/6J.
Tissue: Eye.
[5]"Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of stress-induced apoptosis."
Sakai T., Liu L., Teng X., Mukai-Sakai R., Shimada H., Kaji R., Mitani T., Matsumoto M., Toida K., Ishimura K., Shishido Y., Mak T.W., Fukui K.
J. Biol. Chem. 279:41131-41140(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH APAF1.
[6]"Nucling mediates apoptosis by inhibiting expression of galectin-3 through interference with nuclear factor kappaB signalling."
Liu L., Sakai T., Sano N., Fukui K.
Biochem. J. 380:31-41(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH LGALS3, DISRUPTION PHENOTYPE.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB030647 mRNA. Translation: BAC78213.1. Different initiation.
AK173203 mRNA. Translation: BAD32481.1. Different initiation.
BC042415 mRNA. Translation: AAH42415.1.
AK087466 mRNA. Translation: BAC39886.1.
CCDSCCDS23259.1. [Q8CGB3-3]
RefSeqNP_082559.1. NM_028283.2.
XP_006511543.1. XM_006511480.1.
UniGeneMm.68819.

3D structure databases

ProteinModelPortalQ8CGB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215442. 3 interactions.

PTM databases

PhosphoSiteQ8CGB3.

Proteomic databases

MaxQBQ8CGB3.
PaxDbQ8CGB3.
PRIDEQ8CGB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050183; ENSMUSP00000062047; ENSMUSG00000034485.
GeneID72565.
KEGGmmu:72565.
UCSCuc009pzi.1. mouse. [Q8CGB3-3]
uc009pzk.1. mouse. [Q8CGB3-1]

Organism-specific databases

CTD55075.
MGIMGI:1919815. Uaca.
RougeSearch...

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00530000063369.
HOGENOMHOG000147885.
HOVERGENHBG066395.
InParanoidQ8CGB3.
OrthoDBEOG7X9G6C.
PhylomeDBQ8CGB3.
TreeFamTF331274.

Gene expression databases

BgeeQ8CGB3.
GenevestigatorQ8CGB3.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUACA. mouse.
NextBio336503.
PROQ8CGB3.
SOURCESearch...

Entry information

Entry nameUACA_MOUSE
AccessionPrimary (citable) accession number: Q8CGB3
Secondary accession number(s): Q69ZG3, Q7TN77, Q8BJC8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot