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Q9BTA9 (WAC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
WW domain-containing adapter protein with coiled-coil
Gene names
Name:WAC
Synonyms:KIAA1844
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length647 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a linker between gene transcription and histone H2B monoubiquitination at 'Lys-120' (H2BK120ub1). Interacts with the RNA polymerase II transcriptional machinery via its WW domain and with RNF20-RNF40 via its coiled coil region, thereby linking and regulating H2BK120ub1 and gene transcription. Regulates the cell-cycle checkpoint activation in response to DNA damage. Positive regulator of amino acid starvation-induced autophagy. May negatively regulate the ubiquitin proteasome pathway. Ref.16 Ref.18

Subunit structure

Interacts (via coiled coil domain) with RNF20, RNF40 and UBE2A. Interacts (via WW domain) with RNA polymerase II. Ref.18

Subcellular location

Nucleus speckle By similarity. Nucleus. Note: In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes By similarity. Ref.18

Post-translational modification

Phosphorylated on tyrosine residues By similarity.

Sequence similarities

Contains 1 WW domain.

Sequence caution

The sequence AAH04258.2 differs from that shown. Reason: Frameshift at position 641.

The sequence AAH10356.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB47473.1 differs from that shown. Reason: Probable cloning artifact.

The sequence CAH70767.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40921.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40923.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1 DNA damage checkpoint

Inferred from mutant phenotype Ref.18. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.18. Source: UniProtKB

histone H2B conserved C-terminal lysine ubiquitination

Inferred from mutant phenotype Ref.18. Source: UniProtKB

histone monoubiquitination

Inferred from mutant phenotype Ref.18. Source: UniProtKB

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.16. Source: BHF-UCL

positive regulation of macroautophagy

Inferred from mutant phenotype Ref.16. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.18. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement Ref.16. Source: BHF-UCL

spliceosomal complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II core binding

Inferred from direct assay Ref.18. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428585EBI-749118,EBI-466029

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BTA9-1)

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: Q9BTA9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
Isoform 3 (identifier: Q9BTA9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.
     430-481: AQPSNQSPMS...PPVSSQPKVS → DIPLHEGIQM...MVQRLLQPSG
     482-647: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 4 (identifier: Q9BTA9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     204-307: MEDKHSSDAS...VPAQKTERKE → K

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 647647WW domain-containing adapter protein with coiled-coil
PRO_0000254558

Regions

Domain129 – 16234WW
Coiled coil618 – 64427 Potential

Amino acid modifications

Modified residue531Phosphoserine Ref.9 Ref.14
Modified residue2931Phosphothreonine Ref.10
Modified residue3021N6-acetyllysine Ref.13
Modified residue4711Phosphothreonine Ref.12
Modified residue5111Phosphoserine Ref.8
Modified residue5231Phosphoserine Ref.12
Modified residue5251Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 4545Missing in isoform 2 and isoform 3.
VSP_021230
Alternative sequence204 – 307104MEDKH…TERKE → K in isoform 4.
VSP_021231
Alternative sequence430 – 48152AQPSN…QPKVS → DIPLHEGIQMERDTHRSKWE VKGSLCQKADKQQECLVWNG SIMVQRLLQPSG in isoform 3.
VSP_021233
Alternative sequence482 – 647166Missing in isoform 3.
VSP_021236
Natural variant2421S → R.
Corresponds to variant rs11595926 [ dbSNP | Ensembl ].
VAR_028838
Natural variant3091T → A.
Corresponds to variant rs2232791 [ dbSNP | Ensembl ].
VAR_053448
Natural variant4751S → L in a colorectal cancer sample; somatic mutation. Ref.17
VAR_036351
Natural variant5311T → S.
Corresponds to variant rs7127 [ dbSNP | Ensembl ].
VAR_028839

Experimental info

Sequence conflict4261L → F in BAB71029. Ref.1
Sequence conflict5811K → R in AAH10356. Ref.6
Sequence conflict5991S → P in BAD97320. Ref.2

Sequences

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

Last modified October 31, 2006. Version 3.
Checksum: 15C32DAAA3A94129

FASTA64770,724
        10         20         30         40         50         60 
MVMYARKQQR LSDGCHDRRG DSQPYQALKY SSKSHPSSGD HRHEKMRDAG DPSPPNKMLR 

        70         80         90        100        110        120 
RSDSPENKYS DSTGHSKAKN VHTHRVRERD GGTSYSPQEN SHNHSALHSS NSHSSNPSNN 

       130        140        150        160        170        180 
PSKTSDAPYD SADDWSEHIS SSGKKYYYNC RTEVSQWEKP KEWLEREQRQ KEANKMAVNS 

       190        200        210        220        230        240 
FPKDRDYRRE VMQATATSGF ASGMEDKHSS DASSLLPQNI LSQTSRHNDR DYRLPRAETH 

       250        260        270        280        290        300 
SSSTPVQHPI KPVVHPTATP STVPSSPFTL QSDHQPKKSF DANGASTLSK LPTPTSSVPA 

       310        320        330        340        350        360 
QKTERKESTS GDKPVSHSCT TPSTSSASGL NPTSAPPTSA SAVPVSPVPQ SPIPPLLQDP 

       370        380        390        400        410        420 
NLLRQLLPAL QATLQLNNSN VDISKINEVL TAAVTQASLQ SIIHKFLTAG PSAFNITSLI 

       430        440        450        460        470        480 
SQAAQLSTQA QPSNQSPMSL TSDASSPRSY VSPRISTPQT NTVPIKPLIS TPPVSSQPKV 

       490        500        510        520        530        540 
STPVVKQGPV SQSATQQPVT ADKQQGHEPV SPRSLQRSSS QRSPSPGPNH TSNSSNASNA 

       550        560        570        580        590        600 
TVVPQNSSAR STCSLTPALA AHFSENLIKH VQGWPADHAE KQASRLREEA HNMGTIHMSE 

       610        620        630        640 
ICTELKNLRS LVRVCEIQAT LREQRILFLR QQIKELEKLK NQNSFMV 

« Hide

Isoform 2 [UniParc].

Checksum: 8CBBD18CA1EB3243
Show »

FASTA60265,482
Isoform 3 [UniParc].

Checksum: 6C379F47ACC90136
Show »

FASTA43647,717
Isoform 4 [UniParc].

Checksum: 93716FBA60085245
Show »

FASTA54459,505

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney and Thalamus.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Testis.
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
[5]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-647 (ISOFORM 4).
Tissue: Kidney and Urinary bladder.
[7]"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-647 (ISOFORMS 1/2).
Tissue: Brain.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-471; SER-523 AND SER-525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC."
McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M., Johansen T., Tooze S.A.
EMBO J. 31:1931-1946(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-475.
[18]"WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
Zhang F., Yu X.
Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF20; RNF40 AND UBE2A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK055852 mRNA. Translation: BAB71029.1.
AK223600 mRNA. Translation: BAD97320.1.
AK290174 mRNA. Translation: BAF82863.1.
AL713727 mRNA. Translation: CAD28517.1.
AL358234, AL161936 Genomic DNA. Translation: CAH70766.1.
AL358234, AL161936 Genomic DNA. Translation: CAH70768.1.
AL161936, AL358234 Genomic DNA. Translation: CAI40922.1.
AL161936, AL358234 Genomic DNA. Translation: CAI40924.1.
AL161936 Genomic DNA. Translation: CAI40921.1. Sequence problems.
AL358234, AL161936 Genomic DNA. Translation: CAH70767.1. Sequence problems.
AL161936, AL358234 Genomic DNA. Translation: CAI40923.1. Sequence problems.
CH471072 Genomic DNA. Translation: EAW86032.1.
CH471072 Genomic DNA. Translation: EAW86035.1.
CH471072 Genomic DNA. Translation: EAW86037.1.
CH471072 Genomic DNA. Translation: EAW86039.1.
CH471072 Genomic DNA. Translation: EAW86040.1.
CH471072 Genomic DNA. Translation: EAW86042.1.
BC004258 mRNA. Translation: AAH04258.2. Frameshift.
BC010356 mRNA. Translation: AAH10356.1. Different initiation.
AB058747 mRNA. Translation: BAB47473.1. Sequence problems.
CCDSCCDS7159.1. [Q9BTA9-1]
CCDS7160.1. [Q9BTA9-5]
RefSeqNP_057712.2. NM_016628.4. [Q9BTA9-1]
NP_567823.1. NM_100486.3. [Q9BTA9-5]
XP_005252514.1. XM_005252457.1. [Q9BTA9-2]
UniGeneHs.743224.

3D structure databases

ProteinModelPortalQ9BTA9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119473. 15 interactions.
IntActQ9BTA9. 11 interactions.
MINTMINT-2873194.

PTM databases

PhosphoSiteQ9BTA9.

Polymorphism databases

DMDM117949358.

Proteomic databases

MaxQBQ9BTA9.
PaxDbQ9BTA9.
PRIDEQ9BTA9.

Protocols and materials databases

DNASU51322.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347934; ENSP00000311106; ENSG00000095787. [Q9BTA9-5]
ENST00000354911; ENSP00000346986; ENSG00000095787. [Q9BTA9-1]
ENST00000375664; ENSP00000364816; ENSG00000095787. [Q9BTA9-2]
ENST00000428935; ENSP00000399706; ENSG00000095787. [Q9BTA9-3]
ENST00000439676; ENSP00000415727; ENSG00000095787. [Q9BTA9-3]
GeneID51322.
KEGGhsa:51322.
UCSCuc001iud.3. human. [Q9BTA9-1]
uc001iue.3. human. [Q9BTA9-5]

Organism-specific databases

CTD51322.
GeneCardsGC10P028861.
HGNCHGNC:17327. WAC.
HPAHPA036528.
HPA042609.
MIM615049. gene.
neXtProtNX_Q9BTA9.
PharmGKBPA134978936.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299824.
HOVERGENHBG057585.
InParanoidQ9BTA9.
OMAHKILTAG.
OrthoDBEOG7T1RB9.
PhylomeDBQ9BTA9.
TreeFamTF328635.

Enzyme and pathway databases

SignaLinkQ9BTA9.

Gene expression databases

ArrayExpressQ9BTA9.
BgeeQ9BTA9.
CleanExHS_WAC.
GenevestigatorQ9BTA9.

Family and domain databases

InterProIPR001202. WW_dom.
[Graphical view]
PfamPF00397. WW. 1 hit.
[Graphical view]
SMARTSM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWAC. human.
GeneWikiWAC_(gene).
GenomeRNAi51322.
NextBio54714.
PROQ9BTA9.
SOURCESearch...

Entry information

Entry nameWAC_HUMAN
AccessionPrimary (citable) accession number: Q9BTA9
Secondary accession number(s): A8K2A9 expand/collapse secondary AC list , C9JBT9, D3DRW5, D3DRW6, D3DRW7, Q53EN9, Q5JU75, Q5JU77, Q5VXK0, Q5VXK2, Q8TCK1, Q96DP3, Q96FW6, Q96JI3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 105 of the entry and version 3 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.

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