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Q9BTA9

- WAC_HUMAN

UniProt

Q9BTA9 - WAC_HUMAN

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Protein

WW domain-containing adapter protein with coiled-coil

Gene

WAC

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. RNA polymerase II core binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. G1 DNA damage checkpoint Source: UniProtKB
  3. histone H2B conserved C-terminal lysine ubiquitination Source: UniProtKB
  4. histone monoubiquitination Source: UniProtKB
  5. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  6. positive regulation of macroautophagy Source: BHF-UCL
  7. positive regulation of transcription, DNA-templated Source: UniProtKB
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiQ9BTA9.

Names & Taxonomyi

Protein namesi
Recommended name:
WW domain-containing adapter protein with coiled-coil
Gene namesi
Name:WAC
Synonyms:KIAA1844
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17327. WAC.

Subcellular locationi

Nucleus speckle By similarity. Nucleus 1 Publication
Note: In distinct nuclear speckles. Colocalizes with pre-mRNA processing complexes (By similarity).By similarity

GO - Cellular componenti

  1. nucleus Source: BHF-UCL
  2. spliceosomal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134978936.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 647647WW domain-containing adapter protein with coiled-coilPRO_0000254558Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531Phosphoserine2 Publications
Modified residuei293 – 2931Phosphothreonine1 Publication
Modified residuei302 – 3021N6-acetyllysine1 Publication
Modified residuei471 – 4711Phosphothreonine1 Publication
Modified residuei511 – 5111Phosphoserine1 Publication
Modified residuei523 – 5231Phosphoserine1 Publication
Modified residuei525 – 5251Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BTA9.
PaxDbiQ9BTA9.
PRIDEiQ9BTA9.

PTM databases

PhosphoSiteiQ9BTA9.

Expressioni

Gene expression databases

BgeeiQ9BTA9.
CleanExiHS_WAC.
ExpressionAtlasiQ9BTA9. baseline and differential.
GenevestigatoriQ9BTA9.

Organism-specific databases

HPAiHPA036528.
HPA042609.

Interactioni

Subunit structurei

Interacts (via coiled coil domain) with RNF20, RNF40 and UBE2A. Interacts (via WW domain) with RNA polymerase II.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428585EBI-749118,EBI-466029

Protein-protein interaction databases

BioGridi119473. 18 interactions.
IntActiQ9BTA9. 12 interactions.
MINTiMINT-2873194.

Structurei

3D structure databases

ProteinModelPortaliQ9BTA9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 16234WWPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili618 – 64427Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG299824.
GeneTreeiENSGT00440000037780.
HOVERGENiHBG057585.
InParanoidiQ9BTA9.
OMAiHKILTAG.
OrthoDBiEOG7T1RB9.
PhylomeDBiQ9BTA9.
TreeFamiTF328635.

Family and domain databases

InterProiIPR001202. WW_dom.
[Graphical view]
PfamiPF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BTA9-1) [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

        10         20         30         40         50
MVMYARKQQR LSDGCHDRRG DSQPYQALKY SSKSHPSSGD HRHEKMRDAG
60 70 80 90 100
DPSPPNKMLR RSDSPENKYS DSTGHSKAKN VHTHRVRERD GGTSYSPQEN
110 120 130 140 150
SHNHSALHSS NSHSSNPSNN PSKTSDAPYD SADDWSEHIS SSGKKYYYNC
160 170 180 190 200
RTEVSQWEKP KEWLEREQRQ KEANKMAVNS FPKDRDYRRE VMQATATSGF
210 220 230 240 250
ASGMEDKHSS DASSLLPQNI LSQTSRHNDR DYRLPRAETH SSSTPVQHPI
260 270 280 290 300
KPVVHPTATP STVPSSPFTL QSDHQPKKSF DANGASTLSK LPTPTSSVPA
310 320 330 340 350
QKTERKESTS GDKPVSHSCT TPSTSSASGL NPTSAPPTSA SAVPVSPVPQ
360 370 380 390 400
SPIPPLLQDP NLLRQLLPAL QATLQLNNSN VDISKINEVL TAAVTQASLQ
410 420 430 440 450
SIIHKFLTAG PSAFNITSLI SQAAQLSTQA QPSNQSPMSL TSDASSPRSY
460 470 480 490 500
VSPRISTPQT NTVPIKPLIS TPPVSSQPKV STPVVKQGPV SQSATQQPVT
510 520 530 540 550
ADKQQGHEPV SPRSLQRSSS QRSPSPGPNH TSNSSNASNA TVVPQNSSAR
560 570 580 590 600
STCSLTPALA AHFSENLIKH VQGWPADHAE KQASRLREEA HNMGTIHMSE
610 620 630 640
ICTELKNLRS LVRVCEIQAT LREQRILFLR QQIKELEKLK NQNSFMV
Length:647
Mass (Da):70,724
Last modified:October 31, 2006 - v3
Checksum:i15C32DAAA3A94129
GO
Isoform 2 (identifier: Q9BTA9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Show »
Length:602
Mass (Da):65,482
Checksum:i8CBBD18CA1EB3243
GO
Isoform 3 (identifier: Q9BTA9-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:436
Mass (Da):47,717
Checksum:i6C379F47ACC90136
GO
Isoform 4 (identifier: Q9BTA9-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:544
Mass (Da):59,505
Checksum:i93716FBA60085245
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti426 – 4261L → F in BAB71029. (PubMed:14702039)Curated
Sequence conflicti581 – 5811K → R in AAH10356. (PubMed:15489334)Curated
Sequence conflicti599 – 5991S → P in BAD97320. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti242 – 2421S → R.
Corresponds to variant rs11595926 [ dbSNP | Ensembl ].
VAR_028838
Natural varianti309 – 3091T → A.
Corresponds to variant rs2232791 [ dbSNP | Ensembl ].
VAR_053448
Natural varianti475 – 4751S → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036351
Natural varianti531 – 5311T → S.
Corresponds to variant rs7127 [ dbSNP | Ensembl ].
VAR_028839

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4545Missing in isoform 2 and isoform 3. 2 PublicationsVSP_021230Add
BLAST
Alternative sequencei204 – 307104MEDKH…TERKE → K in isoform 4. 1 PublicationVSP_021231Add
BLAST
Alternative sequencei430 – 48152AQPSN…QPKVS → DIPLHEGIQMERDTHRSKWE VKGSLCQKADKQQECLVWNG SIMVQRLLQPSG in isoform 3. 1 PublicationVSP_021233Add
BLAST
Alternative sequencei482 – 647166Missing in isoform 3. 1 PublicationVSP_021236Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7159.1. [Q9BTA9-1]
CCDS7160.1. [Q9BTA9-5]
CCDS7161.1. [Q9BTA9-2]
RefSeqiNP_057712.2. NM_016628.4. [Q9BTA9-1]
NP_567822.1. NM_100264.2. [Q9BTA9-2]
NP_567823.1. NM_100486.3. [Q9BTA9-5]
UniGeneiHs.743224.

Genome annotation databases

EnsembliENST00000347934; ENSP00000311106; ENSG00000095787. [Q9BTA9-5]
ENST00000354911; ENSP00000346986; ENSG00000095787. [Q9BTA9-1]
ENST00000375664; ENSP00000364816; ENSG00000095787. [Q9BTA9-2]
ENST00000439676; ENSP00000415727; ENSG00000095787. [Q9BTA9-3]
GeneIDi51322.
KEGGihsa:51322.
UCSCiuc001iud.3. human. [Q9BTA9-1]
uc001iue.3. human. [Q9BTA9-5]

Polymorphism databases

DMDMi117949358.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS7159.1. [Q9BTA9-1 ]
CCDS7160.1. [Q9BTA9-5 ]
CCDS7161.1. [Q9BTA9-2 ]
RefSeqi NP_057712.2. NM_016628.4. [Q9BTA9-1 ]
NP_567822.1. NM_100264.2. [Q9BTA9-2 ]
NP_567823.1. NM_100486.3. [Q9BTA9-5 ]
UniGenei Hs.743224.

3D structure databases

ProteinModelPortali Q9BTA9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119473. 18 interactions.
IntActi Q9BTA9. 12 interactions.
MINTi MINT-2873194.

PTM databases

PhosphoSitei Q9BTA9.

Polymorphism databases

DMDMi 117949358.

Proteomic databases

MaxQBi Q9BTA9.
PaxDbi Q9BTA9.
PRIDEi Q9BTA9.

Protocols and materials databases

DNASUi 51322.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000347934 ; ENSP00000311106 ; ENSG00000095787 . [Q9BTA9-5 ]
ENST00000354911 ; ENSP00000346986 ; ENSG00000095787 . [Q9BTA9-1 ]
ENST00000375664 ; ENSP00000364816 ; ENSG00000095787 . [Q9BTA9-2 ]
ENST00000439676 ; ENSP00000415727 ; ENSG00000095787 . [Q9BTA9-3 ]
GeneIDi 51322.
KEGGi hsa:51322.
UCSCi uc001iud.3. human. [Q9BTA9-1 ]
uc001iue.3. human. [Q9BTA9-5 ]

Organism-specific databases

CTDi 51322.
GeneCardsi GC10P028861.
HGNCi HGNC:17327. WAC.
HPAi HPA036528.
HPA042609.
MIMi 615049. gene.
neXtProti NX_Q9BTA9.
PharmGKBi PA134978936.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG299824.
GeneTreei ENSGT00440000037780.
HOVERGENi HBG057585.
InParanoidi Q9BTA9.
OMAi HKILTAG.
OrthoDBi EOG7T1RB9.
PhylomeDBi Q9BTA9.
TreeFami TF328635.

Enzyme and pathway databases

SignaLinki Q9BTA9.

Miscellaneous databases

ChiTaRSi WAC. human.
GeneWikii WAC_(gene).
GenomeRNAii 51322.
NextBioi 54714.
PROi Q9BTA9.
SOURCEi Search...

Gene expression databases

Bgeei Q9BTA9.
CleanExi HS_WAC.
ExpressionAtlasi Q9BTA9. baseline and differential.
Genevestigatori Q9BTA9.

Family and domain databases

InterProi IPR001202. WW_dom.
[Graphical view ]
Pfami PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiWAC_HUMAN
AccessioniPrimary (citable) accession number: Q9BTA9
Secondary accession number(s): A8K2A9
, C9JBT9, D3DRW5, D3DRW6, D3DRW7, Q53EN9, Q5JU75, Q5JU77, Q5VXK0, Q5VXK2, Q8TCK1, Q96DP3, Q96FW6, Q96JI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: October 29, 2014
This is version 108 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3