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Protein

Telomerase Cajal body protein 1

Gene

WRAP53

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

Functioni

Essential component of the telomerase holoenzyme complex, a ribonucleoprotein complex essential for the replication of chromosome termini that elongates telomeres in most eukaryotes. In the telomerase holoenzyme complex, it controls telomerase localization to Cajal body. Required for delivery of TERC to telomeres during S phase and for telomerase activity. Binds small Cajal body RNAs (scaRNAs). The mRNA encoding this protein plays a critical role in the regulation of p53 expression at the post-transcriptional level; it is involved both in maintaining basal p53 mRNA levels and in p53 induction upon DNA damage.2 Publications

GO - Molecular functioni

  • RNA binding Source: UniProtKB

GO - Biological processi

  • positive regulation of telomerase activity Source: UniProtKB
  • telomere formation via telomerase Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_7974. Telomere Extension By Telomerase.
SignaLinkiQ9BUR4.

Names & Taxonomyi

Protein namesi
Recommended name:
Telomerase Cajal body protein 1
Alternative name(s):
WD repeat-containing protein 79
WD repeat-containing protein WRAP53
WD40 repeat-containing protein antisense to TP53 gene
Gene namesi
Name:WRAP53
Synonyms:TCAB1, WDR79
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:25522. WRAP53.

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • telomerase holoenzyme complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Dyskeratosis congenita, autosomal recessive, 3 (DKCB3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.

See also OMIM:613988
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641F → L in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065873
Natural varianti376 – 3761H → Y in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065874
Natural varianti398 – 3981R → W in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065875
Natural varianti435 – 4351G → R in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065876

Keywords - Diseasei

Disease mutation, Dyskeratosis congenita

Organism-specific databases

MIMi613988. phenotype.
Orphaneti1775. Dyskeratosis congenita.
PharmGKBiPA164727568.

Polymorphism and mutation databases

BioMutaiWRAP53.
DMDMi74761275.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Telomerase Cajal body protein 1PRO_0000242696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphoserine2 Publications
Modified residuei30 – 301Phosphoserine2 Publications
Modified residuei54 – 541Phosphoserine4 Publications
Modified residuei85 – 851Phosphoserine3 Publications
Modified residuei90 – 901Phosphoserine5 Publications
Modified residuei112 – 1121Phosphoserine2 Publications
Modified residuei114 – 1141Phosphoserine2 Publications
Modified residuei489 – 4891Phosphothreonine2 Publications
Modified residuei491 – 4911Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BUR4.
PaxDbiQ9BUR4.
PeptideAtlasiQ9BUR4.
PRIDEiQ9BUR4.

PTM databases

PhosphoSiteiQ9BUR4.

Expressioni

Tissue specificityi

Expressed in all tissues and cell lines examined.1 Publication

Gene expression databases

BgeeiQ9BUR4.
CleanExiHS_WDR79.
ExpressionAtlasiQ9BUR4. baseline and differential.
GenevisibleiQ9BUR4. HS.

Organism-specific databases

HPAiHPA023026.
HPA028130.
HPA029928.

Interactioni

Subunit structurei

Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC).1 Publication

Protein-protein interaction databases

BioGridi120440. 13 interactions.
DIPiDIP-56796N.
IntActiQ9BUR4. 3 interactions.
STRINGi9606.ENSP00000324203.

Structurei

3D structure databases

ProteinModelPortaliQ9BUR4.
SMRiQ9BUR4. Positions 137-483.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati167 – 20640WD 1Add
BLAST
Repeati222 – 26746WD 2Add
BLAST
Repeati272 – 31342WD 3Add
BLAST
Repeati323 – 36442WD 4Add
BLAST
Repeati365 – 40541WD 5Add
BLAST
Repeati411 – 45040WD 6Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 5750Pro-richAdd
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000010169.
HOGENOMiHOG000030352.
HOVERGENiHBG098609.
InParanoidiQ9BUR4.
OMAiEYAEMVP.
OrthoDBiEOG7FNC74.
PhylomeDBiQ9BUR4.
TreeFamiTF315169.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BUR4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLETQPLA PDCCPSDQDP APAHPSPHAS PMNKNADSEL MPPPPERGDP
60 70 80 90 100
PRLSPDPVAG SAVSQELREG DPVSLSTPLE TEFGSPSELS PRIEEQELSE
110 120 130 140 150
NTSLPAEEAN GSLSEEEANG PELGSGKAME DTSGEPAAED EGDTAWNYSF
160 170 180 190 200
SQLPRFLSGS WSEFSTQPEN FLKGCKWAPD GSCILTNSAD NILRIYNLPP
210 220 230 240 250
ELYHEGEQVE YAEMVPVLRM VEGDTIYDYC WYSLMSSAQP DTSYVASSSR
260 270 280 290 300
ENPIHIWDAF TGELRASFRA YNHLDELTAA HSLCFSPDGS QLFCGFNRTV
310 320 330 340 350
RVFSTARPGR DCEVRATFAK KQGQSGIISC IAFSPAQPLY ACGSYGRSLG
360 370 380 390 400
LYAWDDGSPL ALLGGHQGGI THLCFHPDGN RFFSGARKDA ELLCWDLRQS
410 420 430 440 450
GYPLWSLGRE VTTNQRIYFD LDPTGQFLVS GSTSGAVSVW DTDGPGNDGK
460 470 480 490 500
PEPVLSFLPQ KDCTNGVSLH PSLPLLATAS GQRVFPEPTE SGDEGEELGL
510 520 530 540
PLLSTRHVHL ECRLQLWWCG GAPDSSIPDD HQGEKGQGGT EGGVGELI
Length:548
Mass (Da):59,309
Last modified:June 1, 2001 - v1
Checksum:i4687517268A813B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211A → V in BAA91579 (PubMed:14702039).Curated
Sequence conflicti497 – 4971E → G in BAG51781 (PubMed:14702039).Curated
Sequence conflicti526 – 5261S → G in BAG51781 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111P → S.
Corresponds to variant rs17880282 [ dbSNP | Ensembl ].
VAR_026865
Natural varianti68 – 681R → G.2 Publications
Corresponds to variant rs2287499 [ dbSNP | Ensembl ].
VAR_026866
Natural varianti136 – 1361P → R.
Corresponds to variant rs34067256 [ dbSNP | Ensembl ].
VAR_057618
Natural varianti164 – 1641F → L in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065873
Natural varianti187 – 1871N → T.
Corresponds to variant rs35762939 [ dbSNP | Ensembl ].
VAR_057619
Natural varianti376 – 3761H → Y in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065874
Natural varianti398 – 3981R → W in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065875
Natural varianti435 – 4351G → R in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. 1 Publication
VAR_065876
Natural varianti494 – 4941E → Q.
Corresponds to variant rs35123152 [ dbSNP | Ensembl ].
VAR_057620
Natural varianti522 – 5221A → G.1 Publication
Corresponds to variant rs7640 [ dbSNP | Ensembl ].
VAR_026867

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY766322 mRNA. Translation: AAW92115.1.
DQ431240 mRNA. Translation: ABD92817.1.
DQ431241 mRNA. Translation: ABD92818.1.
AK001247 mRNA. Translation: BAA91579.1.
AK056669 mRNA. Translation: BAG51781.1.
CH471108 Genomic DNA. Translation: EAW90136.1.
CH471108 Genomic DNA. Translation: EAW90138.1.
CH471108 Genomic DNA. Translation: EAW90139.1.
BC002336 mRNA. Translation: AAH02336.1.
CCDSiCCDS11119.1.
RefSeqiNP_001137462.1. NM_001143990.1.
NP_001137463.1. NM_001143991.1.
NP_001137464.1. NM_001143992.1.
NP_060551.2. NM_018081.2.
UniGeneiHs.408312.

Genome annotation databases

EnsembliENST00000316024; ENSP00000324203; ENSG00000141499.
ENST00000396463; ENSP00000379727; ENSG00000141499.
ENST00000431639; ENSP00000397219; ENSG00000141499.
ENST00000457584; ENSP00000411061; ENSG00000141499.
GeneIDi55135.
KEGGihsa:55135.
UCSCiuc002gip.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY766322 mRNA. Translation: AAW92115.1.
DQ431240 mRNA. Translation: ABD92817.1.
DQ431241 mRNA. Translation: ABD92818.1.
AK001247 mRNA. Translation: BAA91579.1.
AK056669 mRNA. Translation: BAG51781.1.
CH471108 Genomic DNA. Translation: EAW90136.1.
CH471108 Genomic DNA. Translation: EAW90138.1.
CH471108 Genomic DNA. Translation: EAW90139.1.
BC002336 mRNA. Translation: AAH02336.1.
CCDSiCCDS11119.1.
RefSeqiNP_001137462.1. NM_001143990.1.
NP_001137463.1. NM_001143991.1.
NP_001137464.1. NM_001143992.1.
NP_060551.2. NM_018081.2.
UniGeneiHs.408312.

3D structure databases

ProteinModelPortaliQ9BUR4.
SMRiQ9BUR4. Positions 137-483.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120440. 13 interactions.
DIPiDIP-56796N.
IntActiQ9BUR4. 3 interactions.
STRINGi9606.ENSP00000324203.

PTM databases

PhosphoSiteiQ9BUR4.

Polymorphism and mutation databases

BioMutaiWRAP53.
DMDMi74761275.

Proteomic databases

MaxQBiQ9BUR4.
PaxDbiQ9BUR4.
PeptideAtlasiQ9BUR4.
PRIDEiQ9BUR4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316024; ENSP00000324203; ENSG00000141499.
ENST00000396463; ENSP00000379727; ENSG00000141499.
ENST00000431639; ENSP00000397219; ENSG00000141499.
ENST00000457584; ENSP00000411061; ENSG00000141499.
GeneIDi55135.
KEGGihsa:55135.
UCSCiuc002gip.3. human.

Organism-specific databases

CTDi55135.
GeneCardsiGC17P007589.
GeneReviewsiWRAP53.
HGNCiHGNC:25522. WRAP53.
HPAiHPA023026.
HPA028130.
HPA029928.
MIMi612661. gene.
613988. phenotype.
neXtProtiNX_Q9BUR4.
Orphaneti1775. Dyskeratosis congenita.
PharmGKBiPA164727568.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000010169.
HOGENOMiHOG000030352.
HOVERGENiHBG098609.
InParanoidiQ9BUR4.
OMAiEYAEMVP.
OrthoDBiEOG7FNC74.
PhylomeDBiQ9BUR4.
TreeFamiTF315169.

Enzyme and pathway databases

ReactomeiREACT_7974. Telomere Extension By Telomerase.
SignaLinkiQ9BUR4.

Miscellaneous databases

GenomeRNAii55135.
NextBioi58818.
PROiQ9BUR4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BUR4.
CleanExiHS_WDR79.
ExpressionAtlasiQ9BUR4. baseline and differential.
GenevisibleiQ9BUR4. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Endogenous p53 antisense transcript Wrap53 is required for p53 stabilization upon DNA damage."
    Hammarsund M.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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].
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-68.
  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].
    Tissue: Kidney.
  5. "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-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-54; SER-85; SER-90; SER-112; SER-114; THR-489 AND SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "Wrap53, a natural p53 antisense transcript required for p53 induction upon DNA damage."
    Mahmoudi S., Henriksson S., Corcoran M., Mendez-Vidal C., Wiman K.G., Farnebo M.
    Mol. Cell 33:462-471(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
  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 SER-85; SER-90; SER-112; SER-114; THR-489 AND SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
    Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
    Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX, RNA-BINDING.
  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-26; SER-30; SER-90 AND SER-491, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-85 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Disruption of telomerase trafficking by TCAB1 mutation causes dyskeratosis congenita."
    Zhong F., Savage S.A., Shkreli M., Giri N., Jessop L., Myers T., Chen R., Alter B.P., Artandi S.E.
    Genes Dev. 25:11-16(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DKCB3 LEU-164; TYR-376; TRP-398 AND ARG-435, VARIANTS GLY-68 AND GLY-522, CHARACTERIZATION OF VARIANTS DKCB3 LEU-164; TYR-376; TRP-398 AND ARG-435.

Entry informationi

Entry nameiWAP53_HUMAN
AccessioniPrimary (citable) accession number: Q9BUR4
Secondary accession number(s): B3KPR9
, D3DTQ4, Q08ET9, Q9NW09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 124 of the entry and version 1 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 17
    Human chromosome 17: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.