Q9BUR4 (WAP53_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Telomerase Cajal body protein 1

Alternative name(s):
WD repeat-containing protein 79
WD40 repeat-containing protein encoding RNA antisense to p53

Gene names

Name:	WRAP53
Synonyms:	TCAB1, WDR79

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	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.12
Subunit structure	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). Ref.12
Subcellular location	Nucleus › Cajal body. Cytoplasm Ref.10 Ref.12.
Tissue specificity	Expressed in all tissues and cell lines examined. Ref.10
Involvement in disease	Dyskeratosis congenita, autosomal recessive, 3 (DKCB3) [MIM:613988]: A 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15
Sequence similarities	Contains 6 WD repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dyskeratosis congenita
Domain	Repeat WD repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of telomerase activity Inferred from direct assay Ref.12. Source: UniProtKB telomere formation via telomerase Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular_component	Cajal body Inferred from direct assay Ref.12. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA telomerase holoenzyme complex Inferred from direct assay Ref.12. Source: UniProtKB
Molecular_function	RNA binding Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 548	548	Telomerase Cajal body protein 1		PRO_0000242696
Regions
	Repeat	167 – 206	40	WD 1
	Repeat	222 – 267	46	WD 2
	Repeat	272 – 313	42	WD 3
	Repeat	323 – 364	42	WD 4
	Repeat	365 – 405	41	WD 5
	Repeat	411 – 450	40	WD 6
	Compositional bias	8 – 57	50	Pro-rich
Amino acid modifications
	Modified residue	26	1	Phosphoserine Ref.9 Ref.13
	Modified residue	30	1	Phosphoserine Ref.9 Ref.13
	Modified residue	54	1	Phosphoserine Ref.5 Ref.8 Ref.9
	Modified residue	85	1	Phosphoserine Ref.9 Ref.11
	Modified residue	90	1	Phosphoserine Ref.6 Ref.9 Ref.11 Ref.13
	Modified residue	112	1	Phosphoserine Ref.9 Ref.11
	Modified residue	114	1	Phosphoserine Ref.9 Ref.11
	Modified residue	489	1	Phosphothreonine Ref.9 Ref.11
	Modified residue	491	1	Phosphoserine Ref.9 Ref.11 Ref.13 Ref.14
Natural variations
	Natural variant	11	1	P → S. Corresponds to variant rs17880282 [ dbSNP | Ensembl ].		VAR_026865
	Natural variant	68	1	R → G. Ref.3 Ref.15 Corresponds to variant rs2287499 [ dbSNP | Ensembl ].		VAR_026866
	Natural variant	136	1	P → R. Corresponds to variant rs34067256 [ dbSNP | Ensembl ].		VAR_057618
	Natural variant	164	1	F → L in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. Ref.15		VAR_065873
	Natural variant	187	1	N → T. Corresponds to variant rs35762939 [ dbSNP | Ensembl ].		VAR_057619
	Natural variant	376	1	H → Y in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. Ref.15		VAR_065874
	Natural variant	398	1	R → W in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. Ref.15		VAR_065875
	Natural variant	435	1	G → R in DKCB3; disrupts telomerase localization to Cajal bodies resulting in misdirection of telomerase RNA to nucleoli. Ref.15		VAR_065876
	Natural variant	494	1	E → Q. Corresponds to variant rs35123152 [ dbSNP | Ensembl ].		VAR_057620
	Natural variant	522	1	A → G. Ref.15 Corresponds to variant rs7640 [ dbSNP | Ensembl ].		VAR_026867
Experimental info
	Sequence conflict	21	1	A → V in BAA91579. Ref.2
	Sequence conflict	497	1	E → G in BAG51781. Ref.2
	Sequence conflict	526	1	S → G in BAG51781. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9BUR4 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 4687517268A813B5	FASTA	548	59,309
	10 20 30 40 50 60 MKTLETQPLA PDCCPSDQDP APAHPSPHAS PMNKNADSEL MPPPPERGDP PRLSPDPVAG 70 80 90 100 110 120 SAVSQELREG DPVSLSTPLE TEFGSPSELS PRIEEQELSE NTSLPAEEAN GSLSEEEANG 130 140 150 160 170 180 PELGSGKAME DTSGEPAAED EGDTAWNYSF SQLPRFLSGS WSEFSTQPEN FLKGCKWAPD 190 200 210 220 230 240 GSCILTNSAD NILRIYNLPP ELYHEGEQVE YAEMVPVLRM VEGDTIYDYC WYSLMSSAQP 250 260 270 280 290 300 DTSYVASSSR ENPIHIWDAF TGELRASFRA YNHLDELTAA HSLCFSPDGS QLFCGFNRTV 310 320 330 340 350 360 RVFSTARPGR DCEVRATFAK KQGQSGIISC IAFSPAQPLY ACGSYGRSLG LYAWDDGSPL 370 380 390 400 410 420 ALLGGHQGGI THLCFHPDGN RFFSGARKDA ELLCWDLRQS GYPLWSLGRE VTTNQRIYFD 430 440 450 460 470 480 LDPTGQFLVS GSTSGAVSVW DTDGPGNDGK PEPVLSFLPQ KDCTNGVSLH PSLPLLATAS 490 500 510 520 530 540 GQRVFPEPTE SGDEGEELGL PLLSTRHVHL ECRLQLWWCG GAPDSSIPDD HQGEKGQGGT EGGVGELI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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. , 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], 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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 SER-26; SER-30; SER-54; SER-85; SER-90; SER-112; SER-114; THR-489 AND SER-491, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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, MASS SPECTROMETRY.
[15]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00306087.
RefSeq	NP_001137462.1. NM_001143990.1. NP_001137463.1. NM_001143991.1. NP_001137464.1. NM_001143992.1. NP_060551.2. NM_018081.2.
UniGene	Hs.408312.
3D structure databases
ProteinModelPortal	Q9BUR4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-56796N.
IntAct	Q9BUR4. 1 interaction.
STRING	9606.ENSP00000324203.
PTM databases
PhosphoSite	Q9BUR4.
Polymorphism databases
DMDM	74761275.
Proteomic databases
PaxDb	Q9BUR4.
PeptideAtlas	Q9BUR4.
PRIDE	Q9BUR4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000316024; ENSP00000324203; ENSG00000141499. ENST00000396463; ENSP00000379727; ENSG00000141499. ENST00000431639; ENSP00000397219; ENSG00000141499. ENST00000457584; ENSP00000411061; ENSG00000141499.
GeneID	55135.
KEGG	hsa:55135.
UCSC	uc002gip.3. human.
Organism-specific databases
CTD	55135.
GeneCards	GC17P007589.
HGNC	HGNC:25522. WRAP53.
HPA	HPA023026. HPA028130.
MIM	612661. gene. 613988. phenotype.
neXtProt	NX_Q9BUR4.
PharmGKB	PA164727568.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000030352.
HOVERGEN	HBG098609.
InParanoid	Q9BUR4.
OMA	EYAEMVP.
OrthoDB	EOG4N5VWP.
PhylomeDB	Q9BUR4.
Gene expression databases
ArrayExpress	Q9BUR4.
Bgee	Q9BUR4.
CleanEx	HS_WDR79.
Genevestigator	Q9BUR4.
GermOnline	ENSG00000141499. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 2 hits.
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF00400. WD40. 4 hits. [Graphical view]
SMART	SM00320. WD40. 5 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. 2 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55135.
NextBio	58818.
SOURCE	Search...

Entry information

Entry name

WAP53_HUMAN

Accession

Primary (citable) accession number: Q9BUR4
Secondary accession number(s): B3KPR9 , D3DTQ4, Q08ET9, Q9NW09

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 103 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.