WAP53_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: WAP53_HUMAN
• UniProt AC: Q9BUR4
• Protein Name: Telomerase Cajal body protein 1
• Gene Name: WRAP53
• Organism: Homo sapiens (Human).
• Sequence Length: 548
• Subcellular Localization: Nucleus, Cajal body. Cytoplasm.
• Protein Description: 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..
• Protein Sequence: MKTLETQPLAPDCCPSDQDPAPAHPSPHASPMNKNADSELMPPPPERGDPPRLSPDPVAGSAVSQELREGDPVSLSTPLETEFGSPSELSPRIEEQELSENTSLPAEEANGSLSEEEANGPELGSGKAMEDTSGEPAAEDEGDTAWNYSFSQLPRFLSGSWSEFSTQPENFLKGCKWAPDGSCILTNSADNILRIYNLPPELYHEGEQVEYAEMVPVLRMVEGDTIYDYCWYSLMSSAQPDTSYVASSSRENPIHIWDAFTGELRASFRAYNHLDELTAAHSLCFSPDGSQLFCGFNRTVRVFSTARPGRDCEVRATFAKKQGQSGIISCIAFSPAQPLYACGSYGRSLGLYAWDDGSPLALLGGHQGGITHLCFHPDGNRFFSGARKDAELLCWDLRQSGYPLWSLGREVTTNQRIYFDLDPTGQFLVSGSTSGAVSVWDTDGPGNDGKPEPVLSFLPQKDCTNGVSLHPSLPLLATASGQRVFPEPTESGDEGEELGLPLLSTRHVHLECRLQLWWCGGAPDSSIPDDHQGEKGQGGTEGGVGELI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MKTLETQPL ------CCCCCCCCC	62.91	25953088

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
64	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of WAP53_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of WAP53_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XPC_HUMAN	XPC	physical	22939629
WAPL_HUMAN	WAPAL	physical	22939629
MDC1_HUMAN	MDC1	physical	25512560
RNF8_HUMAN	RNF8	physical	25512560
H2AX_HUMAN	H2AFX	physical	25512560
HNRPU_HUMAN	HNRNPU	physical	26344197
ZFHX3_HUMAN	ZFHX3	physical	26496610
TCPZ_HUMAN	CCT6A	physical	26496610
DKC1_HUMAN	DKC1	physical	26496610
MYBPH_HUMAN	MYBPH	physical	26496610
NDUV3_HUMAN	NDUFV3	physical	26496610
TCPA_HUMAN	TCP1	physical	26496610
TCPG_HUMAN	CCT3	physical	26496610
STK24_HUMAN	STK24	physical	26496610
TCPH_HUMAN	CCT7	physical	26496610
TCPD_HUMAN	CCT4	physical	26496610
TCPB_HUMAN	CCT2	physical	26496610
TCPQ_HUMAN	CCT8	physical	26496610
TCPE_HUMAN	CCT5	physical	26496610
GAR1_HUMAN	GAR1	physical	26496610
PR38B_HUMAN	PRPF38B	physical	26496610
RM14_HUMAN	MRPL14	physical	26496610
H2AX_HUMAN	H2AFX	physical	26734725
MDC1_HUMAN	MDC1	physical	26734725
RNF8_HUMAN	RNF8	physical	26734725
DKC1_HUMAN	DKC1	physical	25416818

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 613988: Dyskeratosis congenita, autosomal recessive, 3 (DKCB3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-30; SER-85;SER-90; SER-112; SER-114; THR-489 AND SER-491, AND MASS SPECTROMETRY.
PubMed: 19690332

"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).
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, AND MASSSPECTROMETRY.
PubMed: 18669648

"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-491, AND MASSSPECTROMETRY.
PubMed: 18220336

"ATM and ATR substrate analysis reveals extensive protein networksresponsive 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.
PubMed: 17525332

"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASSSPECTROMETRY.
PubMed: 17693683

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-85 AND SER-90,AND MASS SPECTROMETRY.
PubMed: 17081983