UT14A_HUMAN - dbPTM
UT14A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UT14A_HUMAN
UniProt AC Q9BVJ6
Protein Name U3 small nucleolar RNA-associated protein 14 homolog A
Gene Name UTP14A
Organism Homo sapiens (Human).
Sequence Length 771
Subcellular Localization Nucleus, nucleolus .
Protein Description May be required for ribosome biogenesis..
Protein Sequence MTANRLAESLLALSQQEELADLPKDYLLSESEDEGDNDGERKHQKLLEAISSLDGKNRRKLAERSEASLKVSEFNVSSEGSGEKLVLADLLEPVKTSSSLATVKKQLSRVKSKKTVELPLNKEEIERIHREVAFNKTAQVLSKWDPVVLKNRQAEQLVFPLEKEEPAIAPIEHVLSGWKARTPLEQEIFNLLHKNKQPVTDPLLTPVEKASLRAMSLEEAKMRRAELQRARALQSYYEAKARREKKIKSKKYHKVVKKGKAKKALKEFEQLRKVNPAAALEELEKIEKARMMERMSLKHQNSGKWAKSKAIMAKYDLEARQAMQEQLSKNKELTQKLQVASESEEEEGGTEDVEELLVPDVVNEVQMNADGPNPWMLRSCTSDTKEAATQEDPEQLPELEAHGVSESEGEERPVAEEEILLREFEERRSLRKRSELSQDAEPAGSQETKDSGSQEVLSELRVLSQKLKENHQSRKQKASSEGTIPQVQREEPAPEEEEPLLLQRPERVQTLEELEELGKEECFQNKELPRPVLEGQQSERTPNNRPDAPKEKKKKEQMIDLQNLLTTQSPSVKSLAVPTIEELEDEEERNHRQMIKEAFAGDDVIRDFLKEKREAVEASKPKDVDLTLPGWGEWGGVGLKPSAKKRRRFLIKAPEGPPRKDKNLPNVIINEKRNIHAAAHQVRVLPYPFTHHWQFERTIQTPIGSTWNTQRAFQKLTTPKVVTKPGHIINPIKAEDVGYRSSSRSDLSVIQRNPKRITTRHKKQLKKCSVD
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 Orthologous
Protein Cluster
9PhosphorylationTANRLAESLLALSQQ
CHHHHHHHHHHHHCH		24.0722199227
14PhosphorylationAESLLALSQQEELAD
HHHHHHHHCHHHHCC		24.9828102081
26PhosphorylationLADLPKDYLLSESED
HCCCCHHHCCCCCCC		18.7029255136
29PhosphorylationLPKDYLLSESEDEGD
CCHHHCCCCCCCCCC		36.1629255136
31PhosphorylationKDYLLSESEDEGDND
HHHCCCCCCCCCCCC		47.1529255136
45SumoylationDGERKHQKLLEAISS
CHHHHHHHHHHHHHC		55.55-
45SumoylationDGERKHQKLLEAISS
CHHHHHHHHHHHHHC		55.55-
51PhosphorylationQKLLEAISSLDGKNR
HHHHHHHHCCCCHHH		31.7130266825
52PhosphorylationKLLEAISSLDGKNRR
HHHHHHHCCCCHHHH		25.1130266825
56AcetylationAISSLDGKNRRKLAE
HHHCCCCHHHHHHHH		47.1226051181
65PhosphorylationRRKLAERSEASLKVS
HHHHHHHHHHHCEEE		29.0824719451
68PhosphorylationLAERSEASLKVSEFN
HHHHHHHHCEEEEEE		25.3524719451
72PhosphorylationSEASLKVSEFNVSSE
HHHHCEEEEEECCCC		34.5824732914
77PhosphorylationKVSEFNVSSEGSGEK
EEEEEECCCCCCCCE		24.6329255136
77UbiquitinationKVSEFNVSSEGSGEK
EEEEEECCCCCCCCE		24.6324816145
78PhosphorylationVSEFNVSSEGSGEKL
EEEEECCCCCCCCEE		41.5129255136
81PhosphorylationFNVSSEGSGEKLVLA
EECCCCCCCCEEEEH		39.4629255136
96PhosphorylationDLLEPVKTSSSLATV
HHCCCCCCCCHHHHH		33.7921712546
97PhosphorylationLLEPVKTSSSLATVK
HCCCCCCCCHHHHHH		16.5328674419
98PhosphorylationLEPVKTSSSLATVKK
CCCCCCCCHHHHHHH		34.3023312004
99PhosphorylationEPVKTSSSLATVKKQ
CCCCCCCHHHHHHHH		23.0725159151
102PhosphorylationKTSSSLATVKKQLSR
CCCCHHHHHHHHHHH		37.84-
122AcetylationTVELPLNKEEIERIH
EEECCCCHHHHHHHH		65.4926051181
122SumoylationTVELPLNKEEIERIH
EEECCCCHHHHHHHH		65.4928112733
127UbiquitinationLNKEEIERIHREVAF
CCHHHHHHHHHHHHH		35.3624816145
136MethylationHREVAFNKTAQVLSK
HHHHHHHHHHHHHHC		38.49115978867
141UbiquitinationFNKTAQVLSKWDPVV
HHHHHHHHHCCCCEE		2.6424816145
143UbiquitinationKTAQVLSKWDPVVLK
HHHHHHHCCCCEEEC		52.00-
155UbiquitinationVLKNRQAEQLVFPLE
EECCCCHHHEEECCC		35.7924816145
169UbiquitinationEKEEPAIAPIEHVLS
CCCCCCCCCHHHHHC		10.9224816145
179UbiquitinationEHVLSGWKARTPLEQ
HHHHCCCCCCCHHHH		31.3629967540
194UbiquitinationEIFNLLHKNKQPVTD
HHHHHHHCCCCCCCC		66.8533845483
196UbiquitinationFNLLHKNKQPVTDPL
HHHHHCCCCCCCCCC		61.86-
200PhosphorylationHKNKQPVTDPLLTPV
HCCCCCCCCCCCCHH		38.2825137130
205PhosphorylationPVTDPLLTPVEKASL
CCCCCCCCHHHHHHH		32.7325159151
211PhosphorylationLTPVEKASLRAMSLE
CCHHHHHHHHHCCHH		29.4721406692
216PhosphorylationKASLRAMSLEEAKMR
HHHHHHCCHHHHHHH		31.4821815630
221UbiquitinationAMSLEEAKMRRAELQ
HCCHHHHHHHHHHHH		35.9024816145
233UbiquitinationELQRARALQSYYEAK
HHHHHHHHHHHHHHH		2.6424816145
2402-HydroxyisobutyrylationLQSYYEAKARREKKI
HHHHHHHHHHHHHHH		30.41-
285AcetylationAALEELEKIEKARMM
HHHHHHHHHHHHHHH		69.6426051181
285UbiquitinationAALEELEKIEKARMM
HHHHHHHHHHHHHHH		69.6424816145
288UbiquitinationEELEKIEKARMMERM
HHHHHHHHHHHHHHH		44.78-
298MethylationMMERMSLKHQNSGKW
HHHHHCHHHCCCCHH		35.52-
305UbiquitinationKHQNSGKWAKSKAIM
HHCCCCHHHHHHHHH		16.6724816145
307MethylationQNSGKWAKSKAIMAK
CCCCHHHHHHHHHHH		51.91-
309MethylationSGKWAKSKAIMAKYD
CCHHHHHHHHHHHHC		41.02-
314SumoylationKSKAIMAKYDLEARQ
HHHHHHHHHCHHHHH		23.16-
314SumoylationKSKAIMAKYDLEARQ
HHHHHHHHHCHHHHH		23.16-
330UbiquitinationMQEQLSKNKELTQKL
HHHHHHHCHHHHHHH		39.3924816145
333UbiquitinationQLSKNKELTQKLQVA
HHHHCHHHHHHHHHH		7.0224816145
340UbiquitinationLTQKLQVASESEEEE
HHHHHHHHCCCHHHC		8.4624816145
341PhosphorylationTQKLQVASESEEEEG
HHHHHHHCCCHHHCC		42.6822210691
343PhosphorylationKLQVASESEEEEGGT
HHHHHCCCHHHCCCC		48.0626029660
389PhosphorylationSDTKEAATQEDPEQL
CCHHHHHHCCCHHHC		39.2728176443
397UbiquitinationQEDPEQLPELEAHGV
CCCHHHCHHHHHCCC		43.7724816145
405PhosphorylationELEAHGVSESEGEER
HHHHCCCCCCCCCCC		39.7429255136
407PhosphorylationEAHGVSESEGEERPV
HHCCCCCCCCCCCCC		43.3129255136
425UbiquitinationEILLREFEERRSLRK
HHHHHHHHHHHHHHH		45.9324816145
429PhosphorylationREFEERRSLRKRSEL
HHHHHHHHHHHHHHH		38.45-
433CitrullinationERRSLRKRSELSQDA
HHHHHHHHHHHCCCC		29.00-
433CitrullinationERRSLRKRSELSQDA
HHHHHHHHHHHCCCC		29.00-
434PhosphorylationRRSLRKRSELSQDAE
HHHHHHHHHHCCCCC		46.0223401153
437PhosphorylationLRKRSELSQDAEPAG
HHHHHHHCCCCCCCC		23.2029255136
445PhosphorylationQDAEPAGSQETKDSG
CCCCCCCCCCCCCCC		27.2729255136
448PhosphorylationEPAGSQETKDSGSQE
CCCCCCCCCCCCHHH		32.3022167270
449SumoylationPAGSQETKDSGSQEV
CCCCCCCCCCCHHHH		49.5028112733
449UbiquitinationPAGSQETKDSGSQEV
CCCCCCCCCCCHHHH		49.5024816145
451PhosphorylationGSQETKDSGSQEVLS
CCCCCCCCCHHHHHH		41.7322167270
453PhosphorylationQETKDSGSQEVLSEL
CCCCCCCHHHHHHHH		27.4129255136
458PhosphorylationSGSQEVLSELRVLSQ
CCHHHHHHHHHHHHH		39.5023927012
466AcetylationELRVLSQKLKENHQS
HHHHHHHHHHHHHHH		59.1425953088
477UbiquitinationNHQSRKQKASSEGTI
HHHHHHHHHHCCCCC		53.9524816145
479PhosphorylationQSRKQKASSEGTIPQ
HHHHHHHHCCCCCCC		35.6419691289
480PhosphorylationSRKQKASSEGTIPQV
HHHHHHHCCCCCCCC		44.9219691289
508UbiquitinationLLQRPERVQTLEELE
HHHCHHHHCCHHHHH		4.9324816145
510PhosphorylationQRPERVQTLEELEEL
HCHHHHCCHHHHHHH		33.0221815630
518UbiquitinationLEELEELGKEECFQN
HHHHHHHCHHHHHCC		38.3124816145
519AcetylationEELEELGKEECFQNK
HHHHHHCHHHHHCCC		64.0626051181
519SumoylationEELEELGKEECFQNK
HHHHHHCHHHHHCCC		64.0628112733
526AcetylationKEECFQNKELPRPVL
HHHHHCCCCCCCCCC		50.2526051181
538PhosphorylationPVLEGQQSERTPNNR
CCCCCCCCCCCCCCC		22.5925159151
541PhosphorylationEGQQSERTPNNRPDA
CCCCCCCCCCCCCCC		26.7325159151
566PhosphorylationIDLQNLLTTQSPSVK
HHHHHHHHCCCCCHH		26.4229255136
567PhosphorylationDLQNLLTTQSPSVKS
HHHHHHHCCCCCHHH		27.3329255136
569PhosphorylationQNLLTTQSPSVKSLA
HHHHHCCCCCHHHCC		19.6329255136
571PhosphorylationLLTTQSPSVKSLAVP
HHHCCCCCHHHCCCC		47.6429255136
574PhosphorylationTQSPSVKSLAVPTIE
CCCCCHHHCCCCCHH		21.2928555341
589CitrullinationELEDEEERNHRQMIK
HHCCHHHHHHHHHHH		47.75-
589CitrullinationELEDEEERNHRQMIK
HHCCHHHHHHHHHHH		47.75-
600UbiquitinationQMIKEAFAGDDVIRD
HHHHHHHCCCHHHHH		27.7933845483
610UbiquitinationDVIRDFLKEKREAVE
HHHHHHHHHHHHHHH		62.2724816145
620SumoylationREAVEASKPKDVDLT
HHHHHHCCCCCCCEE		64.23-
620SumoylationREAVEASKPKDVDLT
HHHHHHCCCCCCCEE		64.23-
627PhosphorylationKPKDVDLTLPGWGEW
CCCCCCEECCCCCCC		26.8328348404
640UbiquitinationEWGGVGLKPSAKKRR
CCCCCCCCCCHHHHC		30.88-
642PhosphorylationGGVGLKPSAKKRRRF
CCCCCCCCHHHHCEE		51.6522199227
652MethylationKRRRFLIKAPEGPPR
HHCEEEECCCCCCCC		61.10-
652UbiquitinationKRRRFLIKAPEGPPR
HHCEEEECCCCCCCC		61.1033845483
662UbiquitinationEGPPRKDKNLPNVII
CCCCCCCCCCCCEEE		64.5224816145
6722-HydroxyisobutyrylationPNVIINEKRNIHAAA
CCEEECCCCCHHHHH		46.38-
672UbiquitinationPNVIINEKRNIHAAA
CCEEECCCCCHHHHH		46.38-
701PhosphorylationQFERTIQTPIGSTWN
EEEEEECCCCCCCHH		17.0228857561
724AcetylationTTPKVVTKPGHIINP
CCCCCCCCCCCCCCC		37.0726051181
733SumoylationGHIINPIKAEDVGYR
CCCCCCCCHHHCCCC		47.16-
733AcetylationGHIINPIKAEDVGYR
CCCCCCCCHHHCCCC		47.1663796817
733SumoylationGHIINPIKAEDVGYR
CCCCCCCCHHHCCCC		47.1628112733
741PhosphorylationAEDVGYRSSSRSDLS
HHHCCCCCCCHHHCH		24.9625159151
742PhosphorylationEDVGYRSSSRSDLSV
HHCCCCCCCHHHCHH		22.2925159151
743PhosphorylationDVGYRSSSRSDLSVI
HCCCCCCCHHHCHHH		36.7325159151
745PhosphorylationGYRSSSRSDLSVIQR
CCCCCCHHHCHHHHC		44.8723186163
748PhosphorylationSSSRSDLSVIQRNPK
CCCHHHCHHHHCCCC		23.3619691289
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

Oops, there are no upstream regulatory protein records of UT14A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UT14A_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UT14A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NINL_HUMANNINLphysical
16189514
CEP70_HUMANCEP70physical
16189514
LDOC1_HUMANLDOC1physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
HOOK2_HUMANHOOK2physical
16189514
P53_HUMANTP53physical
21078665
GA45G_HUMANGADD45Gphysical
15383276
WDR18_HUMANWDR18physical
22939629
VDAC2_HUMANVDAC2physical
22939629
SMYD1_HUMANSMYD1physical
23455924
DKC1_HUMANDKC1physical
26344197
NOP56_HUMANNOP56physical
26344197
NOP58_HUMANNOP58physical
26344197
RPF2_HUMANRPF2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UT14A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-29; SER-31; SER-437 ANDSER-445, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26; SER-29; SER-31;SER-77; SER-437 AND SER-445, AND MASS SPECTROMETRY.
"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-29; SER-31; SER-52;SER-77; SER-405; SER-407 AND SER-445, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-99; THR-389;SER-405; SER-407; SER-437; SER-445; SER-453; SER-479; THR-541;SER-569; SER-571 AND SER-748, AND MASS SPECTROMETRY.
"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-437; SER-445 ANDSER-453, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-451, AND MASSSPECTROMETRY.
"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-29; SER-31 AND SER-445,AND MASS SPECTROMETRY.

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