UT14C_HUMAN - dbPTM
UT14C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UT14C_HUMAN
UniProt AC Q5TAP6
Protein Name U3 small nucleolar RNA-associated protein 14 homolog C
Gene Name UTP14C
Organism Homo sapiens (Human).
Sequence Length 766
Subcellular Localization Nucleus, nucleolus.
Protein Description Essential for spermatogenesis. May be required specifically for ribosome biogenesis and hence protein synthesis during male meiosis (By similarity)..
Protein Sequence MNVNQVAENLALSHQEELVDLPKNYPLSENEDEGDSDGERKHQKLLEAIISLDGKNRRKLAERSEASLKVSEFSVSSEGSGEKLGLADLLEPVKTSSSLATVKKQLNRVKSKKVVELPLNKEKIEQIHREVAFSKTSQVLSKWDPIILKNQQAEQLVFPLGKEQPAIAPIEHALSGWKARTPLEQEIFNLLHKNKQPVTDPLLTPMEKASLQAMSLEEAKMHRAELQRARALQSYYEAKARKEKKIKSKKYHKVVKKGKAKKALKEFEQLQKVNPTVALEEMEKIENARMMERMSLKHQNSGKWAKSKAIMAKYDLEARQAMQEQLAKNKELTQKLQVASESEEEEGGTEVEELLVPHVANEVQMNVDGPNPWMFRSCTSDTKEAATQEDPEQVPELAAHEVSASEAEERPVAEEEILLREFEERQSLRKRSELNQDAEPASSQETKDSSSQEVLSELRALSQKLKEKHQSRKQKASSEGTVPQVQREEPAPEEAEPLLLQRSERVQTLEELEELGKEDCFQNKELPRPVLEGQQSERTPNNRPDAPKEKKEKEQLINLQNFLTTQSPSVRSLAVPTIIEELEDEEERDQRQMIKEAFAGDDVIRDFLKEKREAVEASKPKDVDLTLPGWGEWGGVGLKPSAKKRRQFLIKAPEGPPRKDKNLPNVIISEKRNIHAAAHQVQVLPYPFTHHRQFERTIQTPIGSTWNTQRAFQKLTTPKVVTKPGHIIKPIKAEDVGYQSSSRSDLPVIQRNPKRITTRHNKEEKL
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
28PhosphorylationLPKNYPLSENEDEGD
CCCCCCCCCCCCCCC		33.5920363803
36PhosphorylationENEDEGDSDGERKHQ
CCCCCCCCCCHHHHH		59.3720363803
51PhosphorylationKLLEAIISLDGKNRR
HHHHHHHCCCCCCHH		17.81-
64PhosphorylationRRKLAERSEASLKVS
HHHHHHHHHHCEEEE		29.0822210691
67PhosphorylationLAERSEASLKVSEFS
HHHHHHHCEEEEEEE		25.3522210691
71PhosphorylationSEASLKVSEFSVSSE
HHHCEEEEEEEECCC		31.1927251275
74PhosphorylationSLKVSEFSVSSEGSG
CEEEEEEEECCCCCC		19.6227251275
76PhosphorylationKVSEFSVSSEGSGEK
EEEEEEECCCCCCCC		22.8227251275
77PhosphorylationVSEFSVSSEGSGEKL
EEEEEECCCCCCCCC		43.7727251275
80PhosphorylationFSVSSEGSGEKLGLA
EEECCCCCCCCCCHH		39.4627251275
96PhosphorylationLLEPVKTSSSLATVK
HCCCCCCCCHHHHHH		16.5328674419
97PhosphorylationLEPVKTSSSLATVKK
CCCCCCCCHHHHHHH		34.3023312004
98PhosphorylationEPVKTSSSLATVKKQ
CCCCCCCHHHHHHHH		23.0725159151
101PhosphorylationKTSSSLATVKKQLNR
CCCCHHHHHHHHHHH		37.84-
134PhosphorylationIHREVAFSKTSQVLS
HHHHHHHCHHHHHHH		25.86-
193UbiquitinationEIFNLLHKNKQPVTD
HHHHHHHCCCCCCCC		66.85-
199PhosphorylationHKNKQPVTDPLLTPM
HCCCCCCCCCCCCHH		38.2828842319
204PhosphorylationPVTDPLLTPMEKASL
CCCCCCCCHHHHHHH		28.42-
210PhosphorylationLTPMEKASLQAMSLE
CCHHHHHHHHCCCHH		31.8928348404
215PhosphorylationKASLQAMSLEEAKMH
HHHHHCCCHHHHHHH		35.3321815630
234PhosphorylationQRARALQSYYEAKAR
HHHHHHHHHHHHHHH		30.4523898821
284UbiquitinationVALEEMEKIENARMM
CHHHHHHHHHHHHHH		54.75-
297MethylationMMERMSLKHQNSGKW
HHHHHCHHHCCCCHH		35.52-
303AcetylationLKHQNSGKWAKSKAI
HHHCCCCHHHHHHHH		43.7425953088
306MethylationQNSGKWAKSKAIMAK
CCCCHHHHHHHHHHH		51.91-
308MethylationSGKWAKSKAIMAKYD
CCHHHHHHHHHHHHC		41.02-
313SumoylationKSKAIMAKYDLEARQ
HHHHHHHHHCHHHHH		23.16-
313SumoylationKSKAIMAKYDLEARQ
HHHHHHHHHCHHHHH		23.16-
313AcetylationKSKAIMAKYDLEARQ
HHHHHHHHHCHHHHH		23.1625953088
340PhosphorylationTQKLQVASESEEEEG
HHHHHHHCCCCHHCC		42.68-
342PhosphorylationKLQVASESEEEEGGT
HHHHHCCCCHHCCCC		48.06-
387PhosphorylationSDTKEAATQEDPEQV
CCHHHHHCCCCHHHH		39.2722817900
403PhosphorylationELAAHEVSASEAEER
HHHHHHCCHHHHHHC		24.08-
405PhosphorylationAAHEVSASEAEERPV
HHHHCCHHHHHHCCC		29.81-
432PhosphorylationRQSLRKRSELNQDAE
HHHHHHHHHHCCCCC		49.8528509920
442PhosphorylationNQDAEPASSQETKDS
CCCCCCCCCCCCCCC		43.1825159151
443PhosphorylationQDAEPASSQETKDSS
CCCCCCCCCCCCCCC		33.8628509920
446PhosphorylationEPASSQETKDSSSQE
CCCCCCCCCCCCHHH		32.3029083192
450PhosphorylationSQETKDSSSQEVLSE
CCCCCCCCHHHHHHH		46.29-
451PhosphorylationQETKDSSSQEVLSEL
CCCCCCCHHHHHHHH		34.02-
456PhosphorylationSSSQEVLSELRALSQ
CCHHHHHHHHHHHHH		39.5022210691
462PhosphorylationLSELRALSQKLKEKH
HHHHHHHHHHHHHHH		25.0422210691
508PhosphorylationQRSERVQTLEELEEL
HHHHHCCCHHHHHHH		33.0221815630
536PhosphorylationPVLEGQQSERTPNNR
CCCCCCCCCCCCCCC		22.5925159151
539PhosphorylationEGQQSERTPNNRPDA
CCCCCCCCCCCCCCC		26.7325159151
567PhosphorylationQNFLTTQSPSVRSLA
HHHHHCCCHHHHHHC		19.63-
619SumoylationREAVEASKPKDVDLT
HHHHHHCCCCCCCEE		64.23-
619SumoylationREAVEASKPKDVDLT
HHHHHHCCCCCCCEE		64.23-
626PhosphorylationKPKDVDLTLPGWGEW
CCCCCCEECCCCCCC		26.8328348404
639AcetylationEWGGVGLKPSAKKRR
CCCCCCCCCCHHHHH		30.8826051181
639UbiquitinationEWGGVGLKPSAKKRR
CCCCCCCCCCHHHHH		30.88-
641PhosphorylationGGVGLKPSAKKRRQF
CCCCCCCCHHHHHHE		51.6522199227
651MethylationKRRQFLIKAPEGPPR
HHHHEEECCCCCCCC		61.10-
669PhosphorylationNLPNVIISEKRNIHA
CCCCEEEECCCCHHH		26.4124719451
700PhosphorylationQFERTIQTPIGSTWN
CCCEECCCCCCCCCH		17.0228857561
738PhosphorylationIKAEDVGYQSSSRSD
EEHHHCCCCCCCCCC		12.6920068231
740PhosphorylationAEDVGYQSSSRSDLP
HHHCCCCCCCCCCCC		23.0720068231
741PhosphorylationEDVGYQSSSRSDLPV
HHCCCCCCCCCCCCH		17.7820068231
742PhosphorylationDVGYQSSSRSDLPVI
HCCCCCCCCCCCCHH		40.8420068231
744PhosphorylationGYQSSSRSDLPVIQR
CCCCCCCCCCCHHCC		45.5120068231
762UbiquitinationRITTRHNKEEKL---
CCCCCCCCHHCC---		62.21-
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 UT14C_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UT14C_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 UT14C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOOK2_HUMANHOOK2physical
25416956
TEX11_HUMANTEX11physical
25416956
TRI54_HUMANTRIM54physical
25416956
LZTS2_HUMANLZTS2physical
25416956
K1C40_HUMANKRT40physical
25416956
PRIC1_HUMANPRICKLE1physical
25416956
CCD57_HUMANCCDC57physical
25416956
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 UT14C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-28 AND SER-36, AND MASSSPECTROMETRY.

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