BCD1_HUMAN - dbPTM
BCD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BCD1_HUMAN
UniProt AC Q9NWK9
Protein Name Box C/D snoRNA protein 1
Gene Name ZNHIT6
Organism Homo sapiens (Human).
Sequence Length 470
Subcellular Localization
Protein Description Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis..
Protein Sequence MEFAAENEGKSGGGLHSVAEGVRLSPEPGREGVRDLAGAEEFGGGEEGTGLTGIKEIGDGEEGSGQRPEEIPMDLTVVKQEIIDWPGTEGRLAGQWVEQEVEDRPEVKDENAGVLEVKQETDSSLVVKEAKVGEPEVKEEKVKEEVMDWSEVKEEKDNLEIKQEEKFVGQCIKEELMHGECVKEEKDFLKKEIVDDTKVKEEPPINHPVGCKRKLAMSRCETCGTEEAKYRCPRCMRYSCSLPCVKKHKAELTCNGVRDKTAYISIQQFTEMNLLSDYRFLEDVARTADHISRDAFLKRPISNKYMYFMKNRARRQGINLKLLPNGFTKRKENSTFFDKKKQQFCWHVKLQFPQSQAEYIEKRVPDDKTINEILKPYIDPEKSDPVIRQRLKAYIRSQTGVQILMKIEYMQQNLVRYYELDPYKSLLDNLRNKVIIEYPTLHVVLKGSNNDMKVLHQVKSESTKNVGNEN
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
10UbiquitinationFAAENEGKSGGGLHS
CCCCCCCCCCCCCCC		39.4824816145
11PhosphorylationAAENEGKSGGGLHSV
CCCCCCCCCCCCCCH		54.2323927012
17PhosphorylationKSGGGLHSVAEGVRL
CCCCCCCCHHCCCCC		28.2323927012
25PhosphorylationVAEGVRLSPEPGREG
HHCCCCCCCCCCCCC		19.3629255136
49PhosphorylationFGGGEEGTGLTGIKE
HCCCCCCCCCCCCEE		32.09-
52PhosphorylationGEEGTGLTGIKEIGD
CCCCCCCCCCEEECC		37.90-
55AcetylationGTGLTGIKEIGDGEE
CCCCCCCEEECCCCC		44.6226051181
76PhosphorylationEEIPMDLTVVKQEII
CCCCCCEEEEEEEEC		20.9930631047
79SumoylationPMDLTVVKQEIIDWP
CCCEEEEEEEECCCC		37.5728112733
108SumoylationVEDRPEVKDENAGVL
CCCCCCCCCCCCCEE		58.6328112733
118SumoylationNAGVLEVKQETDSSL
CCCEEEEEEECCCCE		32.80-
118SumoylationNAGVLEVKQETDSSL
CCCEEEEEEECCCCE		32.8028112733
121PhosphorylationVLEVKQETDSSLVVK
EEEEEEECCCCEEEE		38.39-
123PhosphorylationEVKQETDSSLVVKEA
EEEEECCCCEEEEEE		32.75-
138SumoylationKVGEPEVKEEKVKEE
CCCCHHHCHHHHHHH		59.5028112733
138SumoylationKVGEPEVKEEKVKEE
CCCCHHHCHHHHHHH		59.50-
143SumoylationEVKEEKVKEEVMDWS
HHCHHHHHHHHCCHH		60.26-
143SumoylationEVKEEKVKEEVMDWS
HHCHHHHHHHHCCHH		60.2628112733
153SumoylationVMDWSEVKEEKDNLE
HCCHHHHHHHHCCCC		56.98-
153SumoylationVMDWSEVKEEKDNLE
HCCHHHHHHHHCCCC		56.9828112733
162SumoylationEKDNLEIKQEEKFVG
HHCCCCCCHHHHHHH		42.13-
162SumoylationEKDNLEIKQEEKFVG
HHCCCCCCHHHHHHH		42.1328112733
173SumoylationKFVGQCIKEELMHGE
HHHHHHHHHHHHCCC		53.41-
173UbiquitinationKFVGQCIKEELMHGE
HHHHHHHHHHHHCCC		53.4121963094
173SumoylationKFVGQCIKEELMHGE
HHHHHHHHHHHHCCC		53.4128112733
175UbiquitinationVGQCIKEELMHGECV
HHHHHHHHHHCCCCH		46.5222817900
183SumoylationLMHGECVKEEKDFLK
HHCCCCHHHHHHHHH		72.3428112733
190UbiquitinationKEEKDFLKKEIVDDT
HHHHHHHHHHHCCCC		48.6421963094
197PhosphorylationKKEIVDDTKVKEEPP
HHHHCCCCCCCCCCC		33.0222067460
200SumoylationIVDDTKVKEEPPINH
HCCCCCCCCCCCCCC		58.8928112733
200SumoylationIVDDTKVKEEPPINH
HCCCCCCCCCCCCCC		58.89-
207UbiquitinationKEEPPINHPVGCKRK
CCCCCCCCCCCCCHH		21.1021963094
208UbiquitinationEEPPINHPVGCKRKL
CCCCCCCCCCCCHHH		21.5122817900
210UbiquitinationPPINHPVGCKRKLAM
CCCCCCCCCCHHHHH		18.7122817900
212UbiquitinationINHPVGCKRKLAMSR
CCCCCCCCHHHHHHC		46.7921963094
214UbiquitinationHPVGCKRKLAMSRCE
CCCCCCHHHHHHCCC		26.5422817900
218PhosphorylationCKRKLAMSRCETCGT
CCHHHHHHCCCCCCC		28.3323401153
222PhosphorylationLAMSRCETCGTEEAK
HHHHCCCCCCCHHHH		21.6223401153
225PhosphorylationSRCETCGTEEAKYRC
HCCCCCCCHHHHHCC		32.5728985074
229UbiquitinationTCGTEEAKYRCPRCM
CCCCHHHHHCCCCHH		36.1921963094
230PhosphorylationCGTEEAKYRCPRCMR
CCCHHHHHCCCCHHH		25.2123401153
246UbiquitinationSCSLPCVKKHKAELT
ECCCCCCHHHEEEEE		56.7421963094
247UbiquitinationCSLPCVKKHKAELTC
CCCCCCHHHEEEEEE		29.9122817900
249SumoylationLPCVKKHKAELTCNG
CCCCHHHEEEEEECC		53.05-
249SumoylationLPCVKKHKAELTCNG
CCCCHHHEEEEEECC		53.05-
249UbiquitinationLPCVKKHKAELTCNG
CCCCHHHEEEEEECC		53.0522817900
259UbiquitinationLTCNGVRDKTAYISI
EEECCCCCCCEEEEH		50.6922817900
265UbiquitinationRDKTAYISIQQFTEM
CCCCEEEEHHHHHHH		11.1521963094
271UbiquitinationISIQQFTEMNLLSDY
EEHHHHHHHHHHHCH		27.6221963094
290UbiquitinationDVARTADHISRDAFL
HHHHHCHHHCHHHHH		19.9129967540
292UbiquitinationARTADHISRDAFLKR
HHHCHHHCHHHHHCC		22.2329967540
298UbiquitinationISRDAFLKRPISNKY
HCHHHHHCCCCCHHH		50.0721906983
302PhosphorylationAFLKRPISNKYMYFM
HHHCCCCCHHHHHHH		29.9225954137
304UbiquitinationLKRPISNKYMYFMKN
HCCCCCHHHHHHHHH		25.3021963094
305PhosphorylationKRPISNKYMYFMKNR
CCCCCHHHHHHHHHH		10.9925954137
310UbiquitinationNKYMYFMKNRARRQG
HHHHHHHHHHHHHCC		33.1221963094
321UbiquitinationRRQGINLKLLPNGFT
HHCCCCEEECCCCCC		43.41-
323UbiquitinationQGINLKLLPNGFTKR
CCCCEEECCCCCCCC		2.7122505724
329UbiquitinationLLPNGFTKRKENSTF
ECCCCCCCCCCCCCC		60.2529967540
329MethylationLLPNGFTKRKENSTF
ECCCCCCCCCCCCCC		60.2583045199
331UbiquitinationPNGFTKRKENSTFFD
CCCCCCCCCCCCCCC		63.9029967540
334PhosphorylationFTKRKENSTFFDKKK
CCCCCCCCCCCCHHH		27.9020068231
335PhosphorylationTKRKENSTFFDKKKQ
CCCCCCCCCCCHHHC		39.6420068231
336UbiquitinationKRKENSTFFDKKKQQ
CCCCCCCCCCHHHCE		8.1722817900
340UbiquitinationNSTFFDKKKQQFCWH
CCCCCCHHHCEEEEE		58.62-
341UbiquitinationSTFFDKKKQQFCWHV
CCCCCHHHCEEEEEE		55.88-
343UbiquitinationFFDKKKQQFCWHVKL
CCCHHHCEEEEEEEE		44.3329967540
359PhosphorylationFPQSQAEYIEKRVPD
CCHHHHHHHHHHCCC		19.8622817900
362UbiquitinationSQAEYIEKRVPDDKT
HHHHHHHHHCCCCCH		49.4922505724
368UbiquitinationEKRVPDDKTINEILK
HHHCCCCCHHHHHHH		59.7029967540
375UbiquitinationKTINEILKPYIDPEK
CHHHHHHHHHCCHHH		41.2421906983
382UbiquitinationKPYIDPEKSDPVIRQ
HHHCCHHHCCHHHHH		66.6029967540
385UbiquitinationIDPEKSDPVIRQRLK
CCHHHCCHHHHHHHH		30.4421963094
394PhosphorylationIRQRLKAYIRSQTGV
HHHHHHHHHHHHHHH		8.6922210691
397PhosphorylationRLKAYIRSQTGVQIL
HHHHHHHHHHHHHHH		23.6422210691
399PhosphorylationKAYIRSQTGVQILMK
HHHHHHHHHHHHHHH		40.3322210691
414UbiquitinationIEYMQQNLVRYYELD
HHHHHHHCHHHHCCC		1.7029967540
420UbiquitinationNLVRYYELDPYKSLL
HCHHHHCCCHHHHHH		4.6721963094
423PhosphorylationRYYELDPYKSLLDNL
HHHCCCHHHHHHHHH		16.93-
424UbiquitinationYYELDPYKSLLDNLR
HHCCCHHHHHHHHHH		39.7621906983
425UbiquitinationYELDPYKSLLDNLRN
HCCCHHHHHHHHHHC		28.4622817900
425PhosphorylationYELDPYKSLLDNLRN
HCCCHHHHHHHHHHC		28.46-
433UbiquitinationLLDNLRNKVIIEYPT
HHHHHHCCEEEECCC		28.51-
438PhosphorylationRNKVIIEYPTLHVVL
HCCEEEECCCEEEEE		7.3620049867
440PhosphorylationKVIIEYPTLHVVLKG
CEEEECCCEEEEEEC		28.7020049867
453UbiquitinationKGSNNDMKVLHQVKS
ECCCCCHHHHHHHCC		44.5029967540
459SumoylationMKVLHQVKSESTKNV
HHHHHHHCCHHCCCC		41.77-
459UbiquitinationMKVLHQVKSESTKNV
HHHHHHHCCHHCCCC		41.7721963094
459SumoylationMKVLHQVKSESTKNV
HHHHHHHCCHHCCCC		41.7728112733
464UbiquitinationQVKSESTKNVGNEN-
HHCCHHCCCCCCCC-		59.9422817900
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 BCD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BCD1_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 BCD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUFP1_HUMANNUFIP1physical
25404746
ZNHI3_HUMANZNHIT3physical
25404746
RUVB1_HUMANRUVBL1physical
25404746
BCD1_HUMANZNHIT6physical
28561026
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 BCD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-25, 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-25, AND MASSSPECTROMETRY.

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