DSN1_HUMAN - dbPTM
DSN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DSN1_HUMAN
UniProt AC Q9H410
Protein Name Kinetochore-associated protein DSN1 homolog
Gene Name DSN1
Organism Homo sapiens (Human).
Sequence Length 356
Subcellular Localization Nucleus . Chromosome, centromere, kinetochore . Associated with the kinetochore.
Protein Description Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis..
Protein Sequence MTSVTRSEIIDEKGPVMSKTHDHQLESSLSPVEVFAKTSASLEMNQGVSEERIHLGSSPKKGGNCDLSHQERLQSKSLHLSPQEQSASYQDRRQSWRRASMKETNRRKSLHPIHQGITELSRSISVDLAESKRLGCLLLSSFQFSIQKLEPFLRDTKGFSLESFRAKASSLSEELKHFADGLETDGTLQKCFEDSNGKASDFSLEASVAEMKEYITKFSLERQTWDQLLLHYQQEAKEILSRGSTEAKITEVKVEPMTYLGSSQNEVLNTKPDYQKILQNQSKVFDCMELVMDELQGSVKQLQAFMDESTQCFQKVSVQLGKRSMQQLDPSPARKLLKLQLQNPPAIHGSGSGSCQ
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
2Phosphorylation------MTSVTRSEI
------CCCCCHHHH		31.7220068231
3Phosphorylation-----MTSVTRSEII
-----CCCCCHHHHC		21.8620068231
5Phosphorylation---MTSVTRSEIIDE
---CCCCCHHHHCCC		28.3920068231
7Phosphorylation-MTSVTRSEIIDEKG
-CCCCCHHHHCCCCC		24.6320068231
12 (in isoform 4)Phosphorylation-49.8825849741
13SumoylationRSEIIDEKGPVMSKT
HHHHCCCCCCCCCCC		65.84-
13SumoylationRSEIIDEKGPVMSKT
HHHHCCCCCCCCCCC		65.84-
14 (in isoform 4)Phosphorylation-20.2725849741
18PhosphorylationDEKGPVMSKTHDHQL
CCCCCCCCCCCCHHH		34.3427794612
20PhosphorylationKGPVMSKTHDHQLES
CCCCCCCCCCHHHHC		25.8130266825
27PhosphorylationTHDHQLESSLSPVEV
CCCHHHHCCCCCHHH		45.2130266825
28PhosphorylationHDHQLESSLSPVEVF
CCHHHHCCCCCHHHH		24.4023927012
30PhosphorylationHQLESSLSPVEVFAK
HHHHCCCCCHHHHHH		28.9323927012
38PhosphorylationPVEVFAKTSASLEMN
CHHHHHHCCCCHHCC		26.5419691289
39PhosphorylationVEVFAKTSASLEMNQ
HHHHHHCCCCHHCCC		18.3619691289
41PhosphorylationVFAKTSASLEMNQGV
HHHHCCCCHHCCCCC		25.3225159151
44SulfoxidationKTSASLEMNQGVSEE
HCCCCHHCCCCCCCC		5.7121406390
49PhosphorylationLEMNQGVSEERIHLG
HHCCCCCCCCCEECC		40.3325159151
57PhosphorylationEERIHLGSSPKKGGN
CCCEECCCCCCCCCC		50.2329255136
58PhosphorylationERIHLGSSPKKGGNC
CCEECCCCCCCCCCC		38.6529255136
61SumoylationHLGSSPKKGGNCDLS
ECCCCCCCCCCCCCC		75.36-
61SumoylationHLGSSPKKGGNCDLS
ECCCCCCCCCCCCCC		75.36-
68PhosphorylationKGGNCDLSHQERLQS
CCCCCCCCHHHHHHH		15.1825159151
75PhosphorylationSHQERLQSKSLHLSP
CHHHHHHHHCCCCCH		28.8925159151
76SumoylationHQERLQSKSLHLSPQ
HHHHHHHHCCCCCHH		44.04-
76SumoylationHQERLQSKSLHLSPQ
HHHHHHHHCCCCCHH		44.04-
76UbiquitinationHQERLQSKSLHLSPQ
HHHHHHHHCCCCCHH		44.04-
77PhosphorylationQERLQSKSLHLSPQE
HHHHHHHCCCCCHHH		26.6929255136
81PhosphorylationQSKSLHLSPQEQSAS
HHHCCCCCHHHHCCH		17.5029255136
86PhosphorylationHLSPQEQSASYQDRR
CCCHHHHCCHHHHHH		20.5930266825
88PhosphorylationSPQEQSASYQDRRQS
CHHHHCCHHHHHHHH		28.6825159151
89PhosphorylationPQEQSASYQDRRQSW
HHHHCCHHHHHHHHH		17.7223927012
95PhosphorylationSYQDRRQSWRRASMK
HHHHHHHHHHHHHHH		22.2723882029
100PhosphorylationRQSWRRASMKETNRR
HHHHHHHHHHHHHHH		28.6822817900
108SumoylationMKETNRRKSLHPIHQ
HHHHHHHHCCCHHHH		54.88-
108SumoylationMKETNRRKSLHPIHQ
HHHHHHHHCCCHHHH		54.88-
108UbiquitinationMKETNRRKSLHPIHQ
HHHHHHHHCCCHHHH		54.88-
109 (in isoform 2)Ubiquitination-30.0521890473
109PhosphorylationKETNRRKSLHPIHQG
HHHHHHHCCCHHHHH		30.0523401153
110UbiquitinationETNRRKSLHPIHQGI
HHHHHHCCCHHHHHH		6.6321890473
118PhosphorylationHPIHQGITELSRSIS
CHHHHHHHHHHHHCC		37.3822067460
123PhosphorylationGITELSRSISVDLAE
HHHHHHHHCCCCHHH		18.8130266825
125PhosphorylationTELSRSISVDLAESK
HHHHHHCCCCHHHHH		15.7223401153
131PhosphorylationISVDLAESKRLGCLL
CCCCHHHHHHHCHHH		19.9129978859
132UbiquitinationSVDLAESKRLGCLLL
CCCHHHHHHHCHHHH		43.05-
150 (in isoform 2)Ubiquitination-40.8321890473
157SumoylationEPFLRDTKGFSLESF
HHHHCCCCCCCHHHH		63.35-
157UbiquitinationEPFLRDTKGFSLESF
HHHHCCCCCCCHHHH		63.35-
157SumoylationEPFLRDTKGFSLESF
HHHHCCCCCCCHHHH		63.35-
160PhosphorylationLRDTKGFSLESFRAK
HCCCCCCCHHHHHHH		39.6423909892
163PhosphorylationTKGFSLESFRAKASS
CCCCCHHHHHHHHHC		25.8923909892
167UbiquitinationSLESFRAKASSLSEE
CHHHHHHHHHCHHHH		44.54-
167SumoylationSLESFRAKASSLSEE
CHHHHHHHHHCHHHH		44.54-
167SumoylationSLESFRAKASSLSEE
CHHHHHHHHHCHHHH		44.54-
170PhosphorylationSFRAKASSLSEELKH
HHHHHHHCHHHHHHH		40.5522067460
172PhosphorylationRAKASSLSEELKHFA
HHHHHCHHHHHHHHH		30.8529414761
176 (in isoform 1)Ubiquitination-39.7021890473
176UbiquitinationSSLSEELKHFADGLE
HCHHHHHHHHHHCCC		39.7021906983
181 (in isoform 2)Ubiquitination-23.2221890473
190UbiquitinationETDGTLQKCFEDSNG
CCCCHHHHHHHCCCC		43.96-
201UbiquitinationDSNGKASDFSLEASV
CCCCCCCCCCCHHHH		41.8521890473
204 (in isoform 2)Ubiquitination-6.8621890473
207PhosphorylationSDFSLEASVAEMKEY
CCCCCHHHHHHHHHH		16.6920860994
209 (in isoform 2)Ubiquitination-14.5221890473
212UbiquitinationEASVAEMKEYITKFS
HHHHHHHHHHHHHHC		38.58-
217 (in isoform 1)Ubiquitination-24.3221890473
217UbiquitinationEMKEYITKFSLERQT
HHHHHHHHHCHHHCH		24.3221890473
219PhosphorylationKEYITKFSLERQTWD
HHHHHHHCHHHCHHH		30.77-
237UbiquitinationLHYQQEAKEILSRGS
HHHHHHHHHHHHCCC		44.53-
241PhosphorylationQEAKEILSRGSTEAK
HHHHHHHHCCCCCCE		40.0124719451
244PhosphorylationKEILSRGSTEAKITE
HHHHHCCCCCCEEEE		23.2017081983
245PhosphorylationEILSRGSTEAKITEV
HHHHCCCCCCEEEEE		42.6722817900
248UbiquitinationSRGSTEAKITEVKVE
HCCCCCCEEEEEEEE		43.8821906983
248 (in isoform 1)Ubiquitination-43.8821890473
253SumoylationEAKITEVKVEPMTYL
CCEEEEEEEECCEEC		34.35-
253UbiquitinationEAKITEVKVEPMTYL
CCEEEEEEEECCEEC		34.35-
253SumoylationEAKITEVKVEPMTYL
CCEEEEEEEECCEEC		34.3528112733
271UbiquitinationQNEVLNTKPDYQKIL
HHCHHCCCCCHHHHH		34.5121906983
271 (in isoform 1)Ubiquitination-34.5121890473
276UbiquitinationNTKPDYQKILQNQSK
CCCCCHHHHHHCCCH		38.872190698
276 (in isoform 1)Ubiquitination-38.8721890473
282PhosphorylationQKILQNQSKVFDCME
HHHHHCCCHHHHHHH		38.0323898821
322UbiquitinationKVSVQLGKRSMQQLD
HHHHHHHHHHHHHCC		50.30-
325SulfoxidationVQLGKRSMQQLDPSP
HHHHHHHHHHCCCCH		3.2321406390
331PhosphorylationSMQQLDPSPARKLLK
HHHHCCCCHHHHHHH		30.7523401153
338UbiquitinationSPARKLLKLQLQNPP
CHHHHHHHHHCCCCC		44.62-
338SumoylationSPARKLLKLQLQNPP
CHHHHHHHHHCCCCC		44.62-
338SumoylationSPARKLLKLQLQNPP
CHHHHHHHHHCCCCC		44.62-
350PhosphorylationNPPAIHGSGSGSCQ-
CCCCCCCCCCCCCC-		18.6725159151
352PhosphorylationPAIHGSGSGSCQ---
CCCCCCCCCCCC---		29.2729116813
354PhosphorylationIHGSGSGSCQ-----
CCCCCCCCCC-----		15.8425159151
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
100SPhosphorylationKinaseAURKBQ96GD4
GPS
109SPhosphorylationKinaseAURKBQ96GD4
GPS
331SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DSN1_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 DSN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSL1_HUMANNSL1physical
15502821
KNL1_HUMANCASC5physical
15502821
MIS12_HUMANMIS12physical
15502821
CBX3_HUMANCBX3physical
15502821
PMF1_HUMANPMF1physical
15502821
CBX5_HUMANCBX5physical
15502821
NSL1_HUMANNSL1physical
20231385
HS90A_HUMANHSP90AA1physical
20404110
SGT1_HUMANSUGT1physical
20404110
NSL1_HUMANNSL1physical
20404110
PMF1_HUMANPMF1physical
20404110
MIS12_HUMANMIS12physical
20404110
A4_HUMANAPPphysical
21832049
SGT1_HUMANSUGT1physical
22869522
BRE1A_HUMANRNF20physical
26186194
BRE1B_HUMANRNF40physical
26186194
KNL1_HUMANCASC5physical
26186194
SPC25_HUMANSPC25physical
26186194
EXOC7_HUMANEXOC7physical
26186194
BRCA2_HUMANBRCA2physical
26186194
SPC24_HUMANSPC24physical
26186194
NDC80_HUMANNDC80physical
26186194
PMF1_HUMANPMF1physical
26186194
CBX5_HUMANCBX5physical
26186194
MIS12_HUMANMIS12physical
26186194
EXOC5_HUMANEXOC5physical
26186194
EXOC6_HUMANEXOC6physical
26186194
NUF2_HUMANNUF2physical
26186194
SALL1_HUMANSALL1physical
26186194
SPF27_HUMANBCAS2physical
26186194
FHL2_HUMANFHL2physical
26186194
P73_HUMANTP73physical
26186194
COPA_HUMANCOPAphysical
26496610
PCNA_HUMANPCNAphysical
26496610
PML_HUMANPMLphysical
26496610
TTC3_HUMANTTC3physical
26496610
CTDP1_HUMANCTDP1physical
26496610
NDC80_HUMANNDC80physical
26496610
ZWINT_HUMANZWINTphysical
26496610
PMF1_HUMANPMF1physical
26496610
CBX5_HUMANCBX5physical
26496610
NSL1_HUMANNSL1physical
26496610
UBR5_HUMANUBR5physical
26496610
RPC2_HUMANPOLR3Bphysical
26496610
KNL1_HUMANCASC5physical
26496610
SPC25_HUMANSPC25physical
26496610
MIS12_HUMANMIS12physical
26496610
ICE2_HUMANICE2physical
26496610
NUF2_HUMANNUF2physical
26496610
C102A_HUMANCCDC102Aphysical
26496610
SPC24_HUMANSPC24physical
26496610
SPC25_HUMANSPC25physical
28514442
SPC24_HUMANSPC24physical
28514442
MIS12_HUMANMIS12physical
28514442
KNL1_HUMANCASC5physical
28514442
NDC80_HUMANNDC80physical
28514442
NUF2_HUMANNUF2physical
28514442
SALL1_HUMANSALL1physical
28514442
EXOC7_HUMANEXOC7physical
28514442
EXOC5_HUMANEXOC5physical
28514442
CBX5_HUMANCBX5physical
28514442
EXOC6_HUMANEXOC6physical
28514442
FHL2_HUMANFHL2physical
28514442
BRE1B_HUMANRNF40physical
28514442
BRE1A_HUMANRNF20physical
28514442
BRCA2_HUMANBRCA2physical
28514442
SPF27_HUMANBCAS2physical
28514442
SALL2_HUMANSALL2physical
28514442
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 DSN1_HUMAN

loading...

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-30, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND THR-245, ANDMASS 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-28; SER-30; SER-77 ANDSER-81, AND MASS SPECTROMETRY.
"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-86, AND MASSSPECTROMETRY.
"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-7; THR-38; SER-41;SER-49; SER-68; SER-77; SER-81; SER-123; SER-125; SER-244 AND SER-331,AND MASS SPECTROMETRY.
"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-28 AND SER-30, 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-86, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory