DUS11_HUMAN - dbPTM
DUS11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS11_HUMAN
UniProt AC O75319
Protein Name RNA/RNP complex-1-interacting phosphatase
Gene Name DUSP11
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Possesses RNA 5'-triphosphatase and diphosphatase activities, but displays a poor protein-tyrosine phosphatase activity. In addition, has phosphatase activity with ATP, ADP and O-methylfluorescein phosphate (in vitro). Binds to RNA. May participate in nuclear mRNA metabolism..
Protein Sequence MRNSETLERGVGGCRVFSCLGSYPGIEGAGLALLADLALGGRLLGTHMSQWHHPRSGWGRRRDFSGRSSAKKKGGNHIPERWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLKIFTVGHQVPDDETIFKFKHAVNGFLKENKDNDKLIGVHCTHGLNRTGYLICRYLIDVEGVRPDDAIELFNRCRGHCLERQNYIEDLQNGPIRKNWNSSVPRSSDFEDSAHLMQPVHNKPVKQGPRYNLHQIQGHSAPRHFHTQTQSLQQSVRKFSENPHVYQRHHLPPPGPPGEDYSHRRYSWNVKPNASRAAQDRRRWYPYNYSRLSYPACWEWTQ
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
8MethylationMRNSETLERGVGGCR
CCCHHHHHCCCCCCC
43.37-
18PhosphorylationVGGCRVFSCLGSYPG
CCCCCHHHCCCCCCC
37.2728102081
21PhosphorylationCRVFSCLGSYPGIEG
CCHHHCCCCCCCCCC
37.8728102081
22PhosphorylationRVFSCLGSYPGIEGA
CHHHCCCCCCCCCCH
42.6228102081
36UbiquitinationAGLALLADLALGGRL
HHHHHHHHHHHHCHH
42.59-
38PhosphorylationLALLADLALGGRLLG
HHHHHHHHHHCHHHH
14.8029496907
54SumoylationHMSQWHHPRSGWGRR
CHHCCCCCCCCCCCC
33.64-
54UbiquitinationHMSQWHHPRSGWGRR
CHHCCCCCCCCCCCC
33.64-
55MethylationMSQWHHPRSGWGRRR
HHCCCCCCCCCCCCC
4.64-
59UbiquitinationHHPRSGWGRRRDFSG
CCCCCCCCCCCCCCC
65.87-
64UbiquitinationGWGRRRDFSGRSSAK
CCCCCCCCCCCCCCC
42.56-
64SumoylationGWGRRRDFSGRSSAK
CCCCCCCCCCCCCCC
42.56-
79UbiquitinationKKGGNHIPERWKDYL
CCCCCCCCHHHHHCC
35.49-
83UbiquitinationNHIPERWKDYLPVGQ
CCCCHHHHHCCCCCC
53.43-
99PhosphorylationMPGTRFIAFKVPLQK
CCCCEEEEEECCCHH
13.1628152594
100PhosphorylationPGTRFIAFKVPLQKS
CCCEEEEEECCCHHH
23.4328152594
101UbiquitinationGTRFIAFKVPLQKSF
CCEEEEEECCCHHHH
32.75-
101SumoylationGTRFIAFKVPLQKSF
CCEEEEEECCCHHHH
32.75-
101SumoylationGTRFIAFKVPLQKSF
CCEEEEEECCCHHHH
32.75-
106UbiquitinationAFKVPLQKSFEKKLA
EEECCCHHHHHHHCC
47.75-
111SumoylationLQKSFEKKLAPEECF
CHHHHHHHCCCHHHC
19.11-
111UbiquitinationLQKSFEKKLAPEECF
CHHHHHHHCCCHHHC
19.1122505724
126UbiquitinationSPLDLFNKIREQNEE
CHHHHHHHHHHHHHH
38.41-
129UbiquitinationDLFNKIREQNEELGL
HHHHHHHHHHHHHCE
50.05-
129AcetylationDLFNKIREQNEELGL
HHHHHHHHHHHHHCE
50.0526051181
129SumoylationDLFNKIREQNEELGL
HHHHHHHHHHHHHCE
50.05-
131SumoylationFNKIREQNEELGLII
HHHHHHHHHHHCEEE
31.11-
131UbiquitinationFNKIREQNEELGLII
HHHHHHHHHHHCEEE
31.11-
139SumoylationEELGLIIDLTYTQRY
HHHCEEEEEEEECCC
57.91-
148SumoylationTYTQRYYKPEDLPET
EEECCCCCHHHCCCC
7.16-
176UbiquitinationPDDETIFKFKHAVNG
CCCHHHHHHHHHHHH
47.62-
176SumoylationPDDETIFKFKHAVNG
CCCHHHHHHHHHHHH
47.62-
178SumoylationDETIFKFKHAVNGFL
CHHHHHHHHHHHHHH
12.44-
178UbiquitinationDETIFKFKHAVNGFL
CHHHHHHHHHHHHHH
12.44-
186SumoylationHAVNGFLKENKDNDK
HHHHHHHHHCCCCCC
34.35-
186UbiquitinationHAVNGFLKENKDNDK
HHHHHHHHHCCCCCC
34.35-
206UbiquitinationCTHGLNRTGYLICRY
ECCCCCCCCCEEEEE
68.01-
216PhosphorylationLICRYLIDVEGVRPD
EEEEEEEECCCCCCH
47.8228787133
218PhosphorylationCRYLIDVEGVRPDDA
EEEEEECCCCCCHHH
14.0222798277
231 (in isoform 1)Ubiquitination-35.9921890473
231UbiquitinationDAIELFNRCRGHCLE
HHHHHHHHHHCHHHH
35.9921890473
234 (in isoform 1)Ubiquitination-59.0521890473
234UbiquitinationELFNRCRGHCLERQN
HHHHHHHCHHHHHCC
59.05-
248PhosphorylationNYIEDLQNGPIRKNW
CHHHHHHCCCCCCCC
46.9528555341
251MethylationEDLQNGPIRKNWNSS
HHHHCCCCCCCCCCC
44.83-
253UbiquitinationLQNGPIRKNWNSSVP
HHCCCCCCCCCCCCC
7.62-
255PhosphorylationNGPIRKNWNSSVPRS
CCCCCCCCCCCCCCC
32.1624043423
257PhosphorylationPIRKNWNSSVPRSSD
CCCCCCCCCCCCCCC
22.6824043423
259PhosphorylationRKNWNSSVPRSSDFE
CCCCCCCCCCCCCCC
31.3724043423
263PhosphorylationNSSVPRSSDFEDSAH
CCCCCCCCCCCCCCH
15.7828555341
265MethylationSVPRSSDFEDSAHLM
CCCCCCCCCCCCHHC
39.28-
266MethylationVPRSSDFEDSAHLMQ
CCCCCCCCCCCHHCC
51.60-
266UbiquitinationVPRSSDFEDSAHLMQ
CCCCCCCCCCCHHCC
51.60-
266SumoylationVPRSSDFEDSAHLMQ
CCCCCCCCCCCHHCC
51.60-
268PhosphorylationRSSDFEDSAHLMQPV
CCCCCCCCCHHCCCC
39.2328555341
274PhosphorylationDSAHLMQPVHNKPVK
CCCHHCCCCCCCCCC
9.2227642862
278UbiquitinationLMQPVHNKPVKQGPR
HCCCCCCCCCCCCCC
42.0721890473
281UbiquitinationPVHNKPVKQGPRYNL
CCCCCCCCCCCCCCC
53.49-
289PhosphorylationQGPRYNLHQIQGHSA
CCCCCCCHHCCCCCC
11.32-
290PhosphorylationGPRYNLHQIQGHSAP
CCCCCCHHCCCCCCC
23.88-
294PhosphorylationNLHQIQGHSAPRHFH
CCHHCCCCCCCCHHH
20.2829496907
295PhosphorylationLHQIQGHSAPRHFHT
CHHCCCCCCCCHHHH
15.4627067055
298MethylationIQGHSAPRHFHTQTQ
CCCCCCCCHHHHHHH
9.92-
299UbiquitinationQGHSAPRHFHTQTQS
CCCCCCCHHHHHHHH
29.37-
299AcetylationQGHSAPRHFHTQTQS
CCCCCCCHHHHHHHH
29.3726051181
299SumoylationQGHSAPRHFHTQTQS
CCCCCCCHHHHHHHH
29.37-
312MethylationQSLQQSVRKFSENPH
HHHHHHHHHHHCCCC
9.17-
313SumoylationSLQQSVRKFSENPHV
HHHHHHHHHHCCCCH
8.27-
313MethylationSLQQSVRKFSENPHV
HHHHHHHHHHCCCCH
8.27-
313PhosphorylationSLQQSVRKFSENPHV
HHHHHHHHHHCCCCH
8.2728152594
313UbiquitinationSLQQSVRKFSENPHV
HHHHHHHHHHCCCCH
8.27-
315PhosphorylationQQSVRKFSENPHVYQ
HHHHHHHHCCCCHHH
15.8426074081
317PhosphorylationSVRKFSENPHVYQRH
HHHHHHCCCCHHHCC
6.8526074081
318PhosphorylationVRKFSENPHVYQRHH
HHHHHCCCCHHHCCC
24.0926074081
336PhosphorylationPGPPGEDYSHRRYSW
CCCCCCCCCCCCCEE
-
337PhosphorylationGPPGEDYSHRRYSWN
CCCCCCCCCCCCEEC
-
342PhosphorylationDYSHRRYSWNVKPNA
CCCCCCCEECCCCCC
27251275
346SumoylationRRYSWNVKPNASRAA
CCCEECCCCCCHHHH
-
346UbiquitinationRRYSWNVKPNASRAA
CCCEECCCCCCHHHH
-

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 DUS11_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS11_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 DUS11_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRSF9_HUMANSRSF9physical
9685386
SYQ_HUMANQARSphysical
16169070
NIPA4_HUMANNIPAL4physical
27432908
DUS11_HUMANDUSP11physical
27432908
RS15_HUMANRPS15physical
27432908
RT35_HUMANMRPS35physical
27432908
RM04_HUMANMRPL4physical
27432908
RM15_HUMANMRPL15physical
27432908
RT15_HUMANMRPS15physical
27432908
RM19_HUMANMRPL19physical
27432908
RT29_HUMANDAP3physical
27432908
RT07_HUMANMRPS7physical
27432908
RT02_HUMANMRPS2physical
27432908
RL36L_HUMANRPL36ALphysical
27432908
RM22_HUMANMRPL22physical
27432908
TEBP_HUMANPTGES3physical
27432908
RM21_HUMANMRPL21physical
27432908
RM24_HUMANMRPL24physical
27432908
RM50_HUMANMRPL50physical
27432908
RT26_HUMANMRPS26physical
27432908
RM44_HUMANMRPL44physical
27432908
RT25_HUMANMRPS25physical
27432908
RM38_HUMANMRPL38physical
27432908
RT10_HUMANMRPS10physical
27432908
RT16_HUMANMRPS16physical
27432908
RT21_HUMANMRPS21physical
27432908
RM18_HUMANMRPL18physical
27432908
RM13_HUMANMRPL13physical
27432908
RT11_HUMANMRPS11physical
27432908
RL32_HUMANRPL32physical
27432908

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUS11_HUMAN

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Related Literatures of Post-Translational Modification

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