RBMS1_HUMAN - dbPTM
RBMS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBMS1_HUMAN
UniProt AC P29558
Protein Name RNA-binding motif, single-stranded-interacting protein 1
Gene Name RBMS1
Organism Homo sapiens (Human).
Sequence Length 406
Subcellular Localization Nucleus.
Protein Description Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication..
Protein Sequence MGKVWKQQMYPQYATYYYPQYLQAKQSLVPAHPMAPPSPSTTSSNNNSSSSSNSGWDQLSKTNLYIRGLPPHTTDQDLVKLCQPYGKIVSTKAILDKTTNKCKGYGFVDFDSPAAAQKAVSALKASGVQAQMAKQQEQDPTNLYISNLPLSMDEQELENMLKPFGQVISTRILRDSSGTSRGVGFARMESTEKCEAVIGHFNGKFIKTPPGVSAPTEPLLCKFADGGQKKRQNPNKYIPNGRPWHREGEVRLAGMTLTYDPTTAAIQNGFYPSPYSIATNRMITQTSITPYIASPVSAYQVQSPSWMQPQPYILQHPGAVLTPSMEHTMSLQPASMISPLAQQMSHLSLGSTGTYMPATSAMQGAYLPQYAHMQTTAVPVEEASGQQQVAVETSNDHSPYTFQPNK
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
10PhosphorylationKVWKQQMYPQYATYY
HHHHHHCCHHHHHHC		5.26-
13PhosphorylationKQQMYPQYATYYYPQ
HHHCCHHHHHHCCHH		9.08-
15PhosphorylationQMYPQYATYYYPQYL
HCCHHHHHHCCHHHH		13.71-
16PhosphorylationMYPQYATYYYPQYLQ
CCHHHHHHCCHHHHH		7.88-
17PhosphorylationYPQYATYYYPQYLQA
CHHHHHHCCHHHHHH		12.33-
27PhosphorylationQYLQAKQSLVPAHPM
HHHHHHHCCCCCCCC		30.5422199227
38PhosphorylationAHPMAPPSPSTTSSN
CCCCCCCCCCCCCCC		30.3523401153
38 (in isoform 2)Phosphorylation-30.35-
40PhosphorylationPMAPPSPSTTSSNNN
CCCCCCCCCCCCCCC		48.9725159151
41PhosphorylationMAPPSPSTTSSNNNS
CCCCCCCCCCCCCCC		33.8025159151
42PhosphorylationAPPSPSTTSSNNNSS
CCCCCCCCCCCCCCC		34.2025159151
43PhosphorylationPPSPSTTSSNNNSSS
CCCCCCCCCCCCCCC		31.0225159151
44PhosphorylationPSPSTTSSNNNSSSS
CCCCCCCCCCCCCCC		41.2925159151
48PhosphorylationTTSSNNNSSSSSNSG
CCCCCCCCCCCCCCC		33.4526329039
49PhosphorylationTSSNNNSSSSSNSGW
CCCCCCCCCCCCCCH		36.0426329039
50PhosphorylationSSNNNSSSSSNSGWD
CCCCCCCCCCCCCHH		37.2926329039
51PhosphorylationSNNNSSSSSNSGWDQ
CCCCCCCCCCCCHHH		35.1723663014
52PhosphorylationNNNSSSSSNSGWDQL
CCCCCCCCCCCHHHH		36.6423663014
54PhosphorylationNSSSSSNSGWDQLSK
CCCCCCCCCHHHHHH		43.1129978859
60PhosphorylationNSGWDQLSKTNLYIR
CCCHHHHHHCCEEEC		31.6229978859
80AcetylationTTDQDLVKLCQPYGK
CCHHHHHHHHHCCCC		51.3326051181
80UbiquitinationTTDQDLVKLCQPYGK
CCHHHHHHHHHCCCC		51.33-
85PhosphorylationLVKLCQPYGKIVSTK
HHHHHHCCCCEEEEH		12.7429496907
87AcetylationKLCQPYGKIVSTKAI
HHHHCCCCEEEEHHH		33.8126051181
87UbiquitinationKLCQPYGKIVSTKAI
HHHHCCCCEEEEHHH		33.81-
90PhosphorylationQPYGKIVSTKAILDK
HCCCCEEEEHHHHHC		27.8823403867
91PhosphorylationPYGKIVSTKAILDKT
CCCCEEEEHHHHHCC		17.3823403867
97MalonylationSTKAILDKTTNKCKG
EEHHHHHCCCCCCCC		54.5326320211
97UbiquitinationSTKAILDKTTNKCKG
EEHHHHHCCCCCCCC		54.53-
98PhosphorylationTKAILDKTTNKCKGY
EHHHHHCCCCCCCCC		34.96-
99PhosphorylationKAILDKTTNKCKGYG
HHHHHCCCCCCCCCC		38.12-
105PhosphorylationTTNKCKGYGFVDFDS
CCCCCCCCCCCCCCC		7.9020090780
112 (in isoform 2)Phosphorylation-19.21-
112PhosphorylationYGFVDFDSPAAAQKA
CCCCCCCCHHHHHHH		19.2130266825
118UbiquitinationDSPAAAQKAVSALKA
CCHHHHHHHHHHHHH		46.13-
124UbiquitinationQKAVSALKASGVQAQ
HHHHHHHHHHHHHHH		39.98-
132SulfoxidationASGVQAQMAKQQEQD
HHHHHHHHHHHHCCC		5.8830846556
169PhosphorylationKPFGQVISTRILRDS
HHHHHEEEEEEEECC		16.8722210691
170PhosphorylationPFGQVISTRILRDSS
HHHHEEEEEEEECCC		15.5922210691
176PhosphorylationSTRILRDSSGTSRGV
EEEEEECCCCCCCCC		25.0023403867
179PhosphorylationILRDSSGTSRGVGFA
EEECCCCCCCCCCEE		19.7322210691
180PhosphorylationLRDSSGTSRGVGFAR
EECCCCCCCCCCEEE		30.4822210691
190PhosphorylationVGFARMESTEKCEAV
CCEEECCCHHHCCEE		32.3030624053
204AcetylationVIGHFNGKFIKTPPG
EEEECCCEEECCCCC		45.0525953088
207UbiquitinationHFNGKFIKTPPGVSA
ECCCEEECCCCCCCC		59.10-
208PhosphorylationFNGKFIKTPPGVSAP
CCCEEECCCCCCCCC		29.8725159151
208 (in isoform 2)Phosphorylation-29.87-
213PhosphorylationIKTPPGVSAPTEPLL
ECCCCCCCCCCCCCE		34.1522199227
216PhosphorylationPPGVSAPTEPLLCKF
CCCCCCCCCCCEEEE		50.3729396449
222AcetylationPTEPLLCKFADGGQK
CCCCCEEEECCCCCC		43.4826051181
236 (in isoform 2)Ubiquitination-45.9021890473
236UbiquitinationKKRQNPNKYIPNGRP
CCCCCCCCCCCCCCC		45.902189047
236 (in isoform 1)Ubiquitination-45.9021890473
253 (in isoform 2)Phosphorylation-8.6424043423
255 (in isoform 2)Phosphorylation-2.0024043423
256 (in isoform 2)Phosphorylation-18.2824043423
259 (in isoform 2)Phosphorylation-24.0424043423
260 (in isoform 2)Phosphorylation-28.9124043423
268 (in isoform 2)Phosphorylation-36.1122199227
270 (in isoform 2)Phosphorylation-12.1322199227
271PhosphorylationAAIQNGFYPSPYSIA
HHHHCCCCCCCCCCC		12.2822199227
272 (in isoform 2)Phosphorylation-26.9422199227
273PhosphorylationIQNGFYPSPYSIATN
HHCCCCCCCCCCCCC		25.7022199227
273 (in isoform 2)Phosphorylation-25.7024043423
275PhosphorylationNGFYPSPYSIATNRM
CCCCCCCCCCCCCCC		19.6222199227
276 (in isoform 2)Phosphorylation-14.7724043423
276PhosphorylationGFYPSPYSIATNRMI
CCCCCCCCCCCCCCE		14.7722199227
338PhosphorylationLQPASMISPLAQQMS
CCCHHHHHHHHHHHH		12.7626074081
393PhosphorylationQQQVAVETSNDHSPY
CEEEEEEECCCCCCC		26.6526074081
394PhosphorylationQQVAVETSNDHSPYT
EEEEEEECCCCCCCC		27.1026074081
398PhosphorylationVETSNDHSPYTFQPN
EEECCCCCCCCCCCC		23.5926074081
400PhosphorylationTSNDHSPYTFQPNK-
ECCCCCCCCCCCCC-		24.1726074081
401PhosphorylationSNDHSPYTFQPNK--
CCCCCCCCCCCCC--		21.1226074081
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 RBMS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBMS1_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 RBMS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOSB1_HUMANNABP2physical
22939629
TIM44_HUMANTIMM44physical
22939629
RS19_HUMANRPS19physical
22939629
RM53_HUMANMRPL53physical
22939629
SUGP1_HUMANSUGP1physical
22939629
RL38_HUMANRPL38physical
22939629
SNX3_HUMANSNX3physical
22939629
SARNP_HUMANSARNPphysical
22939629
UBC9_HUMANUBE2Iphysical
22939629
RU1C_HUMANSNRPCphysical
22939629
RRFM_HUMANMRRFphysical
22939629
SRPRB_HUMANSRPRBphysical
22939629
RFX5_HUMANRFX5physical
22939629
RIDA_HUMANHRSP12physical
22939629
UBQL1_HUMANUBQLN1physical
22939629
RRBP1_HUMANRRBP1physical
22939629
STX7_HUMANSTX7physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
SBDS_HUMANSBDSphysical
22939629
TFCP2_HUMANTFCP2physical
25416956
ZN143_HUMANZNF143physical
27173435
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 RBMS1_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-112, AND MASSSPECTROMETRY.
"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-112, AND MASSSPECTROMETRY.
"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-112 AND THR-208, ANDMASS SPECTROMETRY.

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