RBM45_HUMAN - dbPTM
RBM45_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM45_HUMAN
UniProt AC Q8IUH3
Protein Name RNA-binding protein 45
Gene Name RBM45
Organism Homo sapiens (Human).
Sequence Length 476
Subcellular Localization Cytoplasm . Nucleus . Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus.
Protein Description RNA-binding protein with binding specificity for poly(C). May play an important role in neural development..
Protein Sequence MDEAGSSASGGGFRPGVDSLDEPPNSRIFLVISKYTPESVLRERFSPFGDIQDIWVVRDKHTKESKGIAFVKFARSSQACRAMEEMHGQCLGPNDTKPIKVFIAQSRSSGSHRDVEDEELTRIFVMIPKSYTEEDLREKFKVYGDIEYCSIIKNKVTGESKGLGYVRYLKPSQAAQAIENCDRSFRAILAEPKNKASESSEQDYYSNMRQEALGHEPRVNMFPFVGEQQSEFSSFDKNDSRGQEAISKRLSVVSRVPFTEEQLFSIFDIVPGLEYCEVQRDPYSNYGHGVVQYFNVASAIYAKYKLHGFQYPPGNRIGVSFIDDGSNATDLLRKMATQMVAAQLASMVWNNPSQQQFMQFGGSSGSQLPQIQTDVVLPSCKKKAPAETPVKERLFIVFNPHPLPLDVLEDIFCRFGNLIEVYLVSGKNVGYAKYADRISANDAIATLHGKILNGVRLKVMLADSPREESNKRQRTY
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
6Phosphorylation--MDEAGSSASGGGF
--CCCCCCCCCCCCC		29.7627251275
7Phosphorylation-MDEAGSSASGGGFR
-CCCCCCCCCCCCCC		26.0727251275
9PhosphorylationDEAGSSASGGGFRPG
CCCCCCCCCCCCCCC		39.6628348404
34SumoylationRIFLVISKYTPESVL
EEEEEEECCCCHHHH		41.8628112733
46PhosphorylationSVLRERFSPFGDIQD
HHHHHCCCCCCCCEE		26.0720068231
97AcetylationCLGPNDTKPIKVFIA
CCCCCCCCCEEEEEE		47.8327452117
143PhosphorylationLREKFKVYGDIEYCS
HHHHCEEECCEEEEE		15.07-
150PhosphorylationYGDIEYCSIIKNKVT
ECCEEEEEEEECCCC		26.8424719451
153AcetylationIEYCSIIKNKVTGES
EEEEEEEECCCCCCC		49.3926051181
161AcetylationNKVTGESKGLGYVRY
CCCCCCCCCCCCEEE		54.587965505
161UbiquitinationNKVTGESKGLGYVRY
CCCCCCCCCCCCEEE		54.5829967540
165PhosphorylationGESKGLGYVRYLKPS
CCCCCCCCEEEECHH		6.18-
170 (in isoform 3)Ubiquitination-33.42-
170UbiquitinationLGYVRYLKPSQAAQA
CCCEEEECHHHHHHH		33.4229967540
184PhosphorylationAIENCDRSFRAILAE
HHHHCCHHHHHHHCC		13.0630576142
193UbiquitinationRAILAEPKNKASESS
HHHHCCCCCCCCCCC		63.6929967540
199PhosphorylationPKNKASESSEQDYYS
CCCCCCCCCHHHHHH		36.3630576142
200PhosphorylationKNKASESSEQDYYSN
CCCCCCCCHHHHHHH		34.9127251275
204PhosphorylationSESSEQDYYSNMRQE
CCCCHHHHHHHHHHH		14.4227642862
205PhosphorylationESSEQDYYSNMRQEA
CCCHHHHHHHHHHHH		11.2327642862
228 (in isoform 2)Phosphorylation-46.2821406692
228 (in isoform 3)Phosphorylation-46.2821406692
231 (in isoform 2)Phosphorylation-45.2521406692
231 (in isoform 3)Phosphorylation-45.2521406692
232 (in isoform 2)Phosphorylation-10.0521406692
232 (in isoform 3)Phosphorylation-10.0521406692
235UbiquitinationQQSEFSSFDKNDSRG
CHHHCCCCCCCCCHH		17.5529967540
235 (in isoform 2)Ubiquitination-17.5521906983
235 (in isoform 3)Ubiquitination-17.5521906983
237UbiquitinationSEFSSFDKNDSRGQE
HHCCCCCCCCCHHHH		61.72-
240PhosphorylationSSFDKNDSRGQEAIS
CCCCCCCCHHHHHHH		47.9429978859
388PhosphorylationKKKAPAETPVKERLF
CCCCCCCCCCCEEEE		35.1728555341
422PhosphorylationFGNLIEVYLVSGKNV
HCCEEEEEEECCCCC		6.6517053785
431PhosphorylationVSGKNVGYAKYADRI
ECCCCCCHHHHHHHC		8.8117053785
431UbiquitinationVSGKNVGYAKYADRI
ECCCCCCHHHHHHHC		8.8129967540
434PhosphorylationKNVGYAKYADRISAN
CCCCHHHHHHHCCCC		12.9317053785
439PhosphorylationAKYADRISANDAIAT
HHHHHHCCCCHHHHH		23.16-
462PhosphorylationVRLKVMLADSPREES
CEEEEEECCCCCHHH		9.3518691976
464PhosphorylationLKVMLADSPREESNK
EEEEECCCCCHHHHC		21.9030266825
469PhosphorylationADSPREESNKRQRTY
CCCCCHHHHCCCCCC		42.7923186163
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 RBM45_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM45_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 RBM45_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM45_HUMANRBM45physical
25416956
ECT2_HUMANECT2physical
26496610
KIF22_HUMANKIF22physical
26496610
PPM1G_HUMANPPM1Gphysical
26496610
ATPK_HUMANATP5J2physical
26496610
AFG32_HUMANAFG3L2physical
26496610
FND3A_HUMANFNDC3Aphysical
26496610
PUM2_HUMANPUM2physical
26496610
CTBL1_HUMANCTNNBL1physical
26496610
DOT1L_HUMANDOT1Lphysical
26496610
RUSD4_HUMANRPUSD4physical
26496610
K2013_HUMANKIAA2013physical
26496610
KMT2D_HUMANKMT2Dphysical
26496610
KEAP1_HUMANKEAP1physical
25939382
NF2L2_HUMANNFE2L2physical
25939382
SQSTM_HUMANSQSTM1physical
25939382
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 RBM45_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-422; TYR-431 ANDTYR-434, AND MASS SPECTROMETRY.

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