SMBP2_HUMAN - dbPTM
SMBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMBP2_HUMAN
UniProt AC P38935
Protein Name DNA-binding protein SMUBP-2
Gene Name IGHMBP2
Organism Homo sapiens (Human).
Sequence Length 993
Subcellular Localization Nucleus . Cytoplasm . Cell projection, axon. Colocalizes with the translation initiation factor EIF4G2..
Protein Description 5' to 3' helicase that unwinds RNA and DNA duplices in an ATP-dependent reaction. Acts as a transcription regulator. Required for the transcriptional activation of the flounder liver-type antifreeze protein gene. Exhibits strong binding specificity to the enhancer element B of the flounder antifreeze protein gene intron. Binds to the insulin II gene RIPE3B enhancer region. May be involved in translation (By similarity). DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence related to the immunoglobulin mu chain switch region. Preferentially binds to the 5'-GGGCT-3' motif. Interacts with tRNA-Tyr. Stimulates the transcription of the human neurotropic virus JCV..
Protein Sequence MASAAVESFVTKQLDLLELERDAEVEERRSWQENISLKELQSRGVCLLKLQVSSQRTGLYGRLLVTFEPRRYGSAAALPSNSFTSGDIVGLYDAANEGSQLATGILTRVTQKSVTVAFDESHDFQLSLDRENSYRLLKLANDVTYRRLKKALIALKKYHSGPASSLIEVLFGRSAPSPASEIHPLTFFNTCLDTSQKEAVLFALSQKELAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKQRILRLGHPARLLESIQQHSLDAVLARSDSAQIVADIRKDIDQVFVKNKKTQDKREKSNFRNEIKLLRKELKEREEAAMLESLTSANVVLATNTGASADGPLKLLPESYFDVVVIDECAQALEASCWIPLLKARKCILAGDHKQLPPTTVSHKAALAGLSLSLMERLAEEYGARVVRTLTVQYRMHQAIMRWASDTMYLGQLTAHSSVARHLLRDLPGVAATEETGVPLLLVDTAGCGLFELEEEDEQSKGNPGEVRLVSLHIQALVDAGVPARDIAVVSPYNLQVDLLRQSLVHRHPELEIKSVDGFQGREKEAVILSFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSRTVNNHAFLKTLVEYFTQHGEVRTAFEYLDDIVPENYSHENSQGSSHAATKPQGPATSTRTGSQRQEGGQEAAAPARQGRKKPAGKSLASEAPSQPSLNGGSPEGVESQDGVDHFRAMIVEFMASKKMQLEFPPSLNSHDRLRVHQIAEEHGLRHDSSGEGKRRFITVSKRAPRPRAALGPPAGTGGPAPLQPVPPTPAQTEQPPREQRGPDQPDLRTLHLERLQRVRSAQGQPASKEQQASGQQKLPEKKKKKAKGHPATDLPTEEDFEALVSAAVKADNTCGFAKCTAGVTTLGQFCQLCSRRYCLSHHLPEIHGCGERARAHARQRISREGVLYAGSGTKNGSLDPAKRAQLQRRLDKKLSELSNQRTSRRKERGT
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
2Acetylation------MASAAVESF
------CCHHHHHHH		14.1022223895
8PhosphorylationMASAAVESFVTKQLD
CCHHHHHHHHHHHHH		20.5829514088
11PhosphorylationAAVESFVTKQLDLLE
HHHHHHHHHHHHHHH		15.8629514088
30PhosphorylationAEVEERRSWQENISL
HHHHHHHHHHHHCCH		39.0520873877
36PhosphorylationRSWQENISLKELQSR
HHHHHHCCHHHHHHC		44.9924719451
38UbiquitinationWQENISLKELQSRGV
HHHHCCHHHHHHCCE		49.9829967540
85PhosphorylationLPSNSFTSGDIVGLY
CCCCCCCCCCEEEEE		32.24-
92PhosphorylationSGDIVGLYDAANEGS
CCCEEEEEECHHCCC		9.52-
138UbiquitinationENSYRLLKLANDVTY
CCHHHHHHHHCHHHH		50.5829967540
160PhosphorylationIALKKYHSGPASSLI
HHHHHHCCCCHHHHH		43.3025159151
218PhosphorylationIIHGPPGTGKTTTVV
EEECCCCCCHHHHHH		41.0822468782
237UbiquitinationQAVKQGLKVLCCAPS
HHHHCCCEEEEECCC		39.7329967540
259UbiquitinationVERLALCKQRILRLG
HHHHHHHHHHHHHCC		43.3829967540
279PhosphorylationLESIQQHSLDAVLAR
HHHHHHCCHHHHHHC		24.4928348404
289PhosphorylationAVLARSDSAQIVADI
HHHHCCCCHHHHHHH		24.2624532841
298UbiquitinationQIVADIRKDIDQVFV
HHHHHHHHHHHHHHH		60.4129967540
306UbiquitinationDIDQVFVKNKKTQDK
HHHHHHHHCCCCCCH		52.1429967540
324UbiquitinationSNFRNEIKLLRKELK
HHHHHHHHHHHHHHH		34.9829967540
394AcetylationIPLLKARKCILAGDH
HHHHHHCCEEECCCC		30.4111924091
394UbiquitinationIPLLKARKCILAGDH
HHHHHHCCEEECCCC		30.4129967540
402UbiquitinationCILAGDHKQLPPTTV
EEECCCCCCCCCCCC		59.2629967540
419PhosphorylationKAALAGLSLSLMERL
HHHHHHHCHHHHHHH		18.2628555341
421PhosphorylationALAGLSLSLMERLAE
HHHHHCHHHHHHHHH		23.4628555341
437PhosphorylationYGARVVRTLTVQYRM
HCCHHHHHHHHHHHH		18.3830622161
439PhosphorylationARVVRTLTVQYRMHQ
CHHHHHHHHHHHHHH		12.6330622161
539PhosphorylationARDIAVVSPYNLQVD
HHHEEEECCCCHHHH		18.3127251275
562AcetylationRHPELEIKSVDGFQG
HCCCCEEEEECCCCC		34.7425953088
572UbiquitinationDGFQGREKEAVILSF
CCCCCCEEEEEEEEE		50.0029967540
651PhosphorylationDDIVPENYSHENSQG
HHHCCCCCCCCCCCC		15.1128555341
652PhosphorylationDIVPENYSHENSQGS
HHCCCCCCCCCCCCC		35.5925627689
656PhosphorylationENYSHENSQGSSHAA
CCCCCCCCCCCCCCC		32.6917525332
675PhosphorylationGPATSTRTGSQRQEG
CCCCCCCCCCCCCCC		41.0728450419
677PhosphorylationATSTRTGSQRQEGGQ
CCCCCCCCCCCCCCC		22.9028450419
701PhosphorylationRKKPAGKSLASEAPS
CCCCCCCCCCCCCCC		28.4026074081
704PhosphorylationPAGKSLASEAPSQPS
CCCCCCCCCCCCCCC		39.3129496963
708PhosphorylationSLASEAPSQPSLNGG
CCCCCCCCCCCCCCC		62.8728450419
711PhosphorylationSEAPSQPSLNGGSPE
CCCCCCCCCCCCCCC		27.1623401153
716PhosphorylationQPSLNGGSPEGVESQ
CCCCCCCCCCCCCCC		22.6025159151
722PhosphorylationGSPEGVESQDGVDHF
CCCCCCCCCCCHHHH		31.0323663014
771PhosphorylationEHGLRHDSSGEGKRR
HHCCCCCCCCCCCEE		33.8328555341
843PhosphorylationERLQRVRSAQGQPAS
HHHHHHHHCCCCCCC		23.3022496350
945PhosphorylationAHARQRISREGVLYA
HHHHHHHCCCCEEEC		26.8624719451
951PhosphorylationISREGVLYAGSGTKN
HCCCCEEECCCCCCC		13.4029978859
954PhosphorylationEGVLYAGSGTKNGSL
CCEEECCCCCCCCCC		34.8121815630
956PhosphorylationVLYAGSGTKNGSLDP
EEECCCCCCCCCCCH		24.0429978859
960PhosphorylationGSGTKNGSLDPAKRA
CCCCCCCCCCHHHHH		38.7129978859
978PhosphorylationRRLDKKLSELSNQRT
HHHHHHHHHHHHHHH		45.4225954137
981PhosphorylationDKKLSELSNQRTSRR
HHHHHHHHHHHHHHH		27.1926074081
985PhosphorylationSELSNQRTSRRKERG
HHHHHHHHHHHHHCC		19.4726074081
986PhosphorylationELSNQRTSRRKERGT
HHHHHHHHHHHHCCC		32.0726074081
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 SMBP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMBP2_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 SMBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR89_HUMANWDR89physical
28514442
NLE1_HUMANNLE1physical
28514442
P52K_HUMANPRKRIRphysical
28514442
WDR12_HUMANWDR12physical
28514442
GRSF1_HUMANGRSF1physical
28514442
RL5_HUMANRPL5physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604320Neuronopathy, distal hereditary motor, 6 (HMN6)
616155Charcot-Marie-Tooth disease 2S (CMT2S)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMBP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656, AND MASSSPECTROMETRY.

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