SSBP2_HUMAN - dbPTM
SSBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSBP2_HUMAN
UniProt AC P81877
Protein Name Single-stranded DNA-binding protein 2
Gene Name SSBP2
Organism Homo sapiens (Human).
Sequence Length 361
Subcellular Localization Nucleus.
Protein Description
Protein Sequence MYGKGKSNSSAVPSDSQAREKLALYVYEYLLHVGAQKSAQTFLSEIRWEKNITLGEPPGFLHSWWCVFWDLYCAAPERRETCEHSSEAKAFHDYSAAAAPSPVLGNIPPGDGMPVGPVPPGFFQPFMSPRYPGGPRPPLRIPNQALGGVPGSQPLLPSGMDPTRQQGHPNMGGPMQRMTPPRGMVPLGPQNYGGAMRPPLNALGGPGMPGMNMGPGGGRPWPNPTNANSIPYSSASPGNYVGPPGGGGPPGTPIMPSPADSTNSGDNMYTLMNAVPPGPNRPNFPMGPGSDGPMGGLGGMESHHMNGSLGSGDMDSISKNSPNNMSLSNQPGTPRDDGEMGGNFLNPFQSESYSPSMTMSV
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
1Acetylation-------MYGKGKSN
-------CCCCCCCC		10.06-
4Ubiquitination----MYGKGKSNSSA
----CCCCCCCCCCC		45.75-
6Acetylation--MYGKGKSNSSAVP
--CCCCCCCCCCCCC		50.37-
6Ubiquitination--MYGKGKSNSSAVP
--CCCCCCCCCCCCC		50.37-
9PhosphorylationYGKGKSNSSAVPSDS
CCCCCCCCCCCCCCH		27.11-
14PhosphorylationSNSSAVPSDSQAREK
CCCCCCCCCHHHHHH		43.21-
21UbiquitinationSDSQAREKLALYVYE
CCHHHHHHHHHHHHH		33.24-
25PhosphorylationAREKLALYVYEYLLH
HHHHHHHHHHHHHHH		8.7222817900
27PhosphorylationEKLALYVYEYLLHVG
HHHHHHHHHHHHHHC		5.8218080319
38PhosphorylationLHVGAQKSAQTFLSE
HHHCCHHHHHHHHHH		17.3322210691
44PhosphorylationKSAQTFLSEIRWEKN
HHHHHHHHHHHHHCC		27.1324719451
130Asymmetric dimethylarginineFQPFMSPRYPGGPRP
CCCCCCCCCCCCCCC		42.86-
136Asymmetric dimethylargininePRYPGGPRPPLRIPN
CCCCCCCCCCCCCCC		49.06-
140Asymmetric dimethylarginineGGPRPPLRIPNQALG
CCCCCCCCCCCCCCC		48.36-
158PhosphorylationGSQPLLPSGMDPTRQ
CCCCCCCCCCCCCCC		46.8728787133
161 (in isoform 5)Phosphorylation-44.9727251275
166 (in isoform 5)Phosphorylation-49.2022210691
170 (in isoform 5)Phosphorylation-35.7422210691
192PhosphorylationVPLGPQNYGGAMRPP
CCCCCCCCCCCCCCC		16.2219658100
233O-linked_GlycosylationNANSIPYSSASPGNY
CCCCCCCCCCCCCCC		17.6730379171
234O-linked_GlycosylationANSIPYSSASPGNYV
CCCCCCCCCCCCCCC		27.2430379171
236O-linked_GlycosylationSIPYSSASPGNYVGP
CCCCCCCCCCCCCCC		34.9830379171
308PhosphorylationESHHMNGSLGSGDMD
CCCCCCCCCCCCCHH		25.26-
316PhosphorylationLGSGDMDSISKNSPN
CCCCCHHHCCCCCCC		23.3226074081
318PhosphorylationSGDMDSISKNSPNNM
CCCHHHCCCCCCCCC		29.7226074081
321PhosphorylationMDSISKNSPNNMSLS
HHHCCCCCCCCCCCC		32.5123927012
326PhosphorylationKNSPNNMSLSNQPGT
CCCCCCCCCCCCCCC		30.6723927012
328PhosphorylationSPNNMSLSNQPGTPR
CCCCCCCCCCCCCCC		26.5523927012
329PhosphorylationPNNMSLSNQPGTPRD
CCCCCCCCCCCCCCC		58.3127251275
333PhosphorylationSLSNQPGTPRDDGEM
CCCCCCCCCCCCCCC		23.1023927012
336PhosphorylationNQPGTPRDDGEMGGN
CCCCCCCCCCCCCCC		70.2627251275
341PhosphorylationPRDDGEMGGNFLNPF
CCCCCCCCCCCCCCC		24.4827251275
350PhosphorylationNFLNPFQSESYSPSM
CCCCCCCCCCCCCCC		28.9626074081
352PhosphorylationLNPFQSESYSPSMTM
CCCCCCCCCCCCCCC		35.8426074081
353PhosphorylationNPFQSESYSPSMTMS
CCCCCCCCCCCCCCC		22.1326074081
354PhosphorylationPFQSESYSPSMTMSV
CCCCCCCCCCCCCCC		21.5626074081
356PhosphorylationQSESYSPSMTMSV--
CCCCCCCCCCCCC--		22.4226074081
358PhosphorylationESYSPSMTMSV----
CCCCCCCCCCC----		15.6126074081
360PhosphorylationYSPSMTMSV------
CCCCCCCCC------		18.6026055452
362PhosphorylationPSMTMSV--------
CCCCCCC--------		27251275
368PhosphorylationV--------------
C--------------		27251275
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 SSBP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSBP2_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 SSBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
I36RA_HUMANIL36RNphysical
16189514
RBTN2_HUMANLMO2physical
17437998
TOM1_HUMANTOM1physical
21988832
LDB1_HUMANLDB1physical
26186194
ISL2_HUMANISL2physical
26186194
ISL1_HUMANISL1physical
26186194
SSBP4_HUMANSSBP4physical
26186194
SSBP3_HUMANSSBP3physical
26186194
CL18A_HUMANCLEC18Aphysical
26186194
LMO4_HUMANLMO4physical
26186194
LHX4_HUMANLHX4physical
26186194
PIN1_HUMANPIN1physical
21516116
SSBP3_HUMANSSBP3physical
28514442
SSBP4_HUMANSSBP4physical
28514442
ISL2_HUMANISL2physical
28514442
LDB1_HUMANLDB1physical
28514442
LMO4_HUMANLMO4physical
28514442
CL18A_HUMANCLEC18Aphysical
28514442
ISL1_HUMANISL1physical
28514442
LHX4_HUMANLHX4physical
28514442
ARHGA_HUMANARHGEF10physical
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 SSBP2_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-321 AND THR-333, ANDMASS SPECTROMETRY.

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