SSBP_HUMAN - dbPTM
SSBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSBP_HUMAN
UniProt AC Q04837
Protein Name Single-stranded DNA-binding protein, mitochondrial
Gene Name SSBP1
Organism Homo sapiens (Human).
Sequence Length 148
Subcellular Localization Mitochondrion . Mitochondrion matrix, mitochondrion nucleoid .
Protein Description This protein binds preferentially and cooperatively to ss-DNA. Probably involved in mitochondrial DNA replication. Associates with mitochondrial DNA..
Protein Sequence MFRRPVLQVLRQFVRHESETTTSLVLERSLNRVHLLGRVGQDPVLRQVEGKNPVTIFSLATNEMWRSGDSEVYQLGDVSQKTTWHRISVFRPGLRDVAYQYVKKGSRIYLEGKIDYGEYMDKNNVRRQATTIIADNIIFLSDQTKEKE
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
51UbiquitinationVLRQVEGKNPVTIFS
HHHCCCCCCCEEEEE		44.5721890473
51MalonylationVLRQVEGKNPVTIFS
HHHCCCCCCCEEEEE		44.5726320211
51AcetylationVLRQVEGKNPVTIFS
HHHCCCCCCCEEEEE		44.5723954790
67PhosphorylationATNEMWRSGDSEVYQ
CCCCHHHCCCCCEEE		31.2925159151
70PhosphorylationEMWRSGDSEVYQLGD
CHHHCCCCCEEECCC		32.2730108239
73PhosphorylationRSGDSEVYQLGDVSQ
HCCCCCEEECCCCCC		8.2527155012
73NitrationRSGDSEVYQLGDVSQ
HCCCCCEEECCCCCC		8.25-
79PhosphorylationVYQLGDVSQKTTWHR
EEECCCCCCCCCCEE		30.6017525332
81UbiquitinationQLGDVSQKTTWHRIS
ECCCCCCCCCCEEEE		40.1821890473
812-HydroxyisobutyrylationQLGDVSQKTTWHRIS
ECCCCCCCCCCEEEE		40.18-
81MalonylationQLGDVSQKTTWHRIS
ECCCCCCCCCCEEEE		40.1826320211
81AcetylationQLGDVSQKTTWHRIS
ECCCCCCCCCCEEEE		40.1823236377
88PhosphorylationKTTWHRISVFRPGLR
CCCCEEEECCCCCHH		18.3720068231
99PhosphorylationPGLRDVAYQYVKKGS
CCHHHHHHHHHHCCC		10.5428152594
101PhosphorylationLRDVAYQYVKKGSRI
HHHHHHHHHHCCCEE		11.1028152594
103SuccinylationDVAYQYVKKGSRIYL
HHHHHHHHCCCEEEE		46.6227452117
103MalonylationDVAYQYVKKGSRIYL
HHHHHHHHCCCEEEE		46.6226320211
1032-HydroxyisobutyrylationDVAYQYVKKGSRIYL
HHHHHHHHCCCEEEE		46.62-
103UbiquitinationDVAYQYVKKGSRIYL
HHHHHHHHCCCEEEE		46.62-
103AcetylationDVAYQYVKKGSRIYL
HHHHHHHHCCCEEEE		46.6219608861
104UbiquitinationVAYQYVKKGSRIYLE
HHHHHHHCCCEEEEE		52.66-
109PhosphorylationVKKGSRIYLEGKIDY
HHCCCEEEEEEECCH		9.52-
113SuccinylationSRIYLEGKIDYGEYM
CEEEEEEECCHHHHC		24.0323954790
113AcetylationSRIYLEGKIDYGEYM
CEEEEEEECCHHHHC		24.0319608861
113MalonylationSRIYLEGKIDYGEYM
CEEEEEEECCHHHHC		24.0326320211
116PhosphorylationYLEGKIDYGEYMDKN
EEEEECCHHHHCCCC		18.4828102081
119PhosphorylationGKIDYGEYMDKNNVR
EECCHHHHCCCCCCC		13.2725884760
120SulfoxidationKIDYGEYMDKNNVRR
ECCHHHHCCCCCCCH		5.2828183972
122MalonylationDYGEYMDKNNVRRQA
CHHHHCCCCCCCHHH		33.6126320211
1222-HydroxyisobutyrylationDYGEYMDKNNVRRQA
CHHHHCCCCCCCHHH		33.61-
122SuccinylationDYGEYMDKNNVRRQA
CHHHHCCCCCCCHHH		33.61-
122UbiquitinationDYGEYMDKNNVRRQA
CHHHHCCCCCCCHHH		33.6121890473
122SuccinylationDYGEYMDKNNVRRQA
CHHHHCCCCCCCHHH		33.61-
122AcetylationDYGEYMDKNNVRRQA
CHHHHCCCCCCCHHH		33.6125038526
130PhosphorylationNNVRRQATTIIADNI
CCCCHHHHEEEECCE		15.36-
145UbiquitinationIFLSDQTKEKE----
EEECCCCCCCC----		62.24-
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
67SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSBP_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 SSBP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSBP_HUMANSSBP1physical
9033597
YBOX1_HUMANYBX1physical
22939629
TBA1C_HUMANTUBA1Cphysical
22939629
TBB1_HUMANTUBB1physical
22939629
SSDH_HUMANALDH5A1physical
22939629
THIL_HUMANACAT1physical
22939629
TBA1B_HUMANTUBA1Bphysical
22939629
VDAC2_HUMANVDAC2physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
VATE1_HUMANATP6V1E1physical
22939629
T126A_HUMANTMEM126Aphysical
22939629
YMEL1_HUMANYME1L1physical
22939629
INT3_HUMANINTS3physical
21659603
INT7_HUMANINTS7physical
21659603
TIAR_HUMANTIAL1physical
26344197
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 SSBP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-113, AND MASS SPECTROMETRY.
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-79, AND MASSSPECTROMETRY.

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