SRBS2_RAT - dbPTM
SRBS2_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRBS2_RAT
UniProt AC O35413
Protein Name Sorbin and SH3 domain-containing protein 2
Gene Name Sorbs2
Organism Rattus norvegicus (Rat).
Sequence Length 1196
Subcellular Localization Cytoplasm, perinuclear region . Apical cell membrane . Cell junction, focal adhesion . Cell projection, lamellipodium . Detected in the stress fibers, synaptosomal cytosol, postsynaptic density fraction, Z-disks and intercalated. The CBL/PTK2B/ARGBP2
Protein Description Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus mediating AKT1-mediated activation of PAK1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibly by acting on WASF1 phosphorylation, enhancing phosphorylation by ABL1, as well as dephosphorylation by PTPN12 (By similarity). Isoform 2 increases water and sodium absorption in the intestine and gall-bladder..
Protein Sequence MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDKKSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPAAKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQHERPVSVYQSSIDRSLERPSSSASMAGDFRKRRKSEPAVGPPRGLGDHSSSRTSPGRADLPGSSSTFTTSFISSSPSSPSRAQGGDDSKMCPPLCSYSGLNGSPSSELECCGAYRRHLDVPQDSQRAITFKNGWQMARQNAEIWSSTEEAVSPKIKSRSCDDLLNDDCGSFPDPKTKSESMGSLLCDEGSKESDPMTWTSPYIPEVCGNSRSRLKHRSAHNAPGFLKMYKKMHRINRKDLMNSEVICSVKSRILQYEKEQQHRGLLHGWSQSSTEEVPRDVVPTRISEFEKLIQKSKSMPNLGDEMLSPVTLEPPQNGLCPKRRFSIESLLEEETQVRHPSQGQRSCKSNTLVPIHIEVTSDEQPRTHMEFSDSDQDGVVSDHSDNVHVERSSFCSESDFDHFSFTSSESFYGSSHHHHHHHHHHGHFISSCKGRCPASYTRFTTMLKHERAKHENIDRPRRQDMDPGLSKLAFLVSPVPFRRKKVLTPQKQTEQAKCKASVVEALDSALKDICDQIKAEKRRGSLPDNSILHRLISELLPQIPKRNSSLNALKRSPMHQPFHPLPQDGAIHCPLYQNDCGRMPHSASFPDVDTTSSYHAQDYGSVLSLQDHESPRSYSSTLTDLGRSVSRERRGTPEKEVKLPAKAVYDFKAQTSKELSFKKGDTVYILRKIDQNWYEGEHHGRVGIFPISYVEKLTPPEKAQPARPPPPVQPGEIGEAIAKYNFNADTNVELSLRKGDRIILLKRVDQNWYEGKIPGTNRQGIFPVSYVEVVKRNTKGSEDYPDPPLPHSYSSDRIYSLSSNKPQRPVFSHENIQGGGEPFQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL
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
27PhosphorylationTSVKRVQSSPNLLAA
EEEEECCCCCCCHHC
44.9328689409
28PhosphorylationSVKRVQSSPNLLAAG
EEEECCCCCCCHHCC
10.7525403869
38PhosphorylationLLAAGRESHSPDSAW
CHHCCCCCCCCCCHH
28.0928432305
40PhosphorylationAAGRESHSPDSAWRS
HCCCCCCCCCCHHHH
39.4226437020
43PhosphorylationRESHSPDSAWRSYNG
CCCCCCCCHHHHCCC
32.8722673903
62PhosphorylationTLNGDATYSSLAAKG
CCCCCCCHHHHHHCC
9.6621940666
72PhosphorylationLAAKGFRSVRPNLQD
HHHCCCCCCCCCCCC
21.8828689409
82PhosphorylationPNLQDKKSPTQSHIT
CCCCCCCCCCCCCEE
38.6328689409
84PhosphorylationLQDKKSPTQSHITIN
CCCCCCCCCCCEEEE
50.2030181290
86PhosphorylationDKKSPTQSHITINGN
CCCCCCCCCEEEECC
21.2330181290
89PhosphorylationSPTQSHITINGNSGG
CCCCCCEEEECCCCC
11.7230181290
94PhosphorylationHITINGNSGGAVSPV
CEEEECCCCCCCCCC
39.7528689409
99PhosphorylationGNSGGAVSPVSYYQR
CCCCCCCCCCEECCC
21.0328689409
102PhosphorylationGGAVSPVSYYQRPFS
CCCCCCCEECCCCCC
22.8528689409
104PhosphorylationAVSPVSYYQRPFSPS
CCCCCEECCCCCCCC
7.1928689409
109PhosphorylationSYYQRPFSPSAYSLP
EECCCCCCCCHHCCC
22.1922673903
111PhosphorylationYQRPFSPSAYSLPAS
CCCCCCCCHHCCCCC
38.3422673903
113PhosphorylationRPFSPSAYSLPASLN
CCCCCCHHCCCCCCC
18.3128689409
114PhosphorylationPFSPSAYSLPASLNS
CCCCCHHCCCCCCCC
27.8228689409
130PhosphorylationIIMPHGRSLDSAETY
EEECCCCCCCCHHHH
40.9122673903
133PhosphorylationPHGRSLDSAETYSQH
CCCCCCCCHHHHHHH
33.0422673903
136PhosphorylationRSLDSAETYSQHAQS
CCCCCHHHHHHHHHH
28.3428826663
137PhosphorylationSLDSAETYSQHAQSL
CCCCHHHHHHHHHHH
9.6122673903
138PhosphorylationLDSAETYSQHAQSLD
CCCHHHHHHHHHHHC
23.9422673903
143PhosphorylationTYSQHAQSLDGTMGS
HHHHHHHHHCCCCCC
29.2528432305
147PhosphorylationHAQSLDGTMGSSIPL
HHHHHCCCCCCCCCC
20.3028432305
148 (in isoform 2)Amidation-6.3211786189
150PhosphorylationSLDGTMGSSIPLYRS
HHCCCCCCCCCCCCC
17.8025575281
151PhosphorylationLDGTMGSSIPLYRSS
HCCCCCCCCCCCCCC
23.6125575281
155PhosphorylationMGSSIPLYRSSEEEK
CCCCCCCCCCCHHHH
11.7725575281
172PhosphorylationTVIKAPHYPGIGPVD
EEEECCCCCCCCCCC
11.33-
246PhosphorylationPAAKTQTYRPLSKSH
CCCCCCCCCCCCHHC
10.62-
250PhosphorylationTQTYRPLSKSHSDNG
CCCCCCCCHHCCCCC
34.4923984901
252PhosphorylationTYRPLSKSHSDNGTD
CCCCCCHHCCCCCCH
25.5028432305
254PhosphorylationRPLSKSHSDNGTDAF
CCCCHHCCCCCCHHH
39.6029779826
258PhosphorylationKSHSDNGTDAFKEAT
HHCCCCCCHHHHHCC
30.3427097102
281PhosphorylationPPRPRDQSSTEKHDW
CCCCCCCCCCCCCCC
43.4425575281
282PhosphorylationPRPRDQSSTEKHDWD
CCCCCCCCCCCCCCC
34.6525575281
283PhosphorylationRPRDQSSTEKHDWDP
CCCCCCCCCCCCCCC
55.0625575281
315PhosphorylationFEYEPGKSSILQHER
EECCCCCCCCCCCCC
28.6423984901
316PhosphorylationEYEPGKSSILQHERP
ECCCCCCCCCCCCCC
30.7023984901
325PhosphorylationLQHERPVSVYQSSID
CCCCCCCEEEHHHHH
20.1425403869
327PhosphorylationHERPVSVYQSSIDRS
CCCCCEEEHHHHHHH
8.6525403869
329PhosphorylationRPVSVYQSSIDRSLE
CCCEEEHHHHHHHCC
16.1528432305
330PhosphorylationPVSVYQSSIDRSLER
CCEEEHHHHHHHCCC
17.0028432305
334PhosphorylationYQSSIDRSLERPSSS
EHHHHHHHCCCCCCC
30.7327097102
339PhosphorylationDRSLERPSSSASMAG
HHHCCCCCCCCCHHH
43.0527097102
340PhosphorylationRSLERPSSSASMAGD
HHCCCCCCCCCHHHH
32.3829779826
341PhosphorylationSLERPSSSASMAGDF
HCCCCCCCCCHHHHH
28.8027097102
343PhosphorylationERPSSSASMAGDFRK
CCCCCCCCHHHHHHH
15.8929779826
354PhosphorylationDFRKRRKSEPAVGPP
HHHHHCCCCCCCCCC
47.1828825834
368PhosphorylationPRGLGDHSSSRTSPG
CCCCCCCCCCCCCCC
34.4523984901
369PhosphorylationRGLGDHSSSRTSPGR
CCCCCCCCCCCCCCC
22.0323984901
370PhosphorylationGLGDHSSSRTSPGRA
CCCCCCCCCCCCCCC
42.4623984901
372PhosphorylationGDHSSSRTSPGRADL
CCCCCCCCCCCCCCC
41.0228826663
373PhosphorylationDHSSSRTSPGRADLP
CCCCCCCCCCCCCCC
25.0129779826
382PhosphorylationGRADLPGSSSTFTTS
CCCCCCCCCCCEEEC
21.1227097102
383PhosphorylationRADLPGSSSTFTTSF
CCCCCCCCCCEEECC
39.0327097102
384PhosphorylationADLPGSSSTFTTSFI
CCCCCCCCCEEECCC
29.2727097102
385PhosphorylationDLPGSSSTFTTSFIS
CCCCCCCCEEECCCC
27.2727097102
387PhosphorylationPGSSSTFTTSFISSS
CCCCCCEEECCCCCC
22.9427097102
388PhosphorylationGSSSTFTTSFISSSP
CCCCCEEECCCCCCC
19.9027097102
389PhosphorylationSSSTFTTSFISSSPS
CCCCEEECCCCCCCC
19.9527097102
392PhosphorylationTFTTSFISSSPSSPS
CEEECCCCCCCCCCC
23.8227097102
393PhosphorylationFTTSFISSSPSSPSR
EEECCCCCCCCCCCC
41.2627097102
394PhosphorylationTTSFISSSPSSPSRA
EECCCCCCCCCCCCC
23.2427097102
396PhosphorylationSFISSSPSSPSRAQG
CCCCCCCCCCCCCCC
57.7528689409
397PhosphorylationFISSSPSSPSRAQGG
CCCCCCCCCCCCCCC
30.2228689409
399PhosphorylationSSSPSSPSRAQGGDD
CCCCCCCCCCCCCCC
42.0428689409
407PhosphorylationRAQGGDDSKMCPPLC
CCCCCCCCCCCCCCC
27.3328689409
478PhosphorylationSPKIKSRSCDDLLND
CHHHHCCCHHHHCCC
29.05-
497PhosphorylationFPDPKTKSESMGSLL
CCCCCCCCCCCCCEE
39.8926022182
499PhosphorylationDPKTKSESMGSLLCD
CCCCCCCCCCCEECC
35.2226022182
589PhosphorylationRGLLHGWSQSSTEEV
CCCCCCCCCCCCCCC
25.4422673903
591PhosphorylationLLHGWSQSSTEEVPR
CCCCCCCCCCCCCCC
33.4422673903
592PhosphorylationLHGWSQSSTEEVPRD
CCCCCCCCCCCCCCC
32.0030240740
593PhosphorylationHGWSQSSTEEVPRDV
CCCCCCCCCCCCCCC
41.2222673903
645PhosphorylationLCPKRRFSIESLLEE
CCCCCCCCHHHHHCH
24.5125403869
648PhosphorylationKRRFSIESLLEEETQ
CCCCCHHHHHCHHHH
36.2625403869
654PhosphorylationESLLEEETQVRHPSQ
HHHHCHHHHCCCCCC
35.3325403869
767UbiquitinationTRFTTMLKHERAKHE
HHHHHHHHHHHHHCC
32.37-
796PhosphorylationSKLAFLVSPVPFRRK
HHHHHHHCCCCCCCC
23.4828432305
810UbiquitinationKKVLTPQKQTEQAKC
CCCCCCHHHHHHHHH
61.46-
844PhosphorylationKAEKRRGSLPDNSIL
HHHHHHCCCCCCHHH
34.6130411139
873UbiquitinationNSSLNALKRSPMHQP
CCCHHHHHCCCCCCC
48.71-
936PhosphorylationQDHESPRSYSSTLTD
CCCCCCCCCCHHHHH
32.5228432305
937PhosphorylationDHESPRSYSSTLTDL
CCCCCCCCCHHHHHH
14.1225575281
938PhosphorylationHESPRSYSSTLTDLG
CCCCCCCCHHHHHHH
20.3528432305
939PhosphorylationESPRSYSSTLTDLGR
CCCCCCCHHHHHHHH
21.1428432305
940PhosphorylationSPRSYSSTLTDLGRS
CCCCCCHHHHHHHHH
27.9528432305
942PhosphorylationRSYSSTLTDLGRSVS
CCCCHHHHHHHHHHC
29.3028432305
955PhosphorylationVSRERRGTPEKEVKL
HCHHHCCCCHHHCCC
26.8529779826
971AcetylationAKAVYDFKAQTSKEL
CCEEEEECCCCCCEE
36.3722902405
1017PhosphorylationISYVEKLTPPEKAQP
HHHHHHCCCCHHCCC
48.1128432305
1075AcetylationDQNWYEGKIPGTNRQ
CCCCCCCCCCCCCCC
33.5122902405
1097PhosphorylationVEVVKRNTKGSEDYP
EEEEECCCCCCCCCC
40.5925575281
1100PhosphorylationVKRNTKGSEDYPDPP
EECCCCCCCCCCCCC
28.9328689409
1103PhosphorylationNTKGSEDYPDPPLPH
CCCCCCCCCCCCCCC
12.8928689409
1111PhosphorylationPDPPLPHSYSSDRIY
CCCCCCCCCCCCCEE
25.4421738781
1112PhosphorylationDPPLPHSYSSDRIYS
CCCCCCCCCCCCEEE
14.7921738781
1113PhosphorylationPPLPHSYSSDRIYSL
CCCCCCCCCCCEEEC
28.8621738781
1114PhosphorylationPLPHSYSSDRIYSLS
CCCCCCCCCCEEECC
23.7522108457
1118PhosphorylationSYSSDRIYSLSSNKP
CCCCCCEEECCCCCC
12.4023984901
1119PhosphorylationYSSDRIYSLSSNKPQ
CCCCCEEECCCCCCC
21.2823984901
1121PhosphorylationSDRIYSLSSNKPQRP
CCCEEECCCCCCCCC
26.4023984901
1122PhosphorylationDRIYSLSSNKPQRPV
CCEEECCCCCCCCCC
54.9223984901
1187PhosphorylationRRTKFFGTFPGNYVK
CCCEEECCCCCCCCC
22.8423984901

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
-KUbiquitinationE3 ubiquitin ligaseCblD3ZV15
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRBS2_RAT !!

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 SRBS2_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLGP1_RATDlgap1physical
10521485
SH3G1_RATSh3gl1physical
15659545
SYNJ1_RATSynj1physical
15659545
DYN1_RATDnm1physical
15659545
DYN2_RATDnm2physical
15659545

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRBS2_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASSSPECTROMETRY.

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