DIP2B_HUMAN - dbPTM
DIP2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DIP2B_HUMAN
UniProt AC Q9P265
Protein Name Disco-interacting protein 2 homolog B
Gene Name DIP2B
Organism Homo sapiens (Human).
Sequence Length 1576
Subcellular Localization
Protein Description
Protein Sequence MAERGLEPSPAAVAALPPEVRAQLAELELELSEGDITQKGYEKKRSKLLSPYSPQTQETDSAVQKELRNQTPAPSAAQTSAPSKYHRTRSGGARDERYRSDIHTEAVQAALAKHKEQKMALPMPTKRRSTFVQSPADACTPPDTSSASEDEGSLRRQAALSAALQQSLQNAESWINRSIQGSSTSSSASSTLSHGEVKGTSGSLADVFANTRIENFSAPPDVTTTTSSSSSSSSIRPANIDLPPSGIVKGMHKGSNRSSLMDTADGVPVSSRVSTKIQQLLNTLKRPKRPPLKEFFVDDSEEIVEVPQPDPNQPKPEGRQMTPVKGEPLGVICNWPPALESALQRWGTTQAKCSCLTALDMTGKPVYTLTYGKLWSRSLKLAYTLLNKLGTKNEPVLKPGDRVALVYPNNDPVMFMVAFYGCLLAEVIPVPIEVPLTRKDAGGQQIGFLLGSCGIALALTSEVCLKGLPKTQNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPAGTEPAYIEYKTSKEGSVMGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKVALVKCRDLHWAMMAHRDQRDVSLSSLRMLIVTDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAMTVAIRRPGVPGAPLPGRAILSMNGLSYGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGPPQLCKTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVNSAGSPVGDVPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLHPCNILMCPHTCVTNLPKPRQKQPGVGPASVMVGNLVAGKRIAQAAGRDLGQIEENDLVRKHQFLAEILQWRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATLPTVRMIVDVSKAACILTSQTLMRLLRSREAAAAVDVKTWPTIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMELENNLFLWLSTVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLSCVRTCVVVAEERPRVALQQSFSKLFKDIGLSPRAVSTTFGSRVNVAICLQGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTIYDSETLQADHFNTRLSFGDAAQTLWARTGYLGFVRRTELTAATGERHDALYVVGALDETLELRGLRYHPIDIETSVSRIHRSIAECAVFTWTNLLVVVVELCGSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDPGVIPINSRGEKQRMHLRDSFLADQLDPIYVAYNM
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
9PhosphorylationAERGLEPSPAAVAAL
CCCCCCCCHHHHHCC
20.1429255136
32PhosphorylationAELELELSEGDITQK
HHHEEECCCCCCCCC
30.11-
37PhosphorylationELSEGDITQKGYEKK
ECCCCCCCCCCHHHH
29.03-
46PhosphorylationKGYEKKRSKLLSPYS
CCHHHHHHHCCCCCC
36.2123312004
47UbiquitinationGYEKKRSKLLSPYSP
CHHHHHHHCCCCCCC
58.4421890473
47 (in isoform 1)Ubiquitination-58.4421890473
50PhosphorylationKKRSKLLSPYSPQTQ
HHHHHCCCCCCCCCH
32.0325159151
52PhosphorylationRSKLLSPYSPQTQET
HHHCCCCCCCCCHHC
29.6125159151
53PhosphorylationSKLLSPYSPQTQETD
HHCCCCCCCCCHHCC
17.5725159151
56PhosphorylationLSPYSPQTQETDSAV
CCCCCCCCHHCCHHH
31.5821712546
59PhosphorylationYSPQTQETDSAVQKE
CCCCCHHCCHHHHHH
25.9924732914
61PhosphorylationPQTQETDSAVQKELR
CCCHHCCHHHHHHHH
37.4524732914
65UbiquitinationETDSAVQKELRNQTP
HCCHHHHHHHHHCCC
52.7121890473
65 (in isoform 1)Ubiquitination-52.7121890473
71PhosphorylationQKELRNQTPAPSAAQ
HHHHHHCCCCCCHHH
25.6029255136
75PhosphorylationRNQTPAPSAAQTSAP
HHCCCCCCHHHCCCC
38.0429255136
79PhosphorylationPAPSAAQTSAPSKYH
CCCCHHHCCCCCCCC
23.3329255136
80PhosphorylationAPSAAQTSAPSKYHR
CCCHHHCCCCCCCCC
26.5429255136
83PhosphorylationAAQTSAPSKYHRTRS
HHHCCCCCCCCCCCC
45.6329255136
84AcetylationAQTSAPSKYHRTRSG
HHCCCCCCCCCCCCC
43.9725953088
84UbiquitinationAQTSAPSKYHRTRSG
HHCCCCCCCCCCCCC
43.97-
85PhosphorylationQTSAPSKYHRTRSGG
HCCCCCCCCCCCCCC
10.8130576142
88PhosphorylationAPSKYHRTRSGGARD
CCCCCCCCCCCCCCC
18.8430576142
90PhosphorylationSKYHRTRSGGARDER
CCCCCCCCCCCCCHH
40.7530576142
98PhosphorylationGGARDERYRSDIHTE
CCCCCHHHHHHHHHH
16.6630266825
100PhosphorylationARDERYRSDIHTEAV
CCCHHHHHHHHHHHH
31.7929255136
104PhosphorylationRYRSDIHTEAVQAAL
HHHHHHHHHHHHHHH
26.4430266825
113UbiquitinationAVQAALAKHKEQKMA
HHHHHHHHCHHHHCC
56.94-
115UbiquitinationQAALAKHKEQKMALP
HHHHHHCHHHHCCCC
62.22-
125PhosphorylationKMALPMPTKRRSTFV
HCCCCCCCCCCCCCC
30.8229514088
126AcetylationMALPMPTKRRSTFVQ
CCCCCCCCCCCCCCC
39.6925953088
126UbiquitinationMALPMPTKRRSTFVQ
CCCCCCCCCCCCCCC
39.69-
129PhosphorylationPMPTKRRSTFVQSPA
CCCCCCCCCCCCCHH
30.1728450419
130PhosphorylationMPTKRRSTFVQSPAD
CCCCCCCCCCCCHHH
26.4728450419
134PhosphorylationRRSTFVQSPADACTP
CCCCCCCCHHHHCCC
19.4323663014
140PhosphorylationQSPADACTPPDTSSA
CCHHHHCCCCCCCCC
39.3121712546
144PhosphorylationDACTPPDTSSASEDE
HHCCCCCCCCCCCCC
30.2923401153
145PhosphorylationACTPPDTSSASEDEG
HCCCCCCCCCCCCCC
31.1521082442
146PhosphorylationCTPPDTSSASEDEGS
CCCCCCCCCCCCCCH
37.6021712546
148PhosphorylationPPDTSSASEDEGSLR
CCCCCCCCCCCCHHH
47.7522617229
153PhosphorylationSASEDEGSLRRQAAL
CCCCCCCHHHHHHHH
19.3622617229
167PhosphorylationLSAALQQSLQNAESW
HHHHHHHHHHHHHHH
20.9727470641
173PhosphorylationQSLQNAESWINRSIQ
HHHHHHHHHHHHHHC
30.7427470641
178PhosphorylationAESWINRSIQGSSTS
HHHHHHHHHCCCCCC
18.1228450419
182PhosphorylationINRSIQGSSTSSSAS
HHHHHCCCCCCCCCC
17.6728450419
183PhosphorylationNRSIQGSSTSSSASS
HHHHCCCCCCCCCCC
38.8528450419
184PhosphorylationRSIQGSSTSSSASST
HHHCCCCCCCCCCCC
34.0328450419
185PhosphorylationSIQGSSTSSSASSTL
HHCCCCCCCCCCCCC
25.0123927012
186PhosphorylationIQGSSTSSSASSTLS
HCCCCCCCCCCCCCC
29.9728450419
187PhosphorylationQGSSTSSSASSTLSH
CCCCCCCCCCCCCCC
31.7523927012
189PhosphorylationSSTSSSASSTLSHGE
CCCCCCCCCCCCCCE
26.2928450419
190PhosphorylationSTSSSASSTLSHGEV
CCCCCCCCCCCCCEE
32.8428450419
191PhosphorylationTSSSASSTLSHGEVK
CCCCCCCCCCCCEEC
29.7728450419
193PhosphorylationSSASSTLSHGEVKGT
CCCCCCCCCCEECCC
29.5428450419
198UbiquitinationTLSHGEVKGTSGSLA
CCCCCEECCCCCCHH
52.77-
200PhosphorylationSHGEVKGTSGSLADV
CCCEECCCCCCHHHH
24.9729255136
201PhosphorylationHGEVKGTSGSLADVF
CCEECCCCCCHHHHH
34.7429255136
203PhosphorylationEVKGTSGSLADVFAN
EECCCCCCHHHHHHC
21.8329255136
211PhosphorylationLADVFANTRIENFSA
HHHHHHCCCEECCCC
29.6023403867
223PhosphorylationFSAPPDVTTTTSSSS
CCCCCCCEECCCCCC
26.3022210691
227PhosphorylationPDVTTTTSSSSSSSS
CCCEECCCCCCCCCC
26.5722210691
231PhosphorylationTTTSSSSSSSSIRPA
ECCCCCCCCCCCCCC
35.8727470641
232PhosphorylationTTSSSSSSSSIRPAN
CCCCCCCCCCCCCCC
30.0122210691
255PhosphorylationVKGMHKGSNRSSLMD
CCCCCCCCCCCCCCC
33.6023927012
258PhosphorylationMHKGSNRSSLMDTAD
CCCCCCCCCCCCCCC
31.8823401153
259PhosphorylationHKGSNRSSLMDTADG
CCCCCCCCCCCCCCC
25.1923927012
263PhosphorylationNRSSLMDTADGVPVS
CCCCCCCCCCCCCCH
16.8123927012
270PhosphorylationTADGVPVSSRVSTKI
CCCCCCCHHHHHHHH
13.3223403867
271PhosphorylationADGVPVSSRVSTKIQ
CCCCCCHHHHHHHHH
36.6128348404
274PhosphorylationVPVSSRVSTKIQQLL
CCCHHHHHHHHHHHH
23.9128348404
275PhosphorylationPVSSRVSTKIQQLLN
CCHHHHHHHHHHHHH
29.3428348404
276UbiquitinationVSSRVSTKIQQLLNT
CHHHHHHHHHHHHHH
30.8921890473
276 (in isoform 1)Ubiquitination-30.8921890473
283PhosphorylationKIQQLLNTLKRPKRP
HHHHHHHHCCCCCCC
33.3623401153
285UbiquitinationQQLLNTLKRPKRPPL
HHHHHHCCCCCCCCC
65.69-
285 (in isoform 1)Ubiquitination-65.6921890473
288UbiquitinationLNTLKRPKRPPLKEF
HHHCCCCCCCCCHHC
79.96-
293UbiquitinationRPKRPPLKEFFVDDS
CCCCCCCHHCCCCCC
59.2421906983
293 (in isoform 1)Ubiquitination-59.2421890473
315UbiquitinationQPDPNQPKPEGRQMT
CCCCCCCCCCCCCCC
46.03-
322PhosphorylationKPEGRQMTPVKGEPL
CCCCCCCCCCCCCEE
19.3224719451
383PhosphorylationSRSLKLAYTLLNKLG
HHHHHHHHHHHHHHC
14.35-
384PhosphorylationRSLKLAYTLLNKLGT
HHHHHHHHHHHHHCC
21.11-
391PhosphorylationTLLNKLGTKNEPVLK
HHHHHHCCCCCCCCC
40.93-
480UbiquitinationNGEIVQFKGWPRLKW
CCCEEEECCCCCEEE
42.8721890473
480 (in isoform 1)Ubiquitination-42.8721890473
492O-linked_GlycosylationLKWVVTDSKYLSKPP
EEEEEECHHHCCCCC
17.5230379171
494PhosphorylationWVVTDSKYLSKPPKD
EEEECHHHCCCCCCC
21.8423403867
496PhosphorylationVTDSKYLSKPPKDWQ
EECHHHCCCCCCCCC
39.7723403867
519UbiquitinationEPAYIEYKTSKEGSV
CCEEEEEECCCCCCC
33.27-
525PhosphorylationYKTSKEGSVMGVTVS
EECCCCCCCEEEEHH
15.2617192257
530PhosphorylationEGSVMGVTVSRLAML
CCCCEEEEHHHHHHH
13.66-
532PhosphorylationSVMGVTVSRLAMLSH
CCEEEEHHHHHHHHH
16.5324719451
554PhosphorylationCNYSEGETIVNVLDF
CCCCCCCEEEEEEEE
40.8722210691
578UbiquitinationMFANVMNKMHTISVP
HHHHHHHHCCCCCCC
17.60-
611UbiquitinationKAKVALVKCRDLHWA
CCEEEEEEHHHHHHH
25.13-
629PhosphorylationHRDQRDVSLSSLRML
CCCCCCCCHHHEEEE
27.1622167270
631PhosphorylationDQRDVSLSSLRMLIV
CCCCCCHHHEEEEEE
21.5922167270
632PhosphorylationQRDVSLSSLRMLIVT
CCCCCHHHEEEEEEC
25.8622167270
714UbiquitinationIRVNTEDKNSALTVQ
EEEECCCCCCCEEEE
46.71-
719PhosphorylationEDKNSALTVQDVGHV
CCCCCCEEEEECCCC
18.8124719451
746PhosphorylationGPPQLCKTDEIGEIC
CCCCCCCCCCCCCEE
37.56-
755PhosphorylationEIGEICVSSRTGGMM
CCCCEEEECCCCCEE
15.08-
756PhosphorylationIGEICVSSRTGGMMY
CCCEEEECCCCCEEE
17.29-
781PhosphorylationFEVIPVNSAGSPVGD
EEEEECCCCCCCCCC
33.9528348404
784PhosphorylationIPVNSAGSPVGDVPF
EECCCCCCCCCCCCC
19.0128348404
794PhosphorylationGDVPFIRSGLLGFVG
CCCCCCCCCCCCEEC
29.0425867546
804PhosphorylationLGFVGPGSLVFVVGK
CCEECCCCEEEEEEE
25.2125867546
819PhosphorylationMDGLLMVSGRRHNAD
CCCEEEEECCCCCHH
16.7725867546
831PhosphorylationNADDIVATGLAVESI
CHHHHHHCCCHHHHH
23.10-
837PhosphorylationATGLAVESIKTVYRG
HCCCHHHHHHHHCCC
23.84-
887PhosphorylationRVLQAIDSIHQVGVY
HHHHHHHHHHHHCCE
18.83-
894PhosphorylationSIHQVGVYCLALVPA
HHHHHCCEEEEEEEC
3.94-
903PhosphorylationLALVPANTLPKTPLG
EEEEECCCCCCCCCC
46.69-
907PhosphorylationPANTLPKTPLGGIHI
ECCCCCCCCCCCEEE
23.08-
956PhosphorylationQPGVGPASVMVGNLV
CCCCCCHHHHCCHHH
17.5527470641
1035PhosphorylationKRAERIASVLGDKGH
HHHHHHHHHHCCCCC
18.59-
1125UbiquitinationAAAAVDVKTWPTIID
HHHCCCCCCCCCEEC
40.1721906983
1125 (in isoform 1)Ubiquitination-40.1721890473
1149PhosphorylationPQLYKPPTPEMLAYL
CCCCCCCCHHHHHCC
40.17-
1155PhosphorylationPTPEMLAYLDFSVST
CCHHHHHCCCEEEEC
11.66-
1297PhosphorylationPRVALQQSFSKLFKD
HHHHHHHHHHHHHHH
20.6624719451
1300UbiquitinationALQQSFSKLFKDIGL
HHHHHHHHHHHHHCC
56.8021890473
1300 (in isoform 1)Ubiquitination-56.8021890473
1303UbiquitinationQSFSKLFKDIGLSPR
HHHHHHHHHHCCCCC
59.89-
1308PhosphorylationLFKDIGLSPRAVSTT
HHHHHCCCCCEECCC
13.7124719451
1359PhosphorylationVERGAPQSLLLSESG
HHCCCCCCEEECCCC
21.6720068231
1363PhosphorylationAPQSLLLSESGKILP
CCCCEEECCCCCCCC
29.6820068231
1365PhosphorylationQSLLLSESGKILPGV
CCEEECCCCCCCCCC
41.8520068231
1367UbiquitinationLLLSESGKILPGVKV
EEECCCCCCCCCCEE
50.802189047
1367 (in isoform 1)Ubiquitination-50.8021890473
1404PhosphorylationSPHTASGYYTIYDSE
CCCCCCEEEEEEECC
8.57-
1430PhosphorylationSFGDAAQTLWARTGY
CHHHHHHHHHHHHCC
21.3825850435
1437PhosphorylationTLWARTGYLGFVRRT
HHHHHHCCCCEEEEE
11.75-
1458PhosphorylationGERHDALYVVGALDE
CCCCEEEEEEECCCC
8.5322817900

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 DIP2B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DIP2B_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 DIP2B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DIP2B_HUMAN !!

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 DIP2B_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-203, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-50; SER-53;THR-71; SER-100; THR-140; SER-145; SER-146 AND SER-148, AND MASSSPECTROMETRY.
"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-525, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-153, ANDMASS SPECTROMETRY.

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