DIP2A_HUMAN - dbPTM
DIP2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DIP2A_HUMAN
UniProt AC Q14689
Protein Name Disco-interacting protein 2 homolog A
Gene Name DIP2A
Organism Homo sapiens (Human).
Sequence Length 1571
Subcellular Localization Nucleus .
Protein Description May provide positional cues for axon pathfinding and patterning in the central nervous system..
Protein Sequence MADRGCPLEAAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIPLIQGIDPSLQAENRIPGPSQTTAAAPKQQKSRPTASRDERFRSDVHTEAVQAALAKYKERKMPMPSKRRSVLVHSSVETYTPPDTSSASEDEGSLRRPGRLTSTPLQSHSSVEPWLDRVIQGSSTSSSASSTSSHPGGRPTTAPSAAATPGAAATTALAGLEAHTHIDLHSAPPDVTTGLVEHSYFERPQVASVRSVPRGCSGSMLETADGVPVNSRVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSVLRGEPLTAGVPRPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTSKNEPLLKPGDRVALVFPNSDPVMFMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKARAALVKSRDMHWSLLAQRGQRDVSLSSLRMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDLGGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNVLMCPHTCVTNLPKPRQKQPEVGPASMIVGNLVAGKRIAQASGRELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRVNVAICLQGTAGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTVYGEEALHADHFSARLSFGDTQTIWARTGYLGFLRRTELTDASGGRHDALYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELDGLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINSRGEKQRMHLRDGFLADQLDPIYVAYNM
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
20PhosphorylationLPAEVRESLAELELE
CCHHHHHHHHHCEEE
23.47-
29PhosphorylationAELELELSEGDITQK
HHCEEEECCCCCCCC
30.11-
34PhosphorylationELSEGDITQKGYEKK
EECCCCCCCCCHHHH
29.03-
38PhosphorylationGDITQKGYEKKRAKL
CCCCCCCHHHHHHHH
31.45-
49PhosphorylationRAKLLARYIPLIQGI
HHHHHHHHHHHHCCC
10.98-
59PhosphorylationLIQGIDPSLQAENRI
HHCCCCHHHCCCCCC
29.39-
85PhosphorylationKQQKSRPTASRDERF
CCCCCCCCCCCCHHH
35.8327470641
94PhosphorylationSRDERFRSDVHTEAV
CCCHHHHHHHHHHHH
41.0729255136
98PhosphorylationRFRSDVHTEAVQAAL
HHHHHHHHHHHHHHH
26.0329255136
107UbiquitinationAVQAALAKYKERKMP
HHHHHHHHHHHCCCC
58.67-
132PhosphorylationHSSVETYTPPDTSSA
ECCEEEECCCCCCCC
35.4524076635
136PhosphorylationETYTPPDTSSASEDE
EEECCCCCCCCCCCC
30.2923898821
137PhosphorylationTYTPPDTSSASEDEG
EECCCCCCCCCCCCC
31.1522817900
138PhosphorylationYTPPDTSSASEDEGS
ECCCCCCCCCCCCCC
37.6030576142
140PhosphorylationPPDTSSASEDEGSLR
CCCCCCCCCCCCCCC
47.7530576142
145PhosphorylationSASEDEGSLRRPGRL
CCCCCCCCCCCCCCC
19.3630576142
153PhosphorylationLRRPGRLTSTPLQSH
CCCCCCCCCCCCCCC
29.2423403867
154PhosphorylationRRPGRLTSTPLQSHS
CCCCCCCCCCCCCCC
32.4025159151
155PhosphorylationRPGRLTSTPLQSHSS
CCCCCCCCCCCCCCC
23.8425159151
159PhosphorylationLTSTPLQSHSSVEPW
CCCCCCCCCCCCCHH
32.7823403867
161PhosphorylationSTPLQSHSSVEPWLD
CCCCCCCCCCCHHHH
41.1323403867
162PhosphorylationTPLQSHSSVEPWLDR
CCCCCCCCCCHHHHH
25.6923403867
176PhosphorylationRVIQGSSTSSSASST
HHHCCCCCCCCCCCC
34.0322817900
217UbiquitinationAGLEAHTHIDLHSAP
HCHHHHCCEECCCCC
11.1621890473
238 (in isoform 3)Ubiquitination-56.0421890473
244PhosphorylationFERPQVASVRSVPRG
CCCCCEEEEEECCCC
21.1424719451
247PhosphorylationPQVASVRSVPRGCSG
CCEEEEEECCCCCCC
34.0328270605
253PhosphorylationRSVPRGCSGSMLETA
EECCCCCCCCCEECC
36.4028270605
255PhosphorylationVPRGCSGSMLETADG
CCCCCCCCCEECCCC
12.1428270605
259PhosphorylationCSGSMLETADGVPVN
CCCCCEECCCCCCCC
26.5328270605
267PhosphorylationADGVPVNSRVSSKIQ
CCCCCCCHHHHHHHH
34.0028270605
272UbiquitinationVNSRVSSKIQQLLNT
CCHHHHHHHHHHHHH
36.71-
279PhosphorylationKIQQLLNTLKRPKRP
HHHHHHHHCCCCCCC
33.3623401153
281 (in isoform 4)Ubiquitination-65.6921890473
281 (in isoform 2)Ubiquitination-65.6921890473
281UbiquitinationQQLLNTLKRPKRPPL
HHHHHHCCCCCCCCH
65.69-
348UbiquitinationRWGTTQPKSPCLTAL
HHCCCCCCCCCEEEE
58.15-
363PhosphorylationDTTGKAVYTLTYGKL
CCCCCEEEEEECHHH
10.8229496907
367PhosphorylationKAVYTLTYGKLWSRS
CEEEEEECHHHHHHH
18.5129496907
384UbiquitinationLAYTLLNKLTSKNEP
HHHHHHHHHCCCCCC
53.78-
388UbiquitinationLLNKLTSKNEPLLKP
HHHHHCCCCCCCCCC
61.16-
394UbiquitinationSKNEPLLKPGDRVAL
CCCCCCCCCCCEEEE
55.42-
466UbiquitinationACQKGLPKAQTGEVA
HHHCCCCCCCCCCEE
59.16-
496UbiquitinationKHLAKPPKDWHPLAQ
CCCCCCCCCCCCCCC
80.24-
515UbiquitinationGTAYIEYKTSKEGST
CEEEEEEEECCCCCE
33.27-
518UbiquitinationYIEYKTSKEGSTVGV
EEEEEECCCCCEEEE
71.91-
558UbiquitinationLTNVLDFKRDAGLWH
HHHHHHHHCCCCCHH
49.38-
569PhosphorylationGLWHGVLTSVMNRMH
CCHHHHHHHHHHHHC
19.50-
582PhosphorylationMHVVSVPYALMKANP
HCCEEHHHHHHHHCC
15.37-
586AcetylationSVPYALMKANPLSWI
EHHHHHHHHCCCHHH
45.9518585193
600UbiquitinationIQKVCFYKARAALVK
HHHHHHHHHHHHHHH
15.90-
625PhosphorylationQRGQRDVSLSSLRML
HCCCCCCCHHHEEEE
27.1622167270
627PhosphorylationGQRDVSLSSLRMLIV
CCCCCCHHHEEEEEE
21.5922167270
628PhosphorylationQRDVSLSSLRMLIVA
CCCCCHHHEEEEEEC
25.8622167270
694PhosphorylationPPRKAVLSMNGLSYG
CCCCEEEECCCCEEE
12.0021406692
699PhosphorylationVLSMNGLSYGVIRVD
EEECCCCEEEEEEEC
22.6521406692
700PhosphorylationLSMNGLSYGVIRVDT
EECCCCEEEEEEECC
22.0621406692
736PhosphorylationCVVKLEGTPYLCKTD
EEEEECCCEEEEECC
10.21-
738PhosphorylationVKLEGTPYLCKTDEV
EEECCCEEEEECCCC
25.27-
883PhosphorylationRVLQAIDSIHQVGVY
HHHHHHHHHHHHCCE
18.83-
890PhosphorylationSIHQVGVYCLALVPA
HHHHHCCEEEEEEEC
3.94-
911PhosphorylationPLGGIHISETKQRFL
CCCCEEEHHHHHHHH
25.6721406692
913PhosphorylationGGIHISETKQRFLEG
CCEEEHHHHHHHHHC
26.2021406692
914UbiquitinationGIHISETKQRFLEGT
CEEEHHHHHHHHHCC
35.112190698
915 (in isoform 1)Ubiquitination-49.1021890473
962AcetylationVGNLVAGKRIAQASG
CCHHHHCHHHHHHCC
30.7830588171
1101PhosphorylationSKSACVLTTQAVTRL
CCHHHHHHHHHHHHH
9.1024667141
1106PhosphorylationVLTTQAVTRLLRSKE
HHHHHHHHHHHHCHH
20.7224667141
1111PhosphorylationAVTRLLRSKEAAAAV
HHHHHHHCHHHHHCC
34.51-
1112UbiquitinationVTRLLRSKEAAAAVD
HHHHHHCHHHHHCCC
44.96-
1139PhosphorylationIPKKKIASVFRPPSP
CCHHHHHHCCCCCCC
25.84-
1173PhosphorylationKMSHAATSALCRSIK
CCCHHHHHHHHHHHH
17.9522210691
1186PhosphorylationIKLQCELYPSRQIAI
HHHEEEECCCCCEEE
4.1125690035
1273PhosphorylationRMKGVNLSCVRTCMV
EECCCCHHHEEEEEH
12.83-
1293PhosphorylationPRIALTQSFSKLFKD
CCEEEEHHHHHHHHH
26.6724719451
1296UbiquitinationALTQSFSKLFKDLGL
EEEHHHHHHHHHHCC
56.80-
1352PhosphorylationVRLVERGSPHSLPLM
EEEHHCCCCCCCCCC
26.1723403867
1355PhosphorylationVERGSPHSLPLMESG
HHCCCCCCCCCCCCC
34.7623403867
1384PhosphorylationTKGPLGDSHLGEIWV
CCCCCCCCCCEEEEE
20.8623401153
1392PhosphorylationHLGEIWVSSPHNATG
CCEEEEECCCCCCCE
24.1323401153
1393PhosphorylationLGEIWVSSPHNATGY
CEEEEECCCCCCCEE
22.1323401153
1400PhosphorylationSPHNATGYYTVYGEE
CCCCCCEEEEEECCC
7.5123401153
1401PhosphorylationPHNATGYYTVYGEEA
CCCCCEEEEEECCCC
7.3523401153
1404PhosphorylationATGYYTVYGEEALHA
CCEEEEEECCCCCCC
15.8323401153

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 DIP2A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DIP2A_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 DIP2A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JMJD6_HUMANJMJD6physical
23455924
MBIP1_HUMANMBIPphysical
25416956
ATL4_HUMANADAMTSL4physical
25416956
GPT2L_HUMANGPATCH2Lphysical
25416956
TRI39_HUMANTRIM39physical
25416956
CCD33_HUMANCCDC33physical
25416956
F214B_HUMANFAM214Bphysical
25416956
CEP44_HUMANCEP44physical
25416956
STAC3_HUMANSTAC3physical
25416956

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 DIP2A_HUMAN

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Related Literatures of Post-Translational Modification

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