NADAP_HUMAN - dbPTM
NADAP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NADAP_HUMAN
UniProt AC Q9BWU0
Protein Name Kanadaptin
Gene Name SLC4A1AP
Organism Homo sapiens (Human).
Sequence Length 796
Subcellular Localization Nucleus . Cytoplasm . Mainly nuclear. Small amounts are found in the cytoplasm.
Protein Description
Protein Sequence MLAPLRNAPGREGATSPSPPTDATGSLGEWDVDRNVKTEGWVSKERISKLHRLRMADILSQSETLASQDLSGDFKKPALPVSPAARSKAPASSSSNPEEVQKEGPTALQDSNSGEPDIPPPQPDCGDFRSLQEEQSRPPTAVSSPGGPARAPPYQEPPWGGPATAPYSLETLKGGTILGTRSLKGTSYCLFGRLSGCDVCLEHPSVSRYHAVLQHRASGPDGECDSNGPGFYLYDLGSTHGTFLNKTRIPPRTYCRVHVGHVVRFGGSTRLFILQGPEEDREAESELTVTQLKELRKQQQILLEKKMLGEDSDEEEEMDTSERKINAGSQDDEMGCTWGMGEDAVEDDAEENPIVLEFQQEREAFYIKDPKKALQGFFDREGEELEYEFDEQGHSTWLCRVRLPVDDSTGKQLVAEAIHSGKKKEAMIQCSLEACRILDTLGLLRQEAVSRKRKAKNWEDEDFYDSDDDTFLDRTGLIEKKRLNRMKKAGKIDEKPETFESLVAKLNDAERELSEISERLKASSQVLSESPSQDSLDAFMSEMKSGSTLDGVSRKKLHLRTFELRKEQQRLKGLIKIVKPAEIPELKKTETQTTGAENKAKKLTLPLFGAMKGGSKFKLKTGTVGKLPPKRPELPPTLMRMKDEPEVEEEEEEEEEEEKEKEEHEKKKLEDGSLSRPQPEIEPEAAVQEMRPPTDLTHFKETQTHENMSQLSEEEQNKDYQDCSKTTSLCAGPSASKNEYEKSRGELKKKKTPGPGKLPPTLSSKYPEDDPDYCVWVPPEGQSGDGRTHLNDKYGY
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
15PhosphorylationAPGREGATSPSPPTD
CCCCCCCCCCCCCCC
52.6127732954
16PhosphorylationPGREGATSPSPPTDA
CCCCCCCCCCCCCCC
23.8927732954
18PhosphorylationREGATSPSPPTDATG
CCCCCCCCCCCCCCC
43.1922210691
21PhosphorylationATSPSPPTDATGSLG
CCCCCCCCCCCCCCC
41.4727732954
24PhosphorylationPSPPTDATGSLGEWD
CCCCCCCCCCCCCCC
30.0727732954
26PhosphorylationPPTDATGSLGEWDVD
CCCCCCCCCCCCCCC
28.9327732954
60PhosphorylationLRMADILSQSETLAS
HHHHHHHHCHHHHHH
31.8129083192
62PhosphorylationMADILSQSETLASQD
HHHHHHCHHHHHHCC
29.2229083192
64PhosphorylationDILSQSETLASQDLS
HHHHCHHHHHHCCCC
32.6326074081
67PhosphorylationSQSETLASQDLSGDF
HCHHHHHHCCCCCCC
27.6026074081
71PhosphorylationTLASQDLSGDFKKPA
HHHHCCCCCCCCCCC
44.6026074081
82PhosphorylationKKPALPVSPAARSKA
CCCCCCCCHHHHCCC
13.5929255136
87PhosphorylationPVSPAARSKAPASSS
CCCHHHHCCCCCCCC
28.5726074081
92PhosphorylationARSKAPASSSSNPEE
HHCCCCCCCCCCHHH
29.6926074081
93PhosphorylationRSKAPASSSSNPEEV
HCCCCCCCCCCHHHH
39.6326074081
94PhosphorylationSKAPASSSSNPEEVQ
CCCCCCCCCCHHHHH
31.4726074081
95PhosphorylationKAPASSSSNPEEVQK
CCCCCCCCCHHHHHH
59.3526074081
106PhosphorylationEVQKEGPTALQDSNS
HHHHHCCCCCCCCCC
51.3526074081
130PhosphorylationPDCGDFRSLQEEQSR
CCCCCCHHHHHHHHC
34.1026552605
136PhosphorylationRSLQEEQSRPPTAVS
HHHHHHHHCCCCCCC
50.4629978859
140PhosphorylationEEQSRPPTAVSSPGG
HHHHCCCCCCCCCCC
42.2330266825
143PhosphorylationSRPPTAVSSPGGPAR
HCCCCCCCCCCCCCC
28.4930266825
144PhosphorylationRPPTAVSSPGGPARA
CCCCCCCCCCCCCCC
22.4430266825
173AcetylationPYSLETLKGGTILGT
CCEEEECCCCEEEEC
63.8226051181
176PhosphorylationLETLKGGTILGTRSL
EEECCCCEEEECCCC
23.0021406692
180PhosphorylationKGGTILGTRSLKGTS
CCCEEEECCCCCCCC
17.4021406692
182PhosphorylationGTILGTRSLKGTSYC
CEEEECCCCCCCCEE
33.9821406692
195PhosphorylationYCLFGRLSGCDVCLE
EEEEEECCCCCEECC
35.69-
238PhosphorylationFYLYDLGSTHGTFLN
EEEEECCCCCCCCCC
25.2426074081
239PhosphorylationYLYDLGSTHGTFLNK
EEEECCCCCCCCCCC
23.6426074081
246AcetylationTHGTFLNKTRIPPRT
CCCCCCCCCCCCCCC
41.1326051181
281MethylationLQGPEEDREAESELT
EECCHHHHHHHHCCC
48.59115480795
297UbiquitinationTQLKELRKQQQILLE
HHHHHHHHHHHHHHH
66.1529967540
312O-linked_GlycosylationKKMLGEDSDEEEEMD
HHHHCCCCCHHHHCC
42.4930379171
312PhosphorylationKKMLGEDSDEEEEMD
HHHHCCCCCHHHHCC
42.4922167270
320PhosphorylationDEEEEMDTSERKINA
CHHHHCCHHHCHHCC
31.0423927012
321PhosphorylationEEEEMDTSERKINAG
HHHHCCHHHCHHCCC
31.0123927012
329PhosphorylationERKINAGSQDDEMGC
HCHHCCCCCCCCCCC
28.2028348404
337PhosphorylationQDDEMGCTWGMGEDA
CCCCCCCCCCCCCCC
21.2326714015
368UbiquitinationEREAFYIKDPKKALQ
HHHEEECCCHHHHHC
57.5129967540
408PhosphorylationVRLPVDDSTGKQLVA
EEEECCCCCCHHHHH
34.3021815630
409PhosphorylationRLPVDDSTGKQLVAE
EEECCCCCCHHHHHH
56.2320068231
420PhosphorylationLVAEAIHSGKKKEAM
HHHHHHHCCCCHHHH
46.3120068231
422UbiquitinationAEAIHSGKKKEAMIQ
HHHHHCCCCHHHHHH
64.7833845483
427SulfoxidationSGKKKEAMIQCSLEA
CCCCHHHHHHHHHHH
1.9721406390
440PhosphorylationEACRILDTLGLLRQE
HHHHHHHHHHHHHHH
21.20-
450PhosphorylationLLRQEAVSRKRKAKN
HHHHHHHHHHHHCCC
38.8529116813
464PhosphorylationNWEDEDFYDSDDDTF
CCCCCCCCCCCCCCC
27.1930266825
466PhosphorylationEDEDFYDSDDDTFLD
CCCCCCCCCCCCCCC
31.4022167270
470PhosphorylationFYDSDDDTFLDRTGL
CCCCCCCCCCCCCCH
32.8522167270
475PhosphorylationDDTFLDRTGLIEKKR
CCCCCCCCCHHHHHH
35.6926434776
480UbiquitinationDRTGLIEKKRLNRMK
CCCCHHHHHHHHHHH
35.8829967540
491UbiquitinationNRMKKAGKIDEKPET
HHHHHCCCCCCCCHH
52.4224816145
495AcetylationKAGKIDEKPETFESL
HCCCCCCCCHHHHHH
44.3926051181
495SumoylationKAGKIDEKPETFESL
HCCCCCCCCHHHHHH
44.3928112733
495UbiquitinationKAGKIDEKPETFESL
HCCCCCCCCHHHHHH
44.3929967540
505UbiquitinationTFESLVAKLNDAERE
HHHHHHHHHHHHHHH
40.1029967540
521UbiquitinationSEISERLKASSQVLS
HHHHHHHHHHHHHHH
53.0629967540
523PhosphorylationISERLKASSQVLSES
HHHHHHHHHHHHHCC
21.5127732954
524PhosphorylationSERLKASSQVLSESP
HHHHHHHHHHHHCCC
29.2117525332
528PhosphorylationKASSQVLSESPSQDS
HHHHHHHHCCCCHHH
36.8525159151
530PhosphorylationSSQVLSESPSQDSLD
HHHHHHCCCCHHHHH
26.8625159151
532PhosphorylationQVLSESPSQDSLDAF
HHHHCCCCHHHHHHH
56.7617525332
535PhosphorylationSESPSQDSLDAFMSE
HCCCCHHHHHHHHHH
22.1025159151
541PhosphorylationDSLDAFMSEMKSGST
HHHHHHHHHCCCCCC
28.2520068231
544UbiquitinationDAFMSEMKSGSTLDG
HHHHHHCCCCCCCCC
47.8422817900
545PhosphorylationAFMSEMKSGSTLDGV
HHHHHCCCCCCCCCC
36.3420068231
547PhosphorylationMSEMKSGSTLDGVSR
HHHCCCCCCCCCCCH
32.6520068231
548PhosphorylationSEMKSGSTLDGVSRK
HHCCCCCCCCCCCHH
32.1820068231
553PhosphorylationGSTLDGVSRKKLHLR
CCCCCCCCHHHHHHH
43.8620068231
587AcetylationPAEIPELKKTETQTT
HHHCCCCCCCCCCCC
56.8620167786
588AcetylationAEIPELKKTETQTTG
HHCCCCCCCCCCCCC
65.3020167786
604PhosphorylationENKAKKLTLPLFGAM
HHHHHHHCHHCCCCC
34.9028555341
612AcetylationLPLFGAMKGGSKFKL
HHCCCCCCCCCCEEE
60.6325953088
642AcetylationPPTLMRMKDEPEVEE
CCCCCCCCCCCCCCH
48.8826051181
702PhosphorylationDLTHFKETQTHENMS
CCCCHHHHHCCHHHH
39.0828287266
704PhosphorylationTHFKETQTHENMSQL
CCHHHHHCCHHHHHC
38.2828122231
709PhosphorylationTQTHENMSQLSEEEQ
HHCCHHHHHCCHHHH
39.2817525332
712PhosphorylationHENMSQLSEEEQNKD
CHHHHHCCHHHHCCC
35.0129255136
718AcetylationLSEEEQNKDYQDCSK
CCHHHHCCCHHHHHH
58.4626051181
720PhosphorylationEEEQNKDYQDCSKTT
HHHHCCCHHHHHHHH
14.0928796482
724PhosphorylationNKDYQDCSKTTSLCA
CCCHHHHHHHHHCCC
41.1320873877
725UbiquitinationKDYQDCSKTTSLCAG
CCHHHHHHHHHCCCC
63.2533845483
734PhosphorylationTSLCAGPSASKNEYE
HHCCCCCCCCCCHHH
44.2325159151
736PhosphorylationLCAGPSASKNEYEKS
CCCCCCCCCCHHHHC
40.1125627689
737AcetylationCAGPSASKNEYEKSR
CCCCCCCCCHHHHCH
54.2226051181
740PhosphorylationPSASKNEYEKSRGEL
CCCCCCHHHHCHHHH
37.74-
766PhosphorylationPPTLSSKYPEDDPDY
CCCHHCCCCCCCCCC
17.5027642862
773PhosphorylationYPEDDPDYCVWVPPE
CCCCCCCCEEECCCC
8.3528796482
793UbiquitinationGRTHLNDKYGY----
CCCCCCCCCCC----
39.2319608861
793AcetylationGRTHLNDKYGY----
CCCCCCCCCCC----
39.2319608861
794PhosphorylationRTHLNDKYGY-----
CCCCCCCCCC-----
25.2327642862
796PhosphorylationHLNDKYGY-------
CCCCCCCC-------
16.5825839225

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 NADAP_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NADAP_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 NADAP_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
B3AT_HUMANSLC4A1physical
9422766
A4_HUMANAPPphysical
21832049
WIPF2_HUMANWIPF2physical
22939629
DCLK1_HUMANDCLK1physical
26344197
TPM2_HUMANTPM2physical
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 NADAP_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-793, AND MASS SPECTROMETRY.
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-312 AND SER-466, ANDMASS SPECTROMETRY.
"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-312; SER-466 ANDSER-535, AND MASS SPECTROMETRY.
"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-312; SER-466 ANDSER-530, AND MASS SPECTROMETRY.
"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-524; SER-532; SER-709AND SER-712, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-466, ANDMASS SPECTROMETRY.
"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-466 AND SER-530, ANDMASS SPECTROMETRY.

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