DCTN1_HUMAN - dbPTM
DCTN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCTN1_HUMAN
UniProt AC Q14203
Protein Name Dynactin subunit 1
Gene Name DCTN1
Organism Homo sapiens (Human).
Sequence Length 1278
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, spindle . Nucleus envelope . Cytoplasm, cel
Protein Description Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. Essential for targeting dynein to microtubule plus ends, recruiting dynein to membranous cargos and enhancing dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Can also act as a brake to slow the dynein motor during motility along the microtubule. [PubMed: 25185702 Can regulate microtubule stability by promoting microtubule formation, nucleation and polymerization and by inhibiting microtubule catastrophe in neurons. Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon]
Protein Sequence MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFELSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGPQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELAFKASEQIYGTPSSSPYECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGAIPGQAPGSVPGPGLVKDSPLLLQQISAMRLHISQLQHENSILKGAQMKASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTHVVDITRTSPAAKSPSAQLMEQVAQLKSLSDTVEKLKDEVLKETVSQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGFGQRHRLVLTQEQLHQLHSRLIS
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
9PhosphorylationAQSKRHVYSRTPSGS
CCCCCCCCCCCCCCC
6.0624719451
10PhosphorylationQSKRHVYSRTPSGSR
CCCCCCCCCCCCCCC
28.7024719451
11 (in isoform 2)Phosphorylation-32.7322210691
11 (in isoform 5)Phosphorylation-32.7322210691
12 (in isoform 2)Phosphorylation-18.8322210691
12 (in isoform 5)Phosphorylation-18.8322210691
13 (in isoform 2)Phosphorylation-35.2722210691
13 (in isoform 5)Phosphorylation-35.2722210691
16PhosphorylationYSRTPSGSRMSAEAS
CCCCCCCCCCCHHHC
29.1925690035
17MethylationSRTPSGSRMSAEASA
CCCCCCCCCCHHHCC
26.97-
19PhosphorylationTPSGSRMSAEASARP
CCCCCCCCHHHCCCC
23.1120363803
23PhosphorylationSRMSAEASARPLRVG
CCCCHHHCCCCCCCC
19.1326270265
25MethylationMSAEASARPLRVGSR
CCHHHCCCCCCCCCE
28.43-
31PhosphorylationARPLRVGSRVEVIGK
CCCCCCCCEEEEECC
30.23-
38AcetylationSRVEVIGKGHRGTVA
CEEEEECCCCCCCEE
40.1825953088
77MalonylationDGTVQGRKYFTCDEG
CCCCCCEEEEEECCC
52.0926320211
78PhosphorylationGTVQGRKYFTCDEGH
CCCCCEEEEEECCCC
11.6224248375
92PhosphorylationHGIFVRQSQIQVFED
CEEEEEHHEEEEECC
20.7729396449
96AcetylationVRQSQIQVFEDGADT
EEHHEEEEECCCCCC
6.4019608861
103PhosphorylationVFEDGADTTSPETPD
EECCCCCCCCCCCCC
28.7425159151
104PhosphorylationFEDGADTTSPETPDS
ECCCCCCCCCCCCCC
42.7125159151
105PhosphorylationEDGADTTSPETPDSS
CCCCCCCCCCCCCCH
23.8830278072
108PhosphorylationADTTSPETPDSSASK
CCCCCCCCCCCHHHH
35.4625159151
111PhosphorylationTSPETPDSSASKVLK
CCCCCCCCHHHHHHH
29.0721712546
112PhosphorylationSPETPDSSASKVLKR
CCCCCCCHHHHHHHH
43.8919691289
114PhosphorylationETPDSSASKVLKREG
CCCCCHHHHHHHHCC
25.8319691289
115UbiquitinationTPDSSASKVLKREGT
CCCCHHHHHHHHCCC
51.83-
116 (in isoform 3)Phosphorylation-7.6427251275
122PhosphorylationKVLKREGTDTTAKTS
HHHHHCCCCCCHHHH
25.9730576142
128PhosphorylationGTDTTAKTSKLRGLK
CCCCCHHHHHHCCCC
28.7320860994
129PhosphorylationTDTTAKTSKLRGLKP
CCCCHHHHHHCCCCC
29.0529759185
133 (in isoform 4)Phosphorylation-48.7927251275
134 (in isoform 6)Phosphorylation-7.49-
145PhosphorylationKAPTARKTTTRRPKP
CCCCCCCCCCCCCCC
28.0423985322
146PhosphorylationAPTARKTTTRRPKPT
CCCCCCCCCCCCCCC
22.7223985322
147PhosphorylationPTARKTTTRRPKPTR
CCCCCCCCCCCCCCC
29.8823985322
158PhosphorylationKPTRPASTGVAGASS
CCCCCCCCCCCCCCC
37.47-
164PhosphorylationSTGVAGASSSLGPSG
CCCCCCCCCCCCCCC
21.39-
172PhosphorylationSSLGPSGSASAGELS
CCCCCCCCCCCCCCC
24.32-
179PhosphorylationSASAGELSSSEPSTP
CCCCCCCCCCCCCCC
27.7620679239
193AcetylationPAQTPLAAPIIPTPV
CCCCCCCCCCCCCCC
11.9619608861
198PhosphorylationLAAPIIPTPVLTSPG
CCCCCCCCCCCCCCC
18.6726074081
202PhosphorylationIIPTPVLTSPGAVPP
CCCCCCCCCCCCCCC
32.8626074081
203PhosphorylationIPTPVLTSPGAVPPL
CCCCCCCCCCCCCCC
19.7126657352
210AcetylationSPGAVPPLPSPSKEE
CCCCCCCCCCCCHHH
5.5519608861
212PhosphorylationGAVPPLPSPSKEEEG
CCCCCCCCCCHHHHC
49.8726972003
214PhosphorylationVPPLPSPSKEEEGLR
CCCCCCCCHHHHCHH
57.9726074081
230AcetylationQVRDLEEKLETLRLK
HHHCHHHHHHHHHHH
42.1023749302
230UbiquitinationQVRDLEEKLETLRLK
HHHCHHHHHHHHHHH
42.1019608861
233PhosphorylationDLEEKLETLRLKRAE
CHHHHHHHHHHHHHH
27.84-
262AcetylationLEQVQEWKSKMQEQQ
HHHHHHHHHHHHHHH
39.1725953088
290AcetylationAKEALEAKERYMEEM
HHHHHHHHHHHHHHH
33.097290025
320PhosphorylationMAEERAESLQQEVEA
HHHHHHHHHHHHHHH
30.4129255136
329UbiquitinationQQEVEALKERVDELT
HHHHHHHHHHHHHHH
50.99-
336PhosphorylationKERVDELTTDLEILK
HHHHHHHHHHHHHHH
19.06-
337PhosphorylationERVDELTTDLEILKA
HHHHHHHHHHHHHHH
51.73-
351PhosphorylationAEIEEKGSDGAASSY
HHHHHHCCCCCHHHH
43.8925159151
356PhosphorylationKGSDGAASSYQLKQL
HCCCCCHHHHHHHHH
29.1021406692
357PhosphorylationGSDGAASSYQLKQLE
CCCCCHHHHHHHHHH
16.5128152594
358PhosphorylationSDGAASSYQLKQLEE
CCCCHHHHHHHHHHH
18.5021406692
367 (in isoform 2)Ubiquitination-30.2421906983
3712-HydroxyisobutyrylationEEQNARLKDALVRMR
HHHHHHHHHHHHHHH
35.09-
371UbiquitinationEEQNARLKDALVRMR
HHHHHHHHHHHHHHH
35.09-
383PhosphorylationRMRDLSSSEKQEHVK
HHHCCCCHHHHHHHH
45.4928842319
390AcetylationSEKQEHVKLQKLMEK
HHHHHHHHHHHHHHH
47.2925953088
393AcetylationQEHVKLQKLMEKKNQ
HHHHHHHHHHHHHHH
61.3025953088
398MalonylationLQKLMEKKNQELEVV
HHHHHHHHHHHHHHH
51.0226320211
417PhosphorylationERLQEELSQAESTID
HHHHHHHHHHHHHHH
30.5328348404
439SulfoxidationAALGAEEMVEMLTDR
HHCCHHHHHHHHHHC
2.0230846556
442SulfoxidationGAEEMVEMLTDRNLN
CHHHHHHHHHHCCCC
3.1230846556
4532-HydroxyisobutyrylationRNLNLEEKVRELRET
CCCCHHHHHHHHHHH
36.90-
453MalonylationRNLNLEEKVRELRET
CCCCHHHHHHHHHHH
36.9026320211
453UbiquitinationRNLNLEEKVRELRET
CCCCHHHHHHHHHHH
36.90-
491SulfoxidationELREQLDMAGARVRE
HHHHHHHHHHHHHHH
5.1530846556
501UbiquitinationARVREAQKRVEAAQE
HHHHHHHHHHHHHHH
66.5121906983
501 (in isoform 1)Ubiquitination-66.5121906983
509PhosphorylationRVEAAQETVADYQQT
HHHHHHHHHHHHHHH
14.6528509920
513PhosphorylationAQETVADYQQTIKKY
HHHHHHHHHHHHHHH
7.8728509920
516PhosphorylationTVADYQQTIKKYRQL
HHHHHHHHHHHHHHH
21.1728509920
518MalonylationADYQQTIKKYRQLTA
HHHHHHHHHHHHHHH
47.3326320211
518UbiquitinationADYQQTIKKYRQLTA
HHHHHHHHHHHHHHH
47.33-
541PhosphorylationLTNQQEASVERQQQP
HHHHHHHHHHHHCCC
24.6121815630
556UbiquitinationPPETFDFKIKFAETK
CCCCCCEEEEEHHHH
46.99-
558UbiquitinationETFDFKIKFAETKAH
CCCCEEEEEHHHHHH
38.83-
563UbiquitinationKIKFAETKAHAKAIE
EEEEHHHHHHHHHHH
29.67-
567MalonylationAETKAHAKAIEMELR
HHHHHHHHHHHHHHH
39.7826320211
567UbiquitinationAETKAHAKAIEMELR
HHHHHHHHHHHHHHH
39.78-
571SulfoxidationAHAKAIEMELRQMEV
HHHHHHHHHHHHHHH
4.8630846556
576SulfoxidationIEMELRQMEVAQANR
HHHHHHHHHHHHHHH
3.4630846556
586PhosphorylationAQANRHMSLLTAFMP
HHHHHCHHHHHHHCC
17.6927251275
589PhosphorylationNRHMSLLTAFMPDSF
HHCHHHHHHHCCHHH
24.1227251275
595PhosphorylationLTAFMPDSFLRPGGD
HHHHCCHHHCCCCCC
21.9527251275
618UbiquitinationLMPRLICKAELIRKQ
HHHHHHHHHHHHHHH
37.59-
629UbiquitinationIRKQAQEKFELSENC
HHHHHHHHCCCCCCC
31.87-
637PhosphorylationFELSENCSERPGLRG
CCCCCCCCCCCCCCC
48.5018452278
687PhosphorylationDVYKKVGSLYPEMSA
HHHHHHHHHCHHCCH
27.93-
693PhosphorylationGSLYPEMSAHERSLD
HHHCHHCCHHHHHHH
25.47-
722UbiquitinationVNVEPLTKAIKYYQH
CCHHHHHHHHHHHHH
56.66-
725AcetylationEPLTKAIKYYQHLYS
HHHHHHHHHHHHHHH
42.6425038526
919PhosphorylationYDAERPPSKPPPVEL
CCCCCCCCCCCCHHH
61.5528348404
920UbiquitinationDAERPPSKPPPVELR
CCCCCCCCCCCHHHH
68.28-
924 (in isoform 5)Phosphorylation-15.5128258704
927 (in isoform 5)Phosphorylation-14.5228258704
936PhosphorylationAALRAEITDAEGLGL
HHHHHHCCCCCCCCC
22.21-
941 (in isoform 5)Phosphorylation-5.6728258704
960MalonylationKELKKSLKIKGEELS
HHHHHHCCCCCHHHH
49.8426320211
9622-HydroxyisobutyrylationLKKSLKIKGEELSEA
HHHHCCCCCHHHHHH
59.70-
962UbiquitinationLKKSLKIKGEELSEA
HHHHCCCCCHHHHHH
59.70-
967PhosphorylationKIKGEELSEANVRLS
CCCCHHHHHHHHHHH
37.6325921289
974PhosphorylationSEANVRLSLLEKKLD
HHHHHHHHHHHHHHH
21.9724719451
9782-HydroxyisobutyrylationVRLSLLEKKLDSAAK
HHHHHHHHHHHHHCH
59.62-
978UbiquitinationVRLSLLEKKLDSAAK
HHHHHHHHHHHHHCH
59.62-
982PhosphorylationLLEKKLDSAAKDADE
HHHHHHHHHCHHHHH
40.33-
986 (in isoform 2)Ubiquitination-55.3021906983
993UbiquitinationDADERIEKVQTRLEE
HHHHHHHHHHHHHHH
36.95-
996PhosphorylationERIEKVQTRLEETQA
HHHHHHHHHHHHHHH
39.9621955146
999 (in isoform 2)Ubiquitination-56.56-
1001PhosphorylationVQTRLEETQALLRKK
HHHHHHHHHHHHHHH
15.1221406692
1016SulfoxidationEKEFEETMDALQADI
HHHHHHHHHHHHHCH
2.9930846556
1017 (in isoform 2)Ubiquitination-52.09-
1021 (in isoform 3)Phosphorylation-19.3128258704
1024 (in isoform 3)Phosphorylation-47.7828258704
1034UbiquitinationEAEKAELKQRLNSQS
HHHHHHHHHHHHHHC
25.52-
1038 (in isoform 3)Phosphorylation-39.9428258704
1038 (in isoform 4)Phosphorylation-39.9428258704
1041PhosphorylationKQRLNSQSKRTIEGL
HHHHHHHCCHHHHCC
24.75-
1041 (in isoform 4)Phosphorylation-24.7528258704
1045 (in isoform 2)Ubiquitination-4.6121906983
1055 (in isoform 4)Phosphorylation-21.2328258704
1059 (in isoform 2)Ubiquitination-1.8221906983
1090PhosphorylationGPGLVKDSPLLLQQI
CCCCCCCCHHHHHHH
16.2428555341
1100SulfoxidationLLQQISAMRLHISQL
HHHHHHHHHHHHHHH
3.6030846556
1101 (in isoform 2)Ubiquitination-23.8821906983
1112PhosphorylationSQLQHENSILKGAQM
HHHHHHCCCCHHHHH
26.7224719451
1115UbiquitinationQHENSILKGAQMKAS
HHHCCCCHHHHHHHH
51.00-
1120UbiquitinationILKGAQMKASLASLP
CCHHHHHHHHHHHCC
23.8121906983
1120 (in isoform 1)Ubiquitination-23.8121906983
1133UbiquitinationLPPLHVAKLSHEGPG
CCCEEEEECCCCCCC
49.81-
1149PhosphorylationELPAGALYRKTSQLL
CCCHHHHHHHHHHHH
14.99-
1151UbiquitinationPAGALYRKTSQLLET
CHHHHHHHHHHHHHH
38.68-
1152PhosphorylationAGALYRKTSQLLETL
HHHHHHHHHHHHHHH
16.8328450419
1153PhosphorylationGALYRKTSQLLETLN
HHHHHHHHHHHHHHH
23.1328450419
1158PhosphorylationKTSQLLETLNQLSTH
HHHHHHHHHHHHCCC
30.8627080861
1174PhosphorylationHVVDITRTSPAAKSP
EEEECCCCCCCCCCH
30.3428555341
1179UbiquitinationTRTSPAAKSPSAQLM
CCCCCCCCCHHHHHH
66.0721906983
1179 (in isoform 1)Ubiquitination-66.0721906983
1180PhosphorylationRTSPAAKSPSAQLME
CCCCCCCCHHHHHHH
21.2525850435
1182PhosphorylationSPAAKSPSAQLMEQV
CCCCCCHHHHHHHHH
35.4225850435
1186SulfoxidationKSPSAQLMEQVAQLK
CCHHHHHHHHHHHHH
1.9421406390
1193UbiquitinationMEQVAQLKSLSDTVE
HHHHHHHHHHHHHHH
36.9521906983
1193 (in isoform 1)Ubiquitination-36.9521906983
1201UbiquitinationSLSDTVEKLKDEVLK
HHHHHHHHHHHHHHH
57.40-
1203UbiquitinationSDTVEKLKDEVLKET
HHHHHHHHHHHHHHH
64.01-
1208UbiquitinationKLKDEVLKETVSQRP
HHHHHHHHHHHHCCC
57.42-
1235UbiquitinationSSAFLRAKEEQQDDT
CHHHHHCCHHHCCCC
56.182190698
1235 (in isoform 1)Ubiquitination-56.1821906983
1244PhosphorylationEQQDDTVYMGKVTFS
HHCCCCEEEEEEEEE
11.4025839225
1245SulfoxidationQQDDTVYMGKVTFSC
HCCCCEEEEEEEEEE
3.4930846556

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
19SPhosphorylationKinaseAURKAO14965
GPS
145TPhosphorylationKinaseSLKQ9H2G2
Uniprot
146TPhosphorylationKinaseSLKQ9H2G2
Uniprot
147TPhosphorylationKinaseSLKQ9H2G2
Uniprot
179SPhosphorylationKinasePLK1P53350
Uniprot
212SPhosphorylationKinaseCDK1P06493
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFBXL5Q9UKA1
PMID:17532294

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
145TPhosphorylation

23985322
146TPhosphorylation

23985322
147TPhosphorylation

23985322
179SPhosphorylation

20679239

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 DCTN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BBS4_HUMANBBS4physical
15107855
VIME_HUMANVIMphysical
14600259
DYHC1_HUMANDYNC1H1physical
14600259
DYST_HUMANDSTphysical
14581450
LIS1_HUMANPAFAH1B1physical
11889140
FBXL5_HUMANFBXL5physical
17532294
K0408_HUMANKIAA0408physical
21900206
DYL1_HUMANDYNLL1physical
11056532
DCTN1_HUMANDCTN1physical
11056532
LIS1_HUMANPAFAH1B1physical
11056532
DCTN2_HUMANDCTN2physical
22939629
DYHC1_HUMANDYNC1H1physical
22939629
S30BP_HUMANSAP30BPphysical
22939629
RPB2_HUMANPOLR2Bphysical
22939629
MCM3_HUMANMCM3physical
22939629
RN168_HUMANRNF168physical
22939629
FLNC_HUMANFLNCphysical
22939629
MCCA_HUMANMCCC1physical
22939629
RANB9_HUMANRANBP9physical
22939629
STRN4_HUMANSTRN4physical
22939629
BICD2_HUMANBICD2physical
22956769
TAU_HUMANMAPTphysical
17932487
BZW1_HUMANBZW1physical
26344197
CYFP1_HUMANCYFIP1physical
26344197
EIF2A_HUMANEIF2Aphysical
26344197
PACN3_HUMANPACSIN3physical
26344197
POP1_HUMANPOP1physical
26344197
ARP10_HUMANACTR10physical
26638075
ACTZ_HUMANACTR1Aphysical
26638075
ACTY_HUMANACTR1Bphysical
26638075
AGK_HUMANAGKphysical
26638075
AURKB_HUMANAURKBphysical
26638075
BTF3_HUMANBTF3physical
26638075
BT3L4_HUMANBTF3L4physical
26638075
SKAP_HUMANKNSTRNphysical
26638075
TM256_HUMANTMEM256physical
26638075
CAMP2_HUMANCAMSAP2physical
26638075
CAZA2_HUMANCAPZA2physical
26638075
CCNB1_HUMANCCNB1physical
26638075
CE170_HUMANCEP170physical
26638075
CKAP2_HUMANCKAP2physical
26638075
CKP2L_HUMANCKAP2Lphysical
26638075
CLAP1_HUMANCLASP1physical
26638075
CLH1_HUMANCLTCphysical
26638075
CPVL_HUMANCPVLphysical
26638075
DCLK1_HUMANDCLK1physical
26638075
DCTN2_HUMANDCTN2physical
26638075
DCTN3_HUMANDCTN3physical
26638075
DCTN4_HUMANDCTN4physical
26638075
DCTN6_HUMANDCTN6physical
26638075
DYN2_HUMANDNM2physical
26638075
DYHC1_HUMANDYNC1H1physical
26638075
EBP2_HUMANEBNA1BP2physical
26638075
EMAL1_HUMANEML1physical
26638075
EMAL4_HUMANEML4physical
26638075
ERLN2_HUMANERLIN2physical
26638075
ADRO_HUMANFDXRphysical
26638075
GPTC1_HUMANGPATCH1physical
26638075
GTSE1_HUMANGTSE1physical
26638075
HAUS8_HUMANHAUS8physical
26638075
HMMR_HUMANHMMRphysical
26638075
HYOU1_HUMANHYOU1physical
26638075
IF2B2_HUMANIGF2BP2physical
26638075
IPO7_HUMANIPO7physical
26638075
IPO9_HUMANIPO9physical
26638075
C170B_HUMANCEP170Bphysical
26638075
KIF2A_HUMANKIF2Aphysical
26638075
LASP1_HUMANLASP1physical
26638075
LONM_HUMANLONP1physical
26638075
LUZP1_HUMANLUZP1physical
26638075
MLP3B_HUMANMAP1LC3Bphysical
26638075
MAP1S_HUMANMAP1Sphysical
26638075
MTAP2_HUMANMAP2physical
26638075
MAP7_HUMANMAP7physical
26638075
MA7D1_HUMANMAP7D1physical
26638075
MA7D2_HUMANMAP7D2physical
26638075
MA7D3_HUMANMAP7D3physical
26638075
MAP9_HUMANMAP9physical
26638075
MARE1_HUMANMAPRE1physical
26638075
MARE2_HUMANMAPRE2physical
26638075
MARE3_HUMANMAPRE3physical
26638075
TAU_HUMANMAPTphysical
26638075
MTUS1_HUMANMTUS1physical
26638075
NP1L1_HUMANNAP1L1physical
26638075
NP1L4_HUMANNAP1L4physical
26638075
NMT1_HUMANNMT1physical
26638075
NNTM_HUMANNNTphysical
26638075
NUBP2_HUMANNUBP2physical
26638075
PKHA5_HUMANPLEKHA5physical
26638075
PSDE_HUMANPSMD14physical
26638075
PSMD7_HUMANPSMD7physical
26638075
RAB2A_HUMANRAB2Aphysical
26638075
RAB35_HUMANRAB35physical
26638075
RAB8A_HUMANRAB8Aphysical
26638075
C560_HUMANSDHCphysical
26638075
SKA2_HUMANSKA2physical
26638075
SKA3_HUMANSKA3physical
26638075
SPAG5_HUMANSPAG5physical
26638075
SRSF2_HUMANSRSF2physical
26638075
EMC3_HUMANEMC3physical
26638075
TRI36_HUMANTRIM36physical
26638075
EFTS_HUMANTSFMphysical
26638075
QCR1_HUMANUQCRC1physical
26638075
ZC3HF_HUMANZC3H15physical
26638075
ZN622_HUMANZNF622physical
26638075
ABRAL_HUMANABRACLphysical
26638075
ANXA1_HUMANANXA1physical
26638075
ARHG2_HUMANARHGEF2physical
26638075
HYPK_HUMANHYPKphysical
26638075
CAMP1_HUMANCAMSAP1physical
26638075
C2D1A_HUMANCC2D1Aphysical
26638075
CC124_HUMANCCDC124physical
26638075
CEP41_HUMANCEP41physical
26638075
CEP44_HUMANCEP44physical
26638075
CHTOP_HUMANCHTOPphysical
26638075
CLAP2_HUMANCLASP2physical
26638075
CLIP1_HUMANCLIP1physical
26638075
DCDC2_HUMANDCDC2physical
26638075
DCLK2_HUMANDCLK2physical
26638075
DCTN5_HUMANDCTN5physical
26638075
DLGP5_HUMANDLGAP5physical
26638075
DVL1_HUMANDVL1physical
26638075
DC1I2_HUMANDYNC1I2physical
26638075
FA83D_HUMANFAM83Dphysical
26638075
GA2L3_HUMANGAS2L3physical
26638075
GPX1_HUMANGPX1physical
26638075
HAUS4_HUMANHAUS4physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS7_HUMANHAUS7physical
26638075
CFA97_HUMANCFAP97physical
26638075
KIF14_HUMANKIF14physical
26638075
KIF2C_HUMANKIF2Cphysical
26638075
LS14B_HUMANLSM14Bphysical
26638075
LTV1_HUMANLTV1physical
26638075
MARK2_HUMANMARK2physical
26638075
STK26_HUMANSTK26physical
26638075
MTPN_HUMANMTPNphysical
26638075
NAA10_HUMANNAA10physical
26638075
NAA15_HUMANNAA15physical
26638075
NACAM_HUMANNACAphysical
26638075
NACA_HUMANNACAphysical
26638075
NDC80_HUMANNDC80physical
26638075
NDUA5_HUMANNDUFA5physical
26638075
NEBL_HUMANNEBLphysical
26638075
NEDD1_HUMANNEDD1physical
26638075
NPL4_HUMANNPLOC4physical
26638075
LIS1_HUMANPAFAH1B1physical
26638075
PAPOG_HUMANPAPOLGphysical
26638075
PDZ11_HUMANPDZD11physical
26638075
PRC1_HUMANPRC1physical
26638075
SKA1_HUMANSKA1physical
26638075
SLAI2_HUMANSLAIN2physical
26638075
SPC24_HUMANSPC24physical
26638075
SRP09_HUMANSRP9physical
26638075
SP16H_HUMANSUPT16Hphysical
26638075
TBCEL_HUMANTBCELphysical
26638075
TDRD3_HUMANTDRD3physical
26638075
TSR1_HUMANTSR1physical
26638075
TTF2_HUMANTTF2physical
26638075
TTK_HUMANTTKphysical
26638075
RENT1_HUMANUPF1physical
26638075
YTDC2_HUMANYTHDC2physical
26638075
YTHD1_HUMANYTHDF1physical
26638075
YTHD2_HUMANYTHDF2physical
26638075
ZC21A_HUMANZC2HC1Aphysical
26638075
ACTY_HUMANACTR1Bphysical
28514442
KLHL2_HUMANKLHL2physical
28514442
DCTN2_HUMANDCTN2physical
28514442
ARP10_HUMANACTR10physical
28514442
CAZA2_HUMANCAPZA2physical
28514442
DCTN4_HUMANDCTN4physical
28514442
DCTN3_HUMANDCTN3physical
28514442
ACTZ_HUMANACTR1Aphysical
28514442
DCTN5_HUMANDCTN5physical
28514442
MIPEP_HUMANMIPEPphysical
28514442
DUSTY_HUMANDSTYKphysical
28514442
ACTA_HUMANACTA2physical
28514442
CAPZB_HUMANCAPZBphysical
28514442
DCTN6_HUMANDCTN6physical
27173435
DCTN4_HUMANDCTN4physical
27173435
AHI1_HUMANAHI1physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607641Neuronopathy, distal hereditary motor, 7B (HMN7B)
105400Amyotrophic lateral sclerosis (ALS)
168605Perry syndrome (PERRYS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCTN1_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-230, 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-105 AND THR-108, ANDMASS SPECTROMETRY.

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