DCTN4_HUMAN - dbPTM
DCTN4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCTN4_HUMAN
UniProt AC Q9UJW0
Protein Name Dynactin subunit 4
Gene Name DCTN4
Organism Homo sapiens (Human).
Sequence Length 460
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . In skeletal muscles, demonstrates a punctate distribution along costameres (By similarity). Has a punctate cytoplasmic distribution as well as centrosomal
Protein Description Could have a dual role in dynein targeting and in ACTR1A/Arp1 subunit of dynactin pointed-end capping. Could be involved in ACTR1A pointed-end binding and in additional roles in linking dynein and dynactin to the cortical cytoskeleton..
Protein Sequence MASLLQSDRVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHTQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSDKYGLGTRLQRPRAGASISTLAGLSLKEGEDQKEIKIEPAQAVDEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDFQPVCASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLFECEEGDPDDINSTAKVVVPPKELVLAGKDAAAEYDELAEPQDFQDDPDIIAFRKANKVGIFIKVTPQREEGEVTVCFKMKHDFKNLAAPIRPIEESDQGTEVIWLTQHVELSLGPLLP
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
2Acetylation------MASLLQSDR
------CCHHHCCCE		14.6422223895
9MethylationASLLQSDRVLYLVQG
CHHHCCCEEEEEECC		26.11-
18UbiquitinationLYLVQGEKKVRAPLS
EEEECCCHHCCCCHH		64.4921890473
19UbiquitinationYLVQGEKKVRAPLSQ
EEECCCHHCCCCHHH		32.43-
25PhosphorylationKKVRAPLSQLYFCRY
HHCCCCHHHHHHHHH		19.6526074081
28PhosphorylationRAPLSQLYFCRYCSE
CCCHHHHHHHHHHHH		7.9326074081
32PhosphorylationSQLYFCRYCSELRSL
HHHHHHHHHHHHCCC		11.0826074081
34PhosphorylationLYFCRYCSELRSLEC
HHHHHHHHHHCCCEE		30.6326074081
60PhosphorylationSCLENMPSAEAKLKK
HHHHHCCHHHHHHHC		28.1530243723
69 (in isoform 2)Ubiquitination-29.79-
84PhosphorylationPGCMHTLSTRATSIS
CCHHHHCCCCCCCHH		19.5924719451
85PhosphorylationGCMHTLSTRATSIST
CHHHHCCCCCCCHHH		27.6927080861
88PhosphorylationHTLSTRATSISTQLP
HHCCCCCCCHHHCCC		24.2528857561
89PhosphorylationTLSTRATSISTQLPD
HCCCCCCCHHHCCCC		17.3528857561
89 (in isoform 2)Ubiquitination-17.35-
91PhosphorylationSTRATSISTQLPDDP
CCCCCCHHHCCCCCH		15.1827251275
100 (in isoform 2)Ubiquitination-50.33-
101PhosphorylationLPDDPAKTTMKKAYY
CCCCHHHHHHHHHHH		33.94-
102PhosphorylationPDDPAKTTMKKAYYL
CCCHHHHHHHHHHHH		26.7028555341
105MalonylationPAKTTMKKAYYLACG
HHHHHHHHHHHHHHC		30.6926320211
105AcetylationPAKTTMKKAYYLACG
HHHHHHHHHHHHHHC		30.6926051181
107PhosphorylationKTTMKKAYYLACGFC
HHHHHHHHHHHHCCC		14.1129496907
108PhosphorylationTTMKKAYYLACGFCR
HHHHHHHHHHHCCCC		7.8429496907
124 (in isoform 2)Ubiquitination-18.36-
126UbiquitinationRDVGMADKSVASGGW
CCCCCCCCCHHCCCC		36.9721890473
127PhosphorylationDVGMADKSVASGGWQ
CCCCCCCCHHCCCCC		24.3821406692
130PhosphorylationMADKSVASGGWQEPE
CCCCCHHCCCCCCCC		35.3721406692
141PhosphorylationQEPENPHTQRMNKLI
CCCCCHHHHHHHHHH		21.0821406692
146UbiquitinationPHTQRMNKLIEYYQQ
HHHHHHHHHHHHHHH		41.3121890473
146SumoylationPHTQRMNKLIEYYQQ
HHHHHHHHHHHHHHH		41.31-
146SumoylationPHTQRMNKLIEYYQQ
HHHHHHHHHHHHHHH		41.31-
146UbiquitinationPHTQRMNKLIEYYQQ
HHHHHHHHHHHHHHH		41.3121890473
149 (in isoform 2)Ubiquitination-48.93-
150PhosphorylationRMNKLIEYYQQLAQK
HHHHHHHHHHHHHHH		10.2827642862
151PhosphorylationMNKLIEYYQQLAQKE
HHHHHHHHHHHHHHH		4.1327642862
157UbiquitinationYYQQLAQKEKVERDR
HHHHHHHHHHHHHHH		54.6221890473
159UbiquitinationQQLAQKEKVERDRKK
HHHHHHHHHHHHHHH		57.33-
173PhosphorylationKLARRRNYMPLAFSD
HHHHHHCCCCCHHHC		9.7821945579
179PhosphorylationNYMPLAFSDKYGLGT
CCCCCHHHCCCCCCC		27.8221945579
181UbiquitinationMPLAFSDKYGLGTRL
CCCHHHCCCCCCCCC		39.7721890473
181UbiquitinationMPLAFSDKYGLGTRL
CCCHHHCCCCCCCCC		39.7721890473
182PhosphorylationPLAFSDKYGLGTRLQ
CCHHHCCCCCCCCCC		23.67-
196PhosphorylationQRPRAGASISTLAGL
CCCCCCCCHHHHHCC		19.0225693802
198PhosphorylationPRAGASISTLAGLSL
CCCCCCHHHHHCCCC		18.1829978859
199PhosphorylationRAGASISTLAGLSLK
CCCCCHHHHHCCCCC		20.9628060719
203PhosphorylationSISTLAGLSLKEGED
CHHHHHCCCCCCCCC		4.5124719451
204PhosphorylationISTLAGLSLKEGEDQ
HHHHHCCCCCCCCCC		36.1628060719
206PhosphorylationTLAGLSLKEGEDQKE
HHHCCCCCCCCCCCE		61.3727251275
206UbiquitinationTLAGLSLKEGEDQKE
HHHCCCCCCCCCCCE		61.3721890473
206AcetylationTLAGLSLKEGEDQKE
HHHCCCCCCCCCCCE		61.3718528655
212UbiquitinationLKEGEDQKEIKIEPA
CCCCCCCCEEEEECC		73.9721890473
215SumoylationGEDQKEIKIEPAQAV
CCCCCEEEEECCCCC		41.9528112733
215UbiquitinationGEDQKEIKIEPAQAV
CCCCCEEEEECCCCC		41.9521890473
232PhosphorylationVEPLPEDYYTRPVNL
CCCCCCCCCCCCCCH		12.6922210691
233PhosphorylationEPLPEDYYTRPVNLT
CCCCCCCCCCCCCHH		14.4822210691
234PhosphorylationPLPEDYYTRPVNLTE
CCCCCCCCCCCCHHH		23.4422210691
267UbiquitinationSQLYPRHKHLLIKRS
HHCCHHHHHHHHHHH		36.91-
274PhosphorylationKHLLIKRSLRCRKCE
HHHHHHHHHHHCCCC		18.37-
279UbiquitinationKRSLRCRKCEHNLSK
HHHHHHCCCCCCCCC		47.83-
286UbiquitinationKCEHNLSKPEFNPTS
CCCCCCCCCCCCCCC		52.30-
295UbiquitinationEFNPTSIKFKIQLVA
CCCCCCCEEEEEEEE		40.13-
313 (in isoform 2)Ubiquitination-32.30-
370UbiquitinationKELVLAGKDAAAEYD
HHHEECCCCHHHHCH		38.2921890473
376PhosphorylationGKDAAAEYDELAEPQ
CCCHHHHCHHHCCCC		15.2528796482
407PhosphorylationVGIFIKVTPQREEGE
EEEEEEEECCCCCCE		14.54-
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 DCTN4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCTN4_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 DCTN4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTZ_HUMANACTR1Aphysical
10671518
ARP10_HUMANACTR10physical
22863883
ACTZ_HUMANACTR1Aphysical
22863883
ACTY_HUMANACTR1Bphysical
22863883
DCTN2_HUMANDCTN2physical
22863883
SEH1_HUMANSEH1Lphysical
22863883
ACTZ_HUMANACTR1Aphysical
26344197
ACTY_HUMANACTR1Bphysical
26344197
CAZA1_HUMANCAPZA1physical
26344197
CAZA2_HUMANCAPZA2physical
26344197
CAPZB_HUMANCAPZBphysical
26344197
DCTN1_HUMANDCTN1physical
26344197
DCTN2_HUMANDCTN2physical
26344197
DCTN5_HUMANDCTN5physical
26344197
DCTN6_HUMANDCTN6physical
26344197
IF4G1_HUMANEIF4G1physical
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 DCTN4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 1), AND MASSSPECTROMETRY.

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