BICD2_HUMAN - dbPTM
BICD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BICD2_HUMAN
UniProt AC Q8TD16
Protein Name Protein bicaudal D homolog 2
Gene Name BICD2
Organism Homo sapiens (Human).
Sequence Length 824
Subcellular Localization Golgi apparatus . Cytoplasm, cytoskeleton . Cytoplasm . Nucleus envelope . Nucleus, nuclear pore complex . In interphase cells mainly localizes to the Golgi complex and colocalizes with dynactin at microtubule plus ends (By similarity). Localizes to
Protein Description Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates and stabilizes the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). Facilitates the binding of RAB6A to the Golgi by stabilizing its GTP-bound form. Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport via its interaction with RAB6A and recruitment of the dynein-dynactin motor complex. [PubMed: 25962623 Contributes to nuclear and centrosomal positioning prior to mitotic entry through regulation of both dynein and kinesin-1. During G2 phase of the cell cycle, associates with RANBP2 at the nuclear pores and recruits dynein and dynactin to the nuclear envelope to ensure proper positioning of the nucleus relative to centrosomes prior to the onset of mitosis (By similarity]
Protein Sequence MSAPSEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLTNTQSENERLASVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNSLRKELSHYMSINDSFYTSHLHVSLDGLKFSDDAAEPNNDAEALVNGFEHGGLAKLPLDNKTSTPKKEGLAPPSPSLVSDLLSELNISEIQKLKQQLMQMEREKAGLLATLQDTQKQLEHTRGSLSEQQEKVTRLTENLSALRRLQASKERQTALDNEKDRDSHEDGDYYEVDINGPEILACKYHVAVAEAGELREQLKALRSTHEAREAQHAEEKGRYEAEGQALTEKVSLLEKASRQDRELLARLEKELKKVSDVAGETQGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYYREGQGGAGRTSPGGRTSPEARGRRSPILLPKGLLAPEAGRADGGTGDSSPSPGSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLELDHEQTRRGRAKAAPKTKPATPSL
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------MSAPSEEEE
------CCCCCHHHH		49.2222814378
2Phosphorylation------MSAPSEEEE
------CCCCCHHHH		49.2227067055
2 (in isoform 2)Acetylation-49.22-
30PhosphorylationRAEVKRLSHELAETT
HHHHHHHHHHHHHHH		20.9629214152
36PhosphorylationLSHELAETTREKIQA
HHHHHHHHHHHHHHH		26.0828555341
37PhosphorylationSHELAETTREKIQAA
HHHHHHHHHHHHHHH		28.4728555341
54UbiquitinationGLAVLEEKHQLKLQF
HHHHHHHHHHHHHHH		27.55-
68 (in isoform 2)Phosphorylation-16.6727642862
98PhosphorylationKVAADGESREESLIQ
HHCCCCCCHHHHHHH		50.9925627689
102PhosphorylationDGESREESLIQESAS
CCCCHHHHHHHHHHC		26.4821815630
110UbiquitinationLIQESASKEQYYVRK
HHHHHHCHHHHHHHH		48.86-
126UbiquitinationLELQTELKQLRNVLT
HHHHHHHHHHHHHHH		40.84-
144PhosphorylationSENERLASVAQELKE
CHHHHHHHHHHHHHH		23.6828555341
181PhosphorylationEARLLQDYSELEEEN
HHHHHHCHHHHHHHC		7.3518691976
181 (in isoform 2)Phosphorylation-7.35-
182PhosphorylationARLLQDYSELEEENI
HHHHHCHHHHHHHCC		43.9525159151
182 (in isoform 2)Phosphorylation-43.95-
190PhosphorylationELEEENISLQKQVSV
HHHHHCCCHHHHHHH		36.0125159151
190 (in isoform 2)Phosphorylation-36.01-
193UbiquitinationEENISLQKQVSVLRQ
HHCCCHHHHHHHHHH		58.94-
224PhosphorylationEETEYLNSQLEDAIR
HHHHHHHHHHHHHHH		33.2825159151
224 (in isoform 2)Phosphorylation-33.28-
236PhosphorylationAIRLKEISERQLEEA
HHHHHHHCHHHHHHH		28.0223312004
248UbiquitinationEEALETLKTEREQKN
HHHHHHHHHHHHHHH		56.62-
256PhosphorylationTEREQKNSLRKELSH
HHHHHHHHHHHHHHH		36.2626055452
264PhosphorylationLRKELSHYMSINDSF
HHHHHHHHHHHCCCC		6.81-
272PhosphorylationMSINDSFYTSHLHVS
HHHCCCCCCCCEEEE		15.98-
286PhosphorylationSLDGLKFSDDAAEPN
EECCCCCCCCCCCCC		32.7517192257
286 (in isoform 2)Phosphorylation-32.75-
310UbiquitinationFEHGGLAKLPLDNKT
CCCCCCCCCCCCCCC		56.53-
317PhosphorylationKLPLDNKTSTPKKEG
CCCCCCCCCCCCCCC		44.0530108239
318PhosphorylationLPLDNKTSTPKKEGL
CCCCCCCCCCCCCCC		44.3025159151
319PhosphorylationPLDNKTSTPKKEGLA
CCCCCCCCCCCCCCC		44.3425159151
319 (in isoform 2)Phosphorylation-44.34-
329PhosphorylationKEGLAPPSPSLVSDL
CCCCCCCCHHHHHHH		26.5125159151
329 (in isoform 2)Phosphorylation-26.5127251275
331PhosphorylationGLAPPSPSLVSDLLS
CCCCCCHHHHHHHHH		45.8225159151
331 (in isoform 2)Phosphorylation-45.82-
334PhosphorylationPPSPSLVSDLLSELN
CCCHHHHHHHHHHCC		28.0325159151
338PhosphorylationSLVSDLLSELNISEI
HHHHHHHHHCCHHHH		47.5417192257
338 (in isoform 2)Phosphorylation-47.54-
343PhosphorylationLLSELNISEIQKLKQ
HHHHCCHHHHHHHHH		27.8117192257
343 (in isoform 2)Phosphorylation-27.81-
349UbiquitinationISEIQKLKQQLMQME
HHHHHHHHHHHHHHH		42.93-
349 (in isoform 2)Ubiquitination-42.93-
359UbiquitinationLMQMEREKAGLLATL
HHHHHHHHHHHHHHH		54.71-
365PhosphorylationEKAGLLATLQDTQKQ
HHHHHHHHHHHHHHH		25.5622210691
369PhosphorylationLLATLQDTQKQLEHT
HHHHHHHHHHHHHHH		25.3822210691
371UbiquitinationATLQDTQKQLEHTRG
HHHHHHHHHHHHHCC		59.97-
376PhosphorylationTQKQLEHTRGSLSEQ
HHHHHHHHCCCHHHH		27.6125627689
379PhosphorylationQLEHTRGSLSEQQEK
HHHHHCCCHHHHHHH		25.9826462736
379 (in isoform 2)Phosphorylation-25.98-
386UbiquitinationSLSEQQEKVTRLTEN
CHHHHHHHHHHHHHH		44.56-
391PhosphorylationQEKVTRLTENLSALR
HHHHHHHHHHHHHHH		21.3818691976
391 (in isoform 2)Phosphorylation-21.38-
395PhosphorylationTRLTENLSALRRLQA
HHHHHHHHHHHHHHH		36.5225159151
395 (in isoform 2)Phosphorylation-36.52-
403PhosphorylationALRRLQASKERQTAL
HHHHHHHHHHHHHHH		23.30-
408PhosphorylationQASKERQTALDNEKD
HHHHHHHHHHHCCCC		35.0929978859
418PhosphorylationDNEKDRDSHEDGDYY
HCCCCCCCCCCCCEE		29.6630576142
418 (in isoform 2)Phosphorylation-29.6627642862
424PhosphorylationDSHEDGDYYEVDING
CCCCCCCEEEEECCC		13.6830576142
424 (in isoform 2)Phosphorylation-13.6827642862
425PhosphorylationSHEDGDYYEVDINGP
CCCCCCEEEEECCCH		17.7630576142
425 (in isoform 2)Phosphorylation-17.7627642862
458PhosphorylationEQLKALRSTHEAREA
HHHHHHHHHHHHHHH		34.66-
459PhosphorylationQLKALRSTHEAREAQ
HHHHHHHHHHHHHHH		19.80-
482PhosphorylationEAEGQALTEKVSLLE
HHHHHHHHHHHHHHH		36.4528555341
484UbiquitinationEGQALTEKVSLLEKA
HHHHHHHHHHHHHHH		31.71-
486PhosphorylationQALTEKVSLLEKASR
HHHHHHHHHHHHHCH		38.0029214152
490UbiquitinationEKVSLLEKASRQDRE
HHHHHHHHHCHHHHH		52.19-
504UbiquitinationELLARLEKELKKVSD
HHHHHHHHHHHHHHH		73.30-
510PhosphorylationEKELKKVSDVAGETQ
HHHHHHHHHHCCCCC		34.94-
538PhosphorylationSEELANLYHHVCMCN
CHHHHHHHHHHHCCC		6.95-
556PhosphorylationPNRVMLDYYREGQGG
CCEEEEECCCCCCCC		10.64-
557PhosphorylationNRVMLDYYREGQGGA
CEEEEECCCCCCCCC		11.23-
567PhosphorylationGQGGAGRTSPGGRTS
CCCCCCCCCCCCCCC		38.0523401153
567 (in isoform 2)Phosphorylation-38.0521406692
568PhosphorylationQGGAGRTSPGGRTSP
CCCCCCCCCCCCCCH		21.8625159151
568 (in isoform 2)Phosphorylation-21.8627251275
573PhosphorylationRTSPGGRTSPEARGR
CCCCCCCCCHHHCCC		52.4923401153
573 (in isoform 2)Phosphorylation-52.49-
574PhosphorylationTSPGGRTSPEARGRR
CCCCCCCCHHHCCCC		21.2728355574
574 (in isoform 2)Phosphorylation-21.2721406692
582PhosphorylationPEARGRRSPILLPKG
HHHCCCCCCCCCCCC		18.2222167270
582 (in isoform 2)Phosphorylation-18.2221406692
602PhosphorylationAGRADGGTGDSSPSP
CCCCCCCCCCCCCCC		43.2625850435
605PhosphorylationADGGTGDSSPSPGSS
CCCCCCCCCCCCCCC		45.5626055452
605 (in isoform 2)Phosphorylation-45.5627251275
606PhosphorylationDGGTGDSSPSPGSSL
CCCCCCCCCCCCCCC		33.8525394399
608PhosphorylationGTGDSSPSPGSSLPS
CCCCCCCCCCCCCCC		43.7926055452
608 (in isoform 2)Phosphorylation-43.79-
611PhosphorylationDSSPSPGSSLPSPLS
CCCCCCCCCCCCCCC		31.8930576142
612PhosphorylationSSPSPGSSLPSPLSD
CCCCCCCCCCCCCCC		50.6525850435
615PhosphorylationSPGSSLPSPLSDPRR
CCCCCCCCCCCCCCC		43.7128176443
615 (in isoform 2)Phosphorylation-43.7127251275
618PhosphorylationSSLPSPLSDPRREPM
CCCCCCCCCCCCCCC		49.2925850435
628PhosphorylationRREPMNIYNLIAIIR
CCCCCCHHHHHHHHH		10.0229523821
647MethylationHLQAAVDRTTELSRQ
HHHHHHHHHHHHHHH		36.63-
648PhosphorylationLQAAVDRTTELSRQR
HHHHHHHHHHHHHHH		21.84-
649PhosphorylationQAAVDRTTELSRQRI
HHHHHHHHHHHHHHH		35.50-
652PhosphorylationVDRTTELSRQRIASQ
HHHHHHHHHHHHHHC		21.82-
658PhosphorylationLSRQRIASQELGPAV
HHHHHHHHCCCCCCC		23.0927050516
658 (in isoform 2)Phosphorylation-23.0927251275
680UbiquitinationMEEILKLKSLLSTKR
HHHHHHHHHHHCCCH		37.15-
684PhosphorylationLKLKSLLSTKREQIT
HHHHHHHCCCHHHHH		36.8624719451
686UbiquitinationLKSLLSTKREQITTL
HHHHHCCCHHHHHHH		51.03-
691PhosphorylationSTKREQITTLRTVLK
CCCHHHHHHHHHHHH		21.3317081983
691 (in isoform 2)Phosphorylation-21.33-
692PhosphorylationTKREQITTLRTVLKA
CCHHHHHHHHHHHHH		18.8328122231
695PhosphorylationEQITTLRTVLKANKQ
HHHHHHHHHHHHCHH		33.0528122231
703PhosphorylationVLKANKQTAEVALAN
HHHHCHHHHHHHHHH		26.7921406692
712AcetylationEVALANLKSKYENEK
HHHHHHHHHHHHHHH		44.717671011
714AcetylationALANLKSKYENEKAM
HHHHHHHHHHHHHHH		55.807711401
723PhosphorylationENEKAMVTETMMKLR
HHHHHHHHHHHHHHH		16.80-
734UbiquitinationMKLRNELKALKEDAA
HHHHHHHHHHHHHHH		45.56-
745PhosphorylationEDAATFSSLRAMFAT
HHHHHHHHHHHHHHH		20.0624719451
780PhosphorylationDEKKTLNSLLRMAIQ
HHHHHHHHHHHHHHH		31.7127134283
789UbiquitinationLRMAIQQKLALTQRL
HHHHHHHHHHHHHHH		21.25-
806PhosphorylationLELDHEQTRRGRAKA
HHCCHHHHHHHCCCC		21.2428555341
817PhosphorylationRAKAAPKTKPATPSL
CCCCCCCCCCCCCCC		41.0023403867
821PhosphorylationAPKTKPATPSL----
CCCCCCCCCCC----		23.1825159151
821 (in isoform 2)Phosphorylation-23.1828348404
823PhosphorylationKTKPATPSL------
CCCCCCCCC------		42.2125159151
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 BICD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BICD2_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 BICD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTZ_HUMANACTR1Aphysical
11483508
DYHC1_HUMANDYNC1H1physical
11483508
RAB6A_HUMANRAB6Aphysical
12447383
DC1I1_HUMANDYNC1I1physical
11483508
LIS1_HUMANPAFAH1B1physical
22956769
RAB6A_HUMANRAB6Aphysical
16473624
NEK9_HUMANNEK9physical
11864968
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615290Spinal muscular atrophy, lower extremity-predominant 2, autosomal dominant (SMALED2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BICD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-823, ANDMASS 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-182; SER-190; SER-582;THR-821 AND SER-823, AND MASS SPECTROMETRY.
"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-182; SER-190; SER-224;SER-286; SER-329; SER-331; SER-338; SER-343; SER-395; SER-582; THR-821AND SER-823, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASSSPECTROMETRY.
"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-582 AND THR-691, 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-582, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-424, AND MASSSPECTROMETRY.

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