BICD1_HUMAN - dbPTM
BICD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BICD1_HUMAN
UniProt AC Q96G01
Protein Name Protein bicaudal D homolog 1
Gene Name BICD1
Organism Homo sapiens (Human).
Sequence Length 975
Subcellular Localization Golgi apparatus.
Protein Description Regulates coat complex coatomer protein I (COPI)-independent Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin motor complex..
Protein Sequence MAAEEVLQTVDHYKTEIERLTKELTETTHEKIQAAEYGLVVLEEKLTLKQQYDELEAEYDSLKQELEQLKEAFGQSFSIHRKVAEDGETREETLLQESASKEAYYLGKILEMQNELKQSRAVVTNVQAENERLTAVVQDLKENNEMVELQRIRMKDEIREYKFREARLLQDYTELEEENITLQKLVSTLKQNQVEYEGLKHEIKRFEEETVLLNSQLEDAIRLKEIAEHQLEEALETLKNEREQKNNLRKELSQYISLNDNHISISVDGLKFAEDGSEPNNDDKMNGHIHGPLVKLNGDYRTPTLRKGESLNPVSDLFSELNISEIQKLKQQLMQVEREKAILLANLQESQTQLEHTKGALTEQHERVHRLTEHVNAMRGLQSSKELKAELDGEKGRDSGEEAHDYEVDINGLEILECKYRVAVTEVIDLKAEIKALKEKYNKSVENYTDEKAKYESKIQMYDEQVTSLEKTTKESGEKMAHMEKELQKMTSIANENHSTLNTAQDELVTFSEELAQLYHHVCLCNNETPNRVMLDYYRQSRVTRSGSLKGPDDPRGLLSPRLARRGVSSPVETRTSSEPVAKESTEASKEPSPTKTPTISPVITAPPSSPVLDTSDIRKEPMNIYNLNAIIRDQIKHLQKAVDRSLQLSRQRAAARELAPMIDKDKEALMEEILKLKSLLSTKREQIATLRAVLKANKQTAEVALANLKNKYENEKAMVTETMTKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNTLLRMAIQQKLALTQRLEDLEFDHEQSRRSKGKLGKSKIGSPKVSGEASVTVPTIDTYLLHSQGPQTPNIRVSSGTQRKRQFSPSLCDQSRPRTSGASYLQNLLRVPPDPTSTESFLLKGPPSMSEFIQGHRLSKEKRLTVAPPDCQQPAASVPPQCSQLAGRQDCPTVSPDTALPEEQPHSSSQCAPLHCLSKPPHP
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
9PhosphorylationAAEEVLQTVDHYKTE
CHHHHHHHHHHHHHH
24.6020049867
13PhosphorylationVLQTVDHYKTEIERL
HHHHHHHHHHHHHHH
18.3620049867
14UbiquitinationLQTVDHYKTEIERLT
HHHHHHHHHHHHHHH
35.9429967540
15PhosphorylationQTVDHYKTEIERLTK
HHHHHHHHHHHHHHH
34.7224043423
21PhosphorylationKTEIERLTKELTETT
HHHHHHHHHHHHHHH
28.7920049867
22UbiquitinationTEIERLTKELTETTH
HHHHHHHHHHHHHHH
56.1529967540
45MethylationGLVVLEEKLTLKQQY
CCEEEEEECCHHHHH
37.08-
47PhosphorylationVVLEEKLTLKQQYDE
EEEEEECCHHHHHHH
42.8724719451
52PhosphorylationKLTLKQQYDELEAEY
ECCHHHHHHHHHHHH
14.6428122231
61PhosphorylationELEAEYDSLKQELEQ
HHHHHHHHHHHHHHH
36.24-
76PhosphorylationLKEAFGQSFSIHRKV
HHHHHCCCCCHHHHH
22.7228555341
82UbiquitinationQSFSIHRKVAEDGET
CCCCHHHHHHCCCCC
31.4729967540
101UbiquitinationLLQESASKEAYYLGK
HHHHHHCHHHHHHHH
46.1929967540
117UbiquitinationLEMQNELKQSRAVVT
HHHHHHHHHCCEEEC
39.80-
184UbiquitinationEENITLQKLVSTLKQ
HHCCCHHHHHHHHHH
54.7029967540
188PhosphorylationTLQKLVSTLKQNQVE
CHHHHHHHHHHCCCC
30.4123403867
190UbiquitinationQKLVSTLKQNQVEYE
HHHHHHHHHCCCCCC
47.4929967540
215PhosphorylationEETVLLNSQLEDAIR
HHHHHHCHHHHHHHH
35.79-
224UbiquitinationLEDAIRLKEIAEHQL
HHHHHHHHHHHHHHH
36.9129967540
239UbiquitinationEEALETLKNEREQKN
HHHHHHHHHHHHHHH
65.2729967540
300PhosphorylationLVKLNGDYRTPTLRK
EEECCCCCCCCCCCC
20.13-
302PhosphorylationKLNGDYRTPTLRKGE
ECCCCCCCCCCCCCC
17.88-
304PhosphorylationNGDYRTPTLRKGESL
CCCCCCCCCCCCCCC
38.28-
307UbiquitinationYRTPTLRKGESLNPV
CCCCCCCCCCCCCCH
70.8729967540
310PhosphorylationPTLRKGESLNPVSDL
CCCCCCCCCCCHHHH
41.9628857561
315PhosphorylationGESLNPVSDLFSELN
CCCCCCHHHHHHHCC
29.8328122231
319PhosphorylationNPVSDLFSELNISEI
CCHHHHHHHCCHHHH
48.7728122231
328UbiquitinationLNISEIQKLKQQLMQ
CCHHHHHHHHHHHHH
64.4129967540
330UbiquitinationISEIQKLKQQLMQVE
HHHHHHHHHHHHHHH
42.9329967540
340UbiquitinationLMQVEREKAILLANL
HHHHHHHHHHHHHHH
47.1229967540
358UbiquitinationQTQLEHTKGALTEQH
HHHHHHHHCHHHHHH
44.0629967540
399PhosphorylationDGEKGRDSGEEAHDY
CCCCCCCCCCCCCCE
46.9030576142
406PhosphorylationSGEEAHDYEVDINGL
CCCCCCCEEEECCCE
14.1628796482
420PhosphorylationLEILECKYRVAVTEV
EEEEEEEEEEEEEEH
23.2122210691
425PhosphorylationCKYRVAVTEVIDLKA
EEEEEEEEEHHHHHH
18.1322210691
443UbiquitinationALKEKYNKSVENYTD
HHHHHHHHCHHCCCC
53.43-
448PhosphorylationYNKSVENYTDEKAKY
HHHCHHCCCCHHHHH
11.3222817900
452UbiquitinationVENYTDEKAKYESKI
HHCCCCHHHHHHHHH
53.65-
454UbiquitinationNYTDEKAKYESKIQM
CCCCHHHHHHHHHHH
61.69-
455PhosphorylationYTDEKAKYESKIQMY
CCCHHHHHHHHHHHH
30.2322817900
471AcetylationEQVTSLEKTTKESGE
HHHHCHHHHHHHHHH
67.787629253
472PhosphorylationQVTSLEKTTKESGEK
HHHCHHHHHHHHHHH
33.4530631047
473PhosphorylationVTSLEKTTKESGEKM
HHCHHHHHHHHHHHH
43.8330631047
479AcetylationTTKESGEKMAHMEKE
HHHHHHHHHHHHHHH
44.937707145
485UbiquitinationEKMAHMEKELQKMTS
HHHHHHHHHHHHHHH
57.03-
537PhosphorylationPNRVMLDYYRQSRVT
CCCCHHHHHHHCCCC
9.15-
538PhosphorylationNRVMLDYYRQSRVTR
CCCHHHHHHHCCCCC
11.22-
546PhosphorylationRQSRVTRSGSLKGPD
HHCCCCCCCCCCCCC
24.3023401153
548PhosphorylationSRVTRSGSLKGPDDP
CCCCCCCCCCCCCCC
28.3130266825
560PhosphorylationDDPRGLLSPRLARRG
CCCCCCCCHHHHHCC
17.0222167270
569PhosphorylationRLARRGVSSPVETRT
HHHHCCCCCCCCCCC
31.5825159151
570PhosphorylationLARRGVSSPVETRTS
HHHCCCCCCCCCCCC
30.4725159151
574PhosphorylationGVSSPVETRTSSEPV
CCCCCCCCCCCCCCC
39.2129396449
576PhosphorylationSSPVETRTSSEPVAK
CCCCCCCCCCCCCCH
43.98-
585PhosphorylationSEPVAKESTEASKEP
CCCCCHHCCCCCCCC
30.7317139249
586PhosphorylationEPVAKESTEASKEPS
CCCCHHCCCCCCCCC
36.3425850435
589PhosphorylationAKESTEASKEPSPTK
CHHCCCCCCCCCCCC
31.1825850435
593PhosphorylationTEASKEPSPTKTPTI
CCCCCCCCCCCCCCC
46.4229255136
595PhosphorylationASKEPSPTKTPTISP
CCCCCCCCCCCCCCC
52.4629255136
597PhosphorylationKEPSPTKTPTISPVI
CCCCCCCCCCCCCCC
28.3017139249
599PhosphorylationPSPTKTPTISPVITA
CCCCCCCCCCCCCCC
39.0425159151
601PhosphorylationPTKTPTISPVITAPP
CCCCCCCCCCCCCCC
18.6525159151
605PhosphorylationPTISPVITAPPSSPV
CCCCCCCCCCCCCCC
33.0926074081
609PhosphorylationPVITAPPSSPVLDTS
CCCCCCCCCCCCCCH
46.3329255136
610PhosphorylationVITAPPSSPVLDTSD
CCCCCCCCCCCCCHH
25.4629255136
615PhosphorylationPSSPVLDTSDIRKEP
CCCCCCCCHHHCCCC
24.9229255136
616PhosphorylationSSPVLDTSDIRKEPM
CCCCCCCHHHCCCCC
30.6129255136
620UbiquitinationLDTSDIRKEPMNIYN
CCCHHHCCCCCCCCC
67.5129967540
678UbiquitinationMEEILKLKSLLSTKR
HHHHHHHHHHHCCCH
37.15-
682PhosphorylationLKLKSLLSTKREQIA
HHHHHHHCCCHHHHH
36.8624719451
684UbiquitinationLKSLLSTKREQIATL
HHHHHCCCHHHHHHH
51.03-
701PhosphorylationVLKANKQTAEVALAN
HHHHCHHHHHHHHHH
26.7921406692
710AcetylationEVALANLKNKYENEK
HHHHHHHHHHHHCHH
51.727671021
713PhosphorylationLANLKNKYENEKAMV
HHHHHHHHHCHHHHH
33.1222817900
732UbiquitinationTKLRNELKALKEDAA
HHHHHHHHHHHHHHH
45.56-
743PhosphorylationEDAATFSSLRAMFAT
HHHHHHHHHHHHHHH
20.0624719451
778PhosphorylationDEKKTLNTLLRMAIQ
HHHHHHHHHHHHHHH
30.2225247763
787UbiquitinationLRMAIQQKLALTQRL
HHHHHHHHHHHHHHH
21.25-
804PhosphorylationLEFDHEQSRRSKGKL
HCCCHHHHHHHCCCC
27.0323401153
823 (in isoform 4)Phosphorylation-37.16-
829 (in isoform 4)Phosphorylation-3.54-
844PhosphorylationLHSQGPQTPNIRVSS
ECCCCCCCCCEEECC
22.8025159151
860PhosphorylationTQRKRQFSPSLCDQS
CCCCCCCCHHHCCCC
12.7727732954
865 (in isoform 3)Phosphorylation-55.5818220336
866 (in isoform 3)Phosphorylation-40.1018220336
902PhosphorylationLKGPPSMSEFIQGHR
HCCCCCHHHHHCCCC
33.4230576142
911PhosphorylationFIQGHRLSKEKRLTV
HHCCCCCCCCCCEEE
38.4330576142

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 BICD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BICD1_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 BICD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT3_HUMANSTAT3physical
21988832
MK14_HUMANMAPK14physical
21988832
RAB6A_HUMANRAB6Aphysical
16473624

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 BICD1_HUMAN

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Related Literatures of Post-Translational Modification

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