BORC6_HUMAN - dbPTM
BORC6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BORC6_HUMAN
UniProt AC Q96GS4
Protein Name BLOC-1-related complex subunit 6 {ECO:0000305}
Gene Name BORCS6 {ECO:0000312|HGNC:HGNC:25939}
Organism Homo sapiens (Human).
Sequence Length 357
Subcellular Localization Lysosome membrane .
Protein Description As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor..
Protein Sequence MESSRGRPGPETDLLAVAEHQALVFGGGPGRTSSEPPAGLRVSGEEETENVGGANRHPRTSPKTSSCGVVHRPEREALENEPGPQGTLSGAGSRRGAPGAEHEPSLSSRHKNPAPPEGKPSSGRDCRRGGPGGGMDVEQQEEEDNDEEAAAGSRAGRSFSSRLQDSRSLDGLSEACGGAGSSGSAESGAGGGRRATISSPLELEGTVSRHGDLTHFVANNLQLKIRLSGAPPPPPSAPARPCPAPAPTPTPAIPPIDPEVLRDLERLSRELGGRVDRLLRGLGGAVQELTALSVGCIQTYRDAVDSLGEAVDMSIKGMYTLLARCEELERALQPVQGLARQVRDIRRTLEVLEALCK
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
43PhosphorylationPPAGLRVSGEEETEN
CCCCCCCCCCCCCCC
28985074
60PhosphorylationGANRHPRTSPKTSSC
CCCCCCCCCCCCCCC
20068231
61PhosphorylationANRHPRTSPKTSSCG
CCCCCCCCCCCCCCC
20068231
62PhosphorylationNRHPRTSPKTSSCGV
CCCCCCCCCCCCCCC
18669648
64PhosphorylationHPRTSPKTSSCGVVH
CCCCCCCCCCCCCCC
23312004
65PhosphorylationPRTSPKTSSCGVVHR
CCCCCCCCCCCCCCC
18669648
66PhosphorylationRTSPKTSSCGVVHRP
CCCCCCCCCCCCCCH
23312004
87PhosphorylationNEPGPQGTLSGAGSR
CCCCCCCCCCCCCCC
30108239
89PhosphorylationPGPQGTLSGAGSRRG
CCCCCCCCCCCCCCC
30108239
93PhosphorylationGTLSGAGSRRGAPGA
CCCCCCCCCCCCCCC
23401153
105PhosphorylationPGAEHEPSLSSRHKN
CCCCCCCCCCCCCCC
28857561
107PhosphorylationAEHEPSLSSRHKNPA
CCCCCCCCCCCCCCC
28857561
108PhosphorylationEHEPSLSSRHKNPAP
CCCCCCCCCCCCCCC
23312004
122PhosphorylationPPEGKPSSGRDCRRG
CCCCCCCCCCCCCCC
28555341
128MethylationSSGRDCRRGGPGGGM
CCCCCCCCCCCCCCC
-
158PhosphorylationAGSRAGRSFSSRLQD
HHHHHHHHHHHHHHC
23312004
160PhosphorylationSRAGRSFSSRLQDSR
HHHHHHHHHHHHCCC
25159151
161PhosphorylationRAGRSFSSRLQDSRS
HHHHHHHHHHHCCCC
28102081
166PhosphorylationFSSRLQDSRSLDGLS
HHHHHHCCCCCCCCH
23401153
168PhosphorylationSRLQDSRSLDGLSEA
HHHHCCCCCCCCHHH
23401153
173PhosphorylationSRSLDGLSEACGGAG
CCCCCCCHHHCCCCC
30266825
181PhosphorylationEACGGAGSSGSAESG
HHCCCCCCCCCCCCC
23927012
182PhosphorylationACGGAGSSGSAESGA
HCCCCCCCCCCCCCC
23927012
184PhosphorylationGGAGSSGSAESGAGG
CCCCCCCCCCCCCCC
21815630
187PhosphorylationGSSGSAESGAGGGRR
CCCCCCCCCCCCCCC
23927012
196PhosphorylationAGGGRRATISSPLEL
CCCCCCEEECCCEEE
29255136
198PhosphorylationGGRRATISSPLELEG
CCCCEEECCCEEEEE
30266825
199PhosphorylationGRRATISSPLELEGT
CCCEEECCCEEEEEE
30266825
206PhosphorylationSPLELEGTVSRHGDL
CCEEEEEEEECCCCC
23927012
208PhosphorylationLELEGTVSRHGDLTH
EEEEEEEECCCCCHH
23403867
224UbiquitinationVANNLQLKIRLSGAP
EECCCEEEEEECCCC
32015554
300PhosphorylationSVGCIQTYRDAVDSL
HHHHHHHHHHHHHHH
22210691
313SulfoxidationSLGEAVDMSIKGMYT
HHHHHHHHHHHHHHH
21406390
320PhosphorylationMSIKGMYTLLARCEE
HHHHHHHHHHHHHHH
22210691

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 BORC6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BORC6_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 BORC6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBX44_HUMANFBXO44physical
25416956
SHPRH_HUMANSHPRHphysical
25416956
KTN1_HUMANKTN1physical
26186194
SPAS2_HUMANSPATS2physical
26186194
LUZP1_HUMANLUZP1physical
26186194
CP250_HUMANCEP250physical
26186194
UACA_HUMANUACAphysical
26186194
GOGB1_HUMANGOLGB1physical
26186194
BICD2_HUMANBICD2physical
26186194
NDE1_HUMANNDE1physical
26186194
NDEL1_HUMANNDEL1physical
26186194
LTOR1_HUMANLAMTOR1physical
26186194
SAS6_HUMANSASS6physical
26186194
DISC1_HUMANDISC1physical
26186194
LTOR2_HUMANLAMTOR2physical
26186194
VPP1_HUMANATP6V0A1physical
26186194
TACC3_HUMANTACC3physical
26186194
CP135_HUMANCEP135physical
26186194
KIF11_HUMANKIF11physical
26186194
CK5P2_HUMANCDK5RAP2physical
26186194
SPAG5_HUMANSPAG5physical
26186194
IFT74_HUMANIFT74physical
26186194
ODF2L_HUMANODF2Lphysical
26186194
BL1S2_HUMANBLOC1S2physical
26186194
SCLT1_HUMANSCLT1physical
26186194
CC122_HUMANCCDC122physical
26186194
BL1S1_HUMANBLOC1S1physical
26186194
LTOR3_HUMANLAMTOR3physical
26186194
BORC5_HUMANLOH12CR1physical
26186194
CEP55_HUMANCEP55physical
26186194
HSBP1_HUMANHSBP1physical
26186194
BORC8_HUMANMEF2BNBphysical
26186194
SKAP_HUMANKNSTRNphysical
26186194
LTOR5_HUMANLAMTOR5physical
26186194
CCD57_HUMANCCDC57physical
26186194
BL1S5_HUMANBLOC1S5physical
26186194
NIN_HUMANNINphysical
26186194
BRE1B_HUMANRNF40physical
26186194
TRI37_HUMANTRIM37physical
26186194
SELT_HUMANSELTphysical
26186194
BORC7_HUMANC10orf32physical
26186194
KXDL1_HUMANKXD1physical
26186194
PIBF1_HUMANPIBF1physical
26186194
SNAPN_HUMANSNAPINphysical
26186194
TARA_HUMANTRIOBPphysical
26186194
FYCO1_HUMANFYCO1physical
26186194
CCD22_HUMANCCDC22physical
26186194
LTOR4_HUMANLAMTOR4physical
26186194
ODF2L_HUMANODF2Lphysical
28514442
BORC5_HUMANLOH12CR1physical
28514442
BORC8_HUMANMEF2BNBphysical
28514442
KXDL1_HUMANKXD1physical
28514442
CCD57_HUMANCCDC57physical
28514442
BL1S1_HUMANBLOC1S1physical
28514442
CP250_HUMANCEP250physical
28514442
LUZP1_HUMANLUZP1physical
28514442
UACA_HUMANUACAphysical
28514442
SCLT1_HUMANSCLT1physical
28514442
CP135_HUMANCEP135physical
28514442
BL1S2_HUMANBLOC1S2physical
28514442
CC122_HUMANCCDC122physical
28514442
BL1S5_HUMANBLOC1S5physical
28514442
TRI37_HUMANTRIM37physical
28514442
NIN_HUMANNINphysical
28514442
BORC7_HUMANC10orf32physical
28514442
SNAPN_HUMANSNAPINphysical
28514442
LTOR2_HUMANLAMTOR2physical
28514442
SPAS2_HUMANSPATS2physical
28514442
BICD2_HUMANBICD2physical
28514442
LTOR4_HUMANLAMTOR4physical
28514442
SAS6_HUMANSASS6physical
28514442
SKAP_HUMANKNSTRNphysical
28514442
LTOR1_HUMANLAMTOR1physical
28514442
NDE1_HUMANNDE1physical
28514442
TACC3_HUMANTACC3physical
28514442
HSBP1_HUMANHSBP1physical
28514442
SPAG5_HUMANSPAG5physical
28514442
TARA_HUMANTRIOBPphysical
28514442
LTOR3_HUMANLAMTOR3physical
28514442
PIBF1_HUMANPIBF1physical
28514442
IFT74_HUMANIFT74physical
28514442
DISC1_HUMANDISC1physical
28514442
NDEL1_HUMANNDEL1physical
28514442
KTN1_HUMANKTN1physical
28514442
CEP55_HUMANCEP55physical
28514442
FYCO1_HUMANFYCO1physical
28514442
KIF11_HUMANKIF11physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of BORC6_HUMAN

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Related Literatures of Post-Translational Modification

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