ABCB6_HUMAN - dbPTM
ABCB6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCB6_HUMAN
UniProt AC Q9NP58
Protein Name ATP-binding cassette sub-family B member 6, mitochondrial
Gene Name ABCB6
Organism Homo sapiens (Human).
Sequence Length 842
Subcellular Localization Cell membrane
Multi-pass membrane protein . Mitochondrion outer membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein . Endosome membrane
Multi-pa
Protein Description Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis..
Protein Sequence MVTVGNYCEAEGPVGPAWMQDGLSPCFFFTLVPSTRMALGTLALVLALPCRRRERPAGADSLSWGAGPRISPYVLQLLLATLQAALPLAGLAGRVGTARGAPLPSYLLLASVLESLAGACGLWLLVVERSQARQRLAMGIWIKFRHSPGLLLLWTVAFAAENLALVSWNSPQWWWARADLGQQVQFSLWVLRYVVSGGLFVLGLWAPGLRPQSYTLQVHEEDQDVERSQVRSAAQQSTWRDFGRKLRLLSGYLWPRGSPALQLVVLICLGLMGLERALNVLVPIFYRNIVNLLTEKAPWNSLAWTVTSYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRRVELLIFSHLHELSLRWHLGRRTGEVLRIADRGTSSVTGLLSYLVFNVIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLTLTIVVTEWRTKFRRAMNTQENATRARAVDSLLNFETVKYYNAESYEVERYREAIIKYQGLEWKSSASLVLLNQTQNLVIGLGLLAGSLLCAYFVTEQKLQVGDYVLFGTYIIQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDLPGAGPLRFQKGRIEFENVHFSYADGRETLQDVSFTVMPGQTLALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQASLRSHIGVVPQDTVLFNDTIADNIRYGRVTAGNDEVEAAAQAAGIHDAIMAFPEGYRTQVGERGLKLSGGEKQRVAIARTILKAPGIILLDEATSALDTSNERAIQASLAKVCANRTTIVVAHRLSTVVNADQILVIKDGCIVERGRHEALLSRGGVYADMWQLQQGQEETSEDTKPQTMER
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
50S-palmitoylationALVLALPCRRRERPA
HHHHHCCCCCCCCCC
5.7129575903
61PhosphorylationERPAGADSLSWGAGP
CCCCCCCCCCCCCCC
24.6228857561
63PhosphorylationPAGADSLSWGAGPRI
CCCCCCCCCCCCCCC
27.6730108239
167PhosphorylationAENLALVSWNSPQWW
HHHCCCCCCCCCCCE
22.7627732954
170PhosphorylationLALVSWNSPQWWWAR
CCCCCCCCCCCEEEE
16.5327732954
357PhosphorylationFSHLHELSLRWHLGR
HHCHHHHHHHHHHCC
16.9524719451
366PhosphorylationRWHLGRRTGEVLRIA
HHHHCCCCCCEEEEE
36.0124702127
418 (in isoform 4)Ubiquitination-3.2621890473
418UbiquitinationAWFGLIVFLCMSLYL
HHHHHHHHHHHHHHH
3.2629901268
436 (in isoform 4)Ubiquitination-35.2921890473
436UbiquitinationIVVTEWRTKFRRAMN
HHHHHHHHHHHHHHH
35.2933845483
444PhosphorylationKFRRAMNTQENATRA
HHHHHHHHHHHHHHH
24.9515979861
449PhosphorylationMNTQENATRARAVDS
HHHHHHHHHHHHHHH
36.1215979853
456PhosphorylationTRARAVDSLLNFETV
HHHHHHHHHHCCEEE
28.3225850435
464 (in isoform 1)Ubiquitination-49.8121890473
464UbiquitinationLLNFETVKYYNAESY
HHCCEEEEEECCCCC
49.8121906983
482 (in isoform 1)Ubiquitination-25.9621890473
482SumoylationRYREAIIKYQGLEWK
HHHHHHHHHCCCCCC
25.96-
482UbiquitinationRYREAIIKYQGLEWK
HHHHHHHHHCCCCCC
25.9621963094
483PhosphorylationYREAIIKYQGLEWKS
HHHHHHHHCCCCCCC
9.4528348404
490PhosphorylationYQGLEWKSSASLVLL
HCCCCCCCCEEEEEE
32.0128348404
491PhosphorylationQGLEWKSSASLVLLN
CCCCCCCCEEEEEEC
20.3928348404
493PhosphorylationLEWKSSASLVLLNQT
CCCCCCEEEEEECCC
22.4328348404
500PhosphorylationSLVLLNQTQNLVIGL
EEEEECCCCCHHHHH
20.5327251275
513PhosphorylationGLGLLAGSLLCAYFV
HHHHHHHHHHHHHHH
16.7428348404
518PhosphorylationAGSLLCAYFVTEQKL
HHHHHHHHHHCCCCC
9.5128348404
521PhosphorylationLLCAYFVTEQKLQVG
HHHHHHHCCCCCCCC
23.8528348404
529UbiquitinationEQKLQVGDYVLFGTY
CCCCCCCCEEEEEEE
31.3533845483
569UbiquitinationENMFDLLKEETEVKD
HHHHHHHHHCCCCCC
61.88-
575UbiquitinationLKEETEVKDLPGAGP
HHHCCCCCCCCCCCC
47.5233845483
605PhosphorylationSYADGRETLQDVSFT
EECCCCCEECEEEEE
28.4920068231
610PhosphorylationRETLQDVSFTVMPGQ
CCEECEEEEEECCCC
24.4020068231
612PhosphorylationTLQDVSFTVMPGQTL
EECEEEEEECCCCEE
14.3720068231
618PhosphorylationFTVMPGQTLALVGPS
EEECCCCEEEEECCC
21.6620068231
625PhosphorylationTLALVGPSGAGKSTI
EEEEECCCCCCHHHH
35.0320068231
680UbiquitinationTVLFNDTIADNIRYG
EEEECCCCCCCCEEC
5.1733845483
697 (in isoform 4)Ubiquitination-30.4621890473
725UbiquitinationTQVGERGLKLSGGEK
CCCCCCCEECCCCHH
6.7229901268
726UbiquitinationQVGERGLKLSGGEKQ
CCCCCCEECCCCHHH
43.3527667366
743UbiquitinationAIARTILKAPGIILL
HHHHHHHHCCCEEEE
49.002190698
743 (in isoform 1)Ubiquitination-49.0021890473
754PhosphorylationIILLDEATSALDTSN
EEEEECCCCCCCCCC
16.6930108239
755PhosphorylationILLDEATSALDTSNE
EEEECCCCCCCCCCH
33.6023025827
759PhosphorylationEATSALDTSNERAIQ
CCCCCCCCCCHHHHH
34.0130108239
760PhosphorylationATSALDTSNERAIQA
CCCCCCCCCHHHHHH
36.0430108239
771UbiquitinationAIQASLAKVCANRTT
HHHHHHHHHHCCCCE
43.0429901268
786PhosphorylationIVVAHRLSTVVNADQ
EEEEECHHHCCCCCE
21.0722468782
790 (in isoform 4)Ubiquitination-33.20-
790UbiquitinationHRLSTVVNADQILVI
ECHHHCCCCCEEEEE
33.2033845483
836UbiquitinationEETSEDTKPQTMER-
CCCCCCCCCCCCCC-
47.6621963094

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 ABCB6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCB6_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 ABCB6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOM40_HUMANTOMM40physical
22939629

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614497Microphthalmia, isolated, with coloboma, 7 (MCOPCB7)
615402Dyschromatosis universalis hereditaria 3 (DUH3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCB6_HUMAN

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Related Literatures of Post-Translational Modification

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