ABCB7_HUMAN - dbPTM
ABCB7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABCB7_HUMAN
UniProt AC O75027
Protein Name ATP-binding cassette sub-family B member 7, mitochondrial
Gene Name ABCB7
Organism Homo sapiens (Human).
Sequence Length 752
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins..
Protein Sequence MALLAMHSWRWAAAAAAFEKRRHSAILIRPLVSVSGSGPQWRPHQLGALGTARAYQIPESLKSITWQRLGKGNSGQFLDAAKALQVWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKEEERKKLQEEIVNSVKGCGNCSC
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
10MethylationLLAMHSWRWAAAAAA
HHHHHHHHHHHHHHH		19.03-
10DimethylationLLAMHSWRWAAAAAA
HHHHHHHHHHHHHHH		19.03-
126PhosphorylationKIIKAMLSYVWPKDR
HHHHHHHHHHCCCCC		12.4524505115
176UbiquitinationNQMSGNMLNLSDAPN
HHCCCCCCCCCCCCH		7.2719608861
176AcetylationNQMSGNMLNLSDAPN
HHCCCCCCCCCCCCH		7.2719608861
196PhosphorylationATAVLIGYGVSRAGA
HHHHHHHCCCCHHHH		13.8321253578
199PhosphorylationVLIGYGVSRAGAAFF
HHHHCCCCHHHHHHH		16.4321253578
211AcetylationAFFNEVRNAVFGKVA
HHHHHHHHHHHHHHH		45.7019608861
216MalonylationVRNAVFGKVAQNSIR
HHHHHHHHHHHHHHH		23.9626320211
216UbiquitinationVRNAVFGKVAQNSIR
HHHHHHHHHHHHHHH		23.9619608861
216AcetylationVRNAVFGKVAQNSIR
HHHHHHHHHHHHHHH		23.9619608861
243PhosphorylationLDLGFHLSRQTGALS
CCCCHHHHHHCCHHH		17.4846156667
251SuccinylationRQTGALSKAIDRGTR
HHCCHHHHHHHHCCH		50.6527452117
251AcetylationRQTGALSKAIDRGTR
HHCCHHHHHHHHCCH		50.6519608861
251UbiquitinationRQTGALSKAIDRGTR
HHCCHHHHHHHHCCH		50.65-
257PhosphorylationSKAIDRGTRGISFVL
HHHHHHCCHHHHHHH		26.9820068231
258PhosphorylationKAIDRGTRGISFVLS
HHHHHCCHHHHHHHH		43.1824719451
261PhosphorylationDRGTRGISFVLSALV
HHCCHHHHHHHHHHH		16.4820068231
265PhosphorylationRGISFVLSALVFNLL
HHHHHHHHHHHHHHH		17.7936012569
282PhosphorylationMFEVMLVSGVLYYKC
HHHHHHHHCHHHHHC		21.1520068231
286PhosphorylationMLVSGVLYYKCGAQF
HHHHCHHHHHCCCEE		9.8522210691
287PhosphorylationLVSGVLYYKCGAQFA
HHHCHHHHHCCCEEE		8.8120068231
336PhosphorylationAGNAAIDSLLNYETV
HHHHHHHHHHCHHHH		28.74-
340PhosphorylationAIDSLLNYETVKYFN
HHHHHHCHHHHHHHC		16.9731136865
342PhosphorylationDSLLNYETVKYFNNE
HHHHCHHHHHHHCCH		16.37-
344UbiquitinationLLNYETVKYFNNERY
HHCHHHHHHHCCHHH		52.09-
345PhosphorylationLNYETVKYFNNERYE
HCHHHHHHHCCHHHH		13.7518083107
356PhosphorylationERYEAQRYDGFLKTY
HHHHHHEECCCHHHH		14.3418083107
361SuccinylationQRYDGFLKTYETASL
HEECCCHHHHHCCCC		46.9623954790
370PhosphorylationYETASLKSTSTLAML
HHCCCCCCCCEEHHH		32.6511003341
371PhosphorylationETASLKSTSTLAMLN
HCCCCCCCCEEHHHH		24.9211003353
446PhosphorylationIDMNTLFTLLKVDTQ
HCHHHHHHHHCCCHH		34.0021712546
461O-linked_GlycosylationIKDKVMASPLQITPQ
HCCHHHCCCCEECCC		14.1930379171
466O-linked_GlycosylationMASPLQITPQTATVA
HCCCCEECCCEEEEE		9.0730379171
489PhosphorylationIEGQKVLSGISFEVP
ECCEEEEECEEEEEC		36.7550558551
492PhosphorylationQKVLSGISFEVPAGK
EEEEECEEEEECCCC		20.9150558559
499SuccinylationSFEVPAGKKVAIVGG
EEEECCCCEEEEECC		46.2923954790
499AcetylationSFEVPAGKKVAIVGG
EEEECCCCEEEEECC		46.2930586663
500UbiquitinationFEVPAGKKVAIVGGS
EEECCCCEEEEECCC		35.66-
509O-linked_GlycosylationAIVGGSGSGKSTIVR
EEECCCCCCHHHHHH		44.7530379171
540PhosphorylationGQNIQDVSLESLRRA
CCCCCCCCHHHHHHH		34.4124719451
600PhosphorylationRMPHGYDTQVGERGL
CCCCCCCCCCCCCCE		19.37110737115
608AcetylationQVGERGLKLSGGEKQ
CCCCCCEECCCCHHH		43.3525953088
608UbiquitinationQVGERGLKLSGGEKQ
CCCCCCEECCCCHHH		43.35-
636PhosphorylationVILYDEATSSLDSIT
EEEEECCCCCCCCCC		19.4628857561
660PhosphorylationDVVKHRTSIFIAHRL
HHHHHHCHHHHHCCC		18.5650558543
743PhosphorylationLQEEIVNSVKGCGNC
HHHHHHHHHCCCCCC		17.8221815630
744PhosphorylationQEEIVNSVKGCGNCS
HHHHHHHHCCCCCCC		5.3627251275
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 ABCB7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABCB7_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 ABCB7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HEMH_HUMANFECHphysical
12480705
A4_HUMANAPPphysical
21832049
RM10_HUMANMRPL10physical
22939629
VATD_HUMANATP6V1Dphysical
22939629
PDCD6_HUMANPDCD6physical
22939629
NDUB6_HUMANNDUFB6physical
22939629
QCR1_HUMANUQCRC1physical
22939629
MTCH1_HUMANMTCH1physical
22939629
SYEP_HUMANEPRSphysical
26344197
RPN1_HUMANRPN1physical
26344197
Drug and Disease Associations
Kegg Disease
H00982 Sideroblastic anemia, including: Pyridoxine-refractory autosomal recessive sideroblastic anemia (PRA
OMIM Disease
301310Anemia, sideroblastic, spinocerebellar ataxia (ASAT)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABCB7_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216 AND LYS-251, AND MASSSPECTROMETRY.

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