ACPM_HUMAN - dbPTM
ACPM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACPM_HUMAN
UniProt AC O14561
Protein Name Acyl carrier protein, mitochondrial
Gene Name NDUFAB1
Organism Homo sapiens (Human).
Sequence Length 156
Subcellular Localization Mitochondrion .
Protein Description Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain. [PubMed: 27626371]
Protein Sequence MASRVLSAYVSRLPAAFAPLPRVRMLAVARPLSTALCSAGTQTRLGTLQPALVLAQVPGRVTQLCRQYSDMPPLTLEGIQDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE
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
3Phosphorylation-----MASRVLSAYV
-----CHHHHHHHHH		22.9425002506
7Phosphorylation-MASRVLSAYVSRLP
-CHHHHHHHHHHHCC		18.0725002506
9PhosphorylationASRVLSAYVSRLPAA
HHHHHHHHHHHCCHH		8.7925002506
11PhosphorylationRVLSAYVSRLPAAFA
HHHHHHHHHCCHHHC		18.5425002506
68PhosphorylationVTQLCRQYSDMPPLT
HHHHHHHHCCCCCEE		6.3122985185
69PhosphorylationTQLCRQYSDMPPLTL
HHHHHHHCCCCCEEE		21.0622985185
75PhosphorylationYSDMPPLTLEGIQDR
HCCCCCEEECHHHHH		28.6522985185
88AcetylationDRVLYVLKLYDKIDP
HHHHHHHHHHHCCCH		34.6525953088
88UbiquitinationDRVLYVLKLYDKIDP
HHHHHHHHHHHCCCH		34.6521890473
88UbiquitinationDRVLYVLKLYDKIDP
HHHHHHHHHHHCCCH		34.6521890473
92UbiquitinationYVLKLYDKIDPEKLS
HHHHHHHCCCHHHCC		35.1422817900
92SuccinylationYVLKLYDKIDPEKLS
HHHHHHHCCCHHHCC		35.1423954790
922-HydroxyisobutyrylationYVLKLYDKIDPEKLS
HHHHHHHCCCHHHCC		35.14-
92AcetylationYVLKLYDKIDPEKLS
HHHHHHHCCCHHHCC		35.1423749302
97UbiquitinationYDKIDPEKLSVNSHF
HHCCCHHHCCCCCHH		51.9922817900
972-HydroxyisobutyrylationYDKIDPEKLSVNSHF
HHCCCHHHCCCCCHH		51.99-
97UbiquitinationYDKIDPEKLSVNSHF
HHCCCHHHCCCCCHH		51.9921890473
97AcetylationYDKIDPEKLSVNSHF
HHCCCHHHCCCCCHH		51.9925953088
99PhosphorylationKIDPEKLSVNSHFMK
CCCHHHCCCCCHHHH		30.2525159151
102PhosphorylationPEKLSVNSHFMKDLG
HHHCCCCCHHHHHCC		18.8823186163
106MethylationSVNSHFMKDLGLDSL
CCCCHHHHHCCCCCH		49.19115973807
112O-(pantetheine 4'-phosphoryl)serineMKDLGLDSLDQVEII
HHHCCCCCHHHHHHH		38.60-
112PhosphorylationMKDLGLDSLDQVEII
HHHCCCCCHHHHHHH		38.60-
119UbiquitinationSLDQVEIIMAMEDEF
CHHHHHHHHHHHCCC		0.6321890473
123UbiquitinationVEIIMAMEDEFGFEI
HHHHHHHHCCCCCCC		44.8722817900
128UbiquitinationAMEDEFGFEIPDIDA
HHHCCCCCCCCCCCH		10.5121890473
147PhosphorylationCPQEIVDYIADKKDV
CCHHHHHHHHHCCCC		6.26-
1512-HydroxyisobutyrylationIVDYIADKKDVYE--
HHHHHHHCCCCCC--		41.68-
151AcetylationIVDYIADKKDVYE--
HHHHHHHCCCCCC--		41.6825038526
152AcetylationVDYIADKKDVYE---
HHHHHHCCCCCC---		53.6325038526
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 ACPM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACPM_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 ACPM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
5NT3A_HUMANNT5C3Aphysical
21988832
SMYD3_HUMANSMYD3physical
21988832
RBM18_HUMANRBM18physical
21988832
OXSM_HUMANOXSMphysical
26186194
LYRM4_HUMANLYRM4physical
26186194
GCSP_HUMANGLDCphysical
26186194
ETFR1_HUMANLYRM5physical
26186194
NFS1_HUMANNFS1physical
26186194
LYRM7_HUMANLYRM7physical
26186194
LYRM2_HUMANLYRM2physical
26186194
ATPF2_HUMANATPAF2physical
26186194
OXSM_HUMANOXSMphysical
28514442
LYRM4_HUMANLYRM4physical
28514442
LYRM7_HUMANLYRM7physical
28514442
NFS1_HUMANNFS1physical
28514442
GCSP_HUMANGLDCphysical
28514442
ETFB_HUMANETFBphysical
28514442
SDHB_HUMANSDHBphysical
28514442
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 ACPM_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-92, AND MASS SPECTROMETRY.

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