MPCP_HUMAN - dbPTM
MPCP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPCP_HUMAN
UniProt AC Q00325
Protein Name Phosphate carrier protein, mitochondrial
Gene Name SLC25A3
Organism Homo sapiens (Human).
Sequence Length 362
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein.
Protein Description Transport of phosphate groups from the cytosol to the mitochondrial matrix. Phosphate is cotransported with H(+). May play a role regulation of the mitochondrial permeability transition pore (mPTP)..
Protein Sequence MFSSVAHLARANPFNTPHLQLVHDGLGDLRSSSPGPTGQPRRPRNLAAAAVEEQYSCDYGSGRFFILCGLGGIISCGTTHTALVPLDLVKCRMQVDPQKYKGIFNGFSVTLKEDGVRGLAKGWAPTFLGYSMQGLCKFGFYEVFKVLYSNMLGEENTYLWRTSLYLAASASAEFFADIALAPMEAAKVRIQTQPGYANTLRDAAPKMYKEEGLKAFYKGVAPLWMRQIPYTMMKFACFERTVEALYKFVVPKPRSECSKPEQLVVTFVAGYIAGVFCAIVSHPADSVVSVLNKEKGSSASLVLKRLGFKGVWKGLFARIIMIGTLTALQWFIYDSVKVYFRLPRPPPPEMPESLKKKLGLTQ
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-----MFSSVAHLAR
-----CCCHHHHHHH		23.7021406692
4Phosphorylation----MFSSVAHLARA
----CCCHHHHHHHH		16.4421406692
31PhosphorylationDGLGDLRSSSPGPTG
CCCCCCCCCCCCCCC		42.3323312004
32PhosphorylationGLGDLRSSSPGPTGQ
CCCCCCCCCCCCCCC		33.8323312004
33PhosphorylationLGDLRSSSPGPTGQP
CCCCCCCCCCCCCCC		34.8128985074
54 (in isoform 2)Phosphorylation-23.1825884760
55PhosphorylationAAAVEEQYSCDYGSG
HHHHHHHHCCCCCCC		17.97-
56PhosphorylationAAVEEQYSCDYGSGR
HHHHHHHCCCCCCCC		10.54-
98 (in isoform 2)Ubiquitination-58.1921890473
992-HydroxyisobutyrylationRMQVDPQKYKGIFNG
CCCCCHHHCCCCCCC		55.08-
99AcetylationRMQVDPQKYKGIFNG
CCCCCHHHCCCCCCC		55.0819608861
99UbiquitinationRMQVDPQKYKGIFNG
CCCCCHHHCCCCCCC		55.0821890473
99 (in isoform 1)Ubiquitination-55.0821890473
100PhosphorylationMQVDPQKYKGIFNGF
CCCCHHHCCCCCCCE		14.8122210691
100 (in isoform 2)Ubiquitination-14.8121890473
101AcetylationQVDPQKYKGIFNGFS
CCCHHHCCCCCCCEE		53.1926051181
101UbiquitinationQVDPQKYKGIFNGFS
CCCHHHCCCCCCCEE		53.1921890473
101 (in isoform 1)Ubiquitination-53.1921890473
108PhosphorylationKGIFNGFSVTLKEDG
CCCCCCEEEEEECCC		18.6520068231
110PhosphorylationIFNGFSVTLKEDGVR
CCCCEEEEEECCCCC		30.8020068231
111 (in isoform 2)Ubiquitination-5.5421890473
1122-HydroxyisobutyrylationNGFSVTLKEDGVRGL
CCEEEEEECCCCCHH		44.38-
112AcetylationNGFSVTLKEDGVRGL
CCEEEEEECCCCCHH		44.3825038526
112MethylationNGFSVTLKEDGVRGL
CCEEEEEECCCCCHH		44.3824129315
112UbiquitinationNGFSVTLKEDGVRGL
CCEEEEEECCCCCHH		44.3821890473
112 (in isoform 1)Ubiquitination-44.3821890473
117MethylationTLKEDGVRGLAKGWA
EEECCCCCHHHCCCC		39.68115917077
120 (in isoform 2)Ubiquitination-15.9021890473
121UbiquitinationDGVRGLAKGWAPTFL
CCCCHHHCCCCCHHH		61.0921890473
121 (in isoform 1)Ubiquitination-61.0921890473
141PhosphorylationGLCKFGFYEVFKVLY
HHHHHCHHHHHHHHH		16.1525147952
151SulfoxidationFKVLYSNMLGEENTY
HHHHHHHCCCCCCCC		4.1228183972
157PhosphorylationNMLGEENTYLWRTSL
HCCCCCCCCHHHHHH		24.22-
158PhosphorylationMLGEENTYLWRTSLY
CCCCCCCCHHHHHHH		18.82-
192PhosphorylationAAKVRIQTQPGYANT
HHHCCEECCCCHHHH		34.0727080861
196NitrationRIQTQPGYANTLRDA
CEECCCCHHHHHHHH		11.89-
196PhosphorylationRIQTQPGYANTLRDA
CEECCCCHHHHHHHH		11.8928152594
199PhosphorylationTQPGYANTLRDAAPK
CCCCHHHHHHHHHHH		18.2627080861
201MethylationPGYANTLRDAAPKMY
CCHHHHHHHHHHHHH		29.50115917081
205 (in isoform 2)Ubiquitination-24.5421890473
2062-HydroxyisobutyrylationTLRDAAPKMYKEEGL
HHHHHHHHHHHHHHH		50.57-
206AcetylationTLRDAAPKMYKEEGL
HHHHHHHHHHHHHHH		50.5725953088
206MalonylationTLRDAAPKMYKEEGL
HHHHHHHHHHHHHHH		50.5726320211
206UbiquitinationTLRDAAPKMYKEEGL
HHHHHHHHHHHHHHH		50.5721890473
206 (in isoform 1)Ubiquitination-50.5721890473
207SulfoxidationLRDAAPKMYKEEGLK
HHHHHHHHHHHHHHH		5.8628183972
208PhosphorylationRDAAPKMYKEEGLKA
HHHHHHHHHHHHHHH		22.7529496907
208 (in isoform 2)Ubiquitination-22.7521890473
2092-HydroxyisobutyrylationDAAPKMYKEEGLKAF
HHHHHHHHHHHHHHH		45.87-
209AcetylationDAAPKMYKEEGLKAF
HHHHHHHHHHHHHHH		45.8723236377
209MalonylationDAAPKMYKEEGLKAF
HHHHHHHHHHHHHHH		45.8726320211
209SuccinylationDAAPKMYKEEGLKAF
HHHHHHHHHHHHHHH		45.8727452117
209UbiquitinationDAAPKMYKEEGLKAF
HHHHHHHHHHHHHHH		45.8721890473
209 (in isoform 1)Ubiquitination-45.8721890473
213 (in isoform 2)Ubiquitination-4.0121890473
2142-HydroxyisobutyrylationMYKEEGLKAFYKGVA
HHHHHHHHHHHHCCH		47.51-
214AcetylationMYKEEGLKAFYKGVA
HHHHHHHHHHHHCCH		47.5125825284
214MalonylationMYKEEGLKAFYKGVA
HHHHHHHHHHHHCCH		47.5132601280
214UbiquitinationMYKEEGLKAFYKGVA
HHHHHHHHHHHHCCH		47.5121890473
214 (in isoform 1)Ubiquitination-47.5121890473
217PhosphorylationEEGLKAFYKGVAPLW
HHHHHHHHHCCHHHH		16.2225367160
217 (in isoform 2)Ubiquitination-16.2221890473
218AcetylationEGLKAFYKGVAPLWM
HHHHHHHHCCHHHHH		40.2225825284
218UbiquitinationEGLKAFYKGVAPLWM
HHHHHHHHCCHHHHH		40.2221890473
218 (in isoform 1)Ubiquitination-40.2221890473
225SulfoxidationKGVAPLWMRQIPYTM
HCCHHHHHHHCCHHH		2.7328465586
226MethylationGVAPLWMRQIPYTMM
CCHHHHHHHCCHHHH		21.50115917085
230PhosphorylationLWMRQIPYTMMKFAC
HHHHHCCHHHHHHHH		14.6421406692
231PhosphorylationWMRQIPYTMMKFACF
HHHHCCHHHHHHHHH		12.8721406692
233 (in isoform 2)Ubiquitination-2.2021890473
234AcetylationQIPYTMMKFACFERT
HCCHHHHHHHHHHHH		20.9825953088
234SuccinylationQIPYTMMKFACFERT
HCCHHHHHHHHHHHH		20.9823954790
234UbiquitinationQIPYTMMKFACFERT
HCCHHHHHHHHHHHH		20.9821890473
234 (in isoform 1)Ubiquitination-20.9821890473
237S-palmitoylationYTMMKFACFERTVEA
HHHHHHHHHHHHHHH		4.0229575903
246PhosphorylationERTVEALYKFVVPKP
HHHHHHHHHHHCCCC		14.9328064214
246 (in isoform 2)Ubiquitination-14.9321890473
2472-HydroxyisobutyrylationRTVEALYKFVVPKPR
HHHHHHHHHHCCCCH		32.31-
247AcetylationRTVEALYKFVVPKPR
HHHHHHHHHHCCCCH		32.3125825284
247SuccinylationRTVEALYKFVVPKPR
HHHHHHHHHHCCCCH		32.3123954790
247UbiquitinationRTVEALYKFVVPKPR
HHHHHHHHHHCCCCH		32.3121890473
247 (in isoform 1)Ubiquitination-32.3121890473
251 (in isoform 2)Ubiquitination-35.3121890473
252UbiquitinationLYKFVVPKPRSECSK
HHHHHCCCCHHHCCC		41.2621890473
252 (in isoform 1)Ubiquitination-41.2621890473
294 (in isoform 2)Ubiquitination-62.6721890473
2952-HydroxyisobutyrylationVSVLNKEKGSSASLV
HHHHCCCCCCCHHHH		66.75-
295AcetylationVSVLNKEKGSSASLV
HHHHCCCCCCCHHHH		66.7525953088
295MalonylationVSVLNKEKGSSASLV
HHHHCCCCCCCHHHH		66.7526320211
295UbiquitinationVSVLNKEKGSSASLV
HHHHCCCCCCCHHHH		66.7521906983
295 (in isoform 1)Ubiquitination-66.7521890473
297PhosphorylationVLNKEKGSSASLVLK
HHCCCCCCCHHHHHH		33.5225159151
298PhosphorylationLNKEKGSSASLVLKR
HCCCCCCCHHHHHHH		30.4625159151
300PhosphorylationKEKGSSASLVLKRLG
CCCCCCHHHHHHHHC		22.4326471730
303 (in isoform 2)Ubiquitination-3.0321890473
3042-HydroxyisobutyrylationSSASLVLKRLGFKGV
CCHHHHHHHHCCCHH		37.79-
304AcetylationSSASLVLKRLGFKGV
CCHHHHHHHHCCCHH		37.7925953088
304MalonylationSSASLVLKRLGFKGV
CCHHHHHHHHCCCHH		37.7926320211
304UbiquitinationSSASLVLKRLGFKGV
CCHHHHHHHHCCCHH		37.7921890473
304 (in isoform 1)Ubiquitination-37.7921890473
308 (in isoform 2)Ubiquitination-8.0321890473
309AcetylationVLKRLGFKGVWKGLF
HHHHHCCCHHHHHHH		51.2430584061
309UbiquitinationVLKRLGFKGVWKGLF
HHHHHCCCHHHHHHH		51.2421890473
309 (in isoform 1)Ubiquitination-51.2421890473
3132-HydroxyisobutyrylationLGFKGVWKGLFARII
HCCCHHHHHHHHHHH		43.24-
321SulfoxidationGLFARIIMIGTLTAL
HHHHHHHHHHHHHHH		1.8428183972
353PhosphorylationPPPEMPESLKKKLGL
CCCCCCHHHHHHHCC		39.3526437602
354 (in isoform 2)Ubiquitination-10.0721890473
3552-HydroxyisobutyrylationPEMPESLKKKLGLTQ
CCCCHHHHHHHCCCC		58.08-
355AcetylationPEMPESLKKKLGLTQ
CCCCHHHHHHHCCCC		58.0826051181
355UbiquitinationPEMPESLKKKLGLTQ
CCCCHHHHHHHCCCC		58.082190698
355 (in isoform 1)Ubiquitination-58.0821890473
356AcetylationEMPESLKKKLGLTQ-
CCCHHHHHHHCCCC-		59.5330584073
356 (in isoform 2)Ubiquitination-59.5321890473
357UbiquitinationMPESLKKKLGLTQ--
CCHHHHHHHCCCC--		46.32-
357 (in isoform 1)Ubiquitination-46.3221890473
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 MPCP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPCP_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 MPCP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL10_HUMANRPL10physical
22939629
OST48_HUMANDDOSTphysical
22939629
VPP2_HUMANATP6V0A2physical
22939629
T126A_HUMANTMEM126Aphysical
22939629
TOM20_HUMANTOMM20physical
22939629
TM177_HUMANTMEM177physical
22939629
MTX2_HUMANMTX2physical
22939629
SUGP2_HUMANSUGP2physical
22939629
ODPX_HUMANPDHXphysical
22939629
NDUV3_HUMANNDUFV3physical
22939629
RM50_HUMANMRPL50physical
22939629
VPP1_HUMANATP6V0A1physical
22939629
RL27_HUMANRPL27physical
22939629
PTN1_HUMANPTPN1physical
22939629
RM02_HUMANMRPL2physical
22939629
NDUB5_HUMANNDUFB5physical
22939629
RM20_HUMANMRPL20physical
22939629
RM13_HUMANMRPL13physical
22939629
NDUV2_HUMANNDUFV2physical
22939629
QSOX2_HUMANQSOX2physical
22939629
TMED4_HUMANTMED4physical
22939629
VATB1_HUMANATP6V1B1physical
22939629
RT30_HUMANMRPS30physical
22939629
NDUB8_HUMANNDUFB8physical
22939629
RM10_HUMANMRPL10physical
22939629
SCFD1_HUMANSCFD1physical
22939629
MIC13_HUMANC19orf70physical
22939629
TM9S2_HUMANTM9SF2physical
22939629
RT26_HUMANMRPS26physical
22939629
SFXN2_HUMANSFXN2physical
22939629
RM09_HUMANMRPL9physical
22939629
SQOR_HUMANSQRDLphysical
22939629
RM17_HUMANMRPL17physical
22939629
RM30_HUMANMRPL30physical
22939629
RAI3_HUMANGPRC5Aphysical
22939629
SPG7_HUMANSPG7physical
22939629
ACADM_HUMANACADMphysical
26344197
AFG32_HUMANAFG3L2physical
26344197
AL3A2_HUMANALDH3A2physical
26344197
ATD3A_HUMANATAD3Aphysical
26344197
AT5F1_HUMANATP5F1physical
26344197
CALX_HUMANCANXphysical
26344197
TCPG_HUMANCCT3physical
26344197
TCPD_HUMANCCT4physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
CLH1_HUMANCLTCphysical
26344197
DHB12_HUMANHSD17B12physical
26344197
ENPL_HUMANHSP90B1physical
26344197
IDH3A_HUMANIDH3Aphysical
26344197
ILVBL_HUMANILVBLphysical
26344197
IPO7_HUMANIPO7physical
26344197
MTCH1_HUMANMTCH1physical
26344197
MTCH2_HUMANMTCH2physical
26344197
COX2_HUMANCOX2physical
26344197
NDUAC_HUMANNDUFA12physical
26344197
NDUBA_HUMANNDUFB10physical
26344197
NDUB8_HUMANNDUFB8physical
26344197
NDUS1_HUMANNDUFS1physical
26344197
NDUS8_HUMANNDUFS8physical
26344197
PYC_HUMANPCphysical
26344197
2AAA_HUMANPPP2R1Aphysical
26344197
2AAB_HUMANPPP2R1Bphysical
26344197
RAB1A_HUMANRAB1Aphysical
26344197
RAB7A_HUMANRAB7Aphysical
26344197
RPN1_HUMANRPN1physical
26344197
ACOD_HUMANSCDphysical
26344197
SDHB_HUMANSDHBphysical
26344197
SSRD_HUMANSSR4physical
26344197
STML2_HUMANSTOML2physical
26344197
TMCO1_HUMANTMCO1physical
26344197
TOM22_HUMANTOMM22physical
26344197
EFTU_HUMANTUFMphysical
26344197
QCR8_HUMANUQCRQphysical
26344197
TERA_HUMANVCPphysical
26344197
VDAC3_HUMANVDAC3physical
26344197
Drug and Disease Associations
Kegg Disease
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
OMIM Disease
610773Mitochondrial phosphate carrier deficiency (MPCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPCP_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-99; LYS-209 AND LYS-214, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-196, AND MASSSPECTROMETRY.

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