CPIN1_HUMAN - dbPTM
CPIN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPIN1_HUMAN
UniProt AC Q6FI81
Protein Name Anamorsin {ECO:0000255|HAMAP-Rule:MF_03115}
Gene Name CIAPIN1 {ECO:0000255|HAMAP-Rule:MF_03115}
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion intermembrane space .
Protein Description Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. [PubMed: 23596212 NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity]
Protein Sequence MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMDLIDSDELLDPEDLKKPDPASLRAASCGEGKKRKACKNCTCGLAEELEKEKSREQMSSQPKSACGNCYLGDAFRCASCPYLGMPAFKPGEKVLLSDSNLHDA
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
26UbiquitinationSSPVEALKGLVDKLQ
CCHHHHHHHHHHHHH		58.19-
26AcetylationSSPVEALKGLVDKLQ
CCHHHHHHHHHHHHH		58.1925953088
31UbiquitinationALKGLVDKLQALTGN
HHHHHHHHHHHHHCC		34.7121890473
312-HydroxyisobutyrylationALKGLVDKLQALTGN
HHHHHHHHHHHHHCC		34.71-
31 (in isoform 1)Ubiquitination-34.7121890473
31 (in isoform 3)Ubiquitination-34.7121890473
48AcetylationRVSVENIKQLLQSAH
CCCHHHHHHHHHHCH		46.6125953088
48 (in isoform 1)Ubiquitination-46.6121890473
48UbiquitinationRVSVENIKQLLQSAH
CCCHHHHHHHHHHCH		46.6121890473
96UbiquitinationPGGCLFLKEPVETAV
CCCEEEECCCCEECC		53.27-
96AcetylationPGGCLFLKEPVETAV
CCCEEEECCCCEECC		53.2726051181
107PhosphorylationETAVDNNSKVKTASK
EECCCCCCHHCHHHH		45.1121601212
117PhosphorylationKTASKLCSALTLSGL
CHHHHHHHHHHHHCC		36.4327251275
136PhosphorylationELQREPLTPEEVQSV
HHHCCCCCHHHHHHH		39.0927273156
142PhosphorylationLTPEEVQSVREHLGH
CCHHHHHHHHHHHCC		28.4624117733
151PhosphorylationREHLGHESDNLLFVQ
HHHHCCCCCCEEEEE		26.5624144214
160PhosphorylationNLLFVQITGKKPNFE
CEEEEEEECCCCCEE		26.3424144214
1622-HydroxyisobutyrylationLFVQITGKKPNFEVG
EEEEEECCCCCEECC		57.30-
163UbiquitinationFVQITGKKPNFEVGS
EEEEECCCCCEECCC		46.68-
163MethylationFVQITGKKPNFEVGS
EEEEECCCCCEECCC		46.6823644510
170PhosphorylationKPNFEVGSSRQLKLS
CCCEECCCCEEEEEE		27.7618491316
171PhosphorylationPNFEVGSSRQLKLSI
CCEECCCCEEEEEEE		20.3724144214
175AcetylationVGSSRQLKLSITKKS
CCCCEEEEEEEECCC		31.6725953088
177PhosphorylationSSRQLKLSITKKSSP
CCEEEEEEEECCCCC		26.9923401153
179PhosphorylationRQLKLSITKKSSPSV
EEEEEEEECCCCCCC		29.1029083192
181UbiquitinationLKLSITKKSSPSVKP
EEEEEECCCCCCCCC		47.73-
182PhosphorylationKLSITKKSSPSVKPA
EEEEECCCCCCCCCC		49.3829255136
183PhosphorylationLSITKKSSPSVKPAV
EEEECCCCCCCCCCC		30.0329255136
185PhosphorylationITKKSSPSVKPAVDP
EECCCCCCCCCCCCH		44.7329255136
187AcetylationKKSSPSVKPAVDPAA
CCCCCCCCCCCCHHH		31.4325953088
187UbiquitinationKKSSPSVKPAVDPAA
CCCCCCCCCCCCHHH		31.43-
199PhosphorylationPAAAKLWTLSANDME
HHHHHHHEEECCCCC		22.6728857561
201PhosphorylationAAKLWTLSANDMEDD
HHHHHEEECCCCCCC		20.0423607784
209PhosphorylationANDMEDDSMDLIDSD
CCCCCCCCCCCCCCC		26.9029116813
212 (in isoform 3)Ubiquitination-3.3421890473
215PhosphorylationDSMDLIDSDELLDPE
CCCCCCCCCCCCCHH		26.4528464451
225 (in isoform 1)Ubiquitination-74.6721890473
225UbiquitinationLLDPEDLKKPDPASL
CCCHHHHCCCCHHHH		74.672190698
226UbiquitinationLDPEDLKKPDPASLR
CCHHHHCCCCHHHHH		63.05-
231PhosphorylationLKKPDPASLRAASCG
HCCCCHHHHHHHHCC		24.6323607784
236PhosphorylationPASLRAASCGEGKKR
HHHHHHHHCCCCCCH		22.9728985074
241AcetylationAASCGEGKKRKACKN
HHHCCCCCCHHHCCC		45.1424846251
247UbiquitinationGKKRKACKNCTCGLA
CCCHHHCCCCCCHHH		60.97-
262PhosphorylationEELEKEKSREQMSSQ
HHHHHHHHHHHHHHC		41.9824505115
268PhosphorylationKSREQMSSQPKSACG
HHHHHHHHCCCCCCC		45.2030576142
271UbiquitinationEQMSSQPKSACGNCY
HHHHHCCCCCCCCCC		42.94-
272PhosphorylationQMSSQPKSACGNCYL
HHHHCCCCCCCCCCC		35.1625159151
278PhosphorylationKSACGNCYLGDAFRC
CCCCCCCCCCHHHHH		20.0928152594
287PhosphorylationGDAFRCASCPYLGMP
CHHHHHCCCCCCCCC		21.1721945579
290PhosphorylationFRCASCPYLGMPAFK
HHHCCCCCCCCCCCC		21.8821945579
297AcetylationYLGMPAFKPGEKVLL
CCCCCCCCCCCEEEC		54.9725953088
301AcetylationPAFKPGEKVLLSDSN
CCCCCCCEEECCCCC		44.0623954790
305PhosphorylationPGEKVLLSDSNLHDA
CCCEEECCCCCCCCC		34.5330266825
307PhosphorylationEKVLLSDSNLHDA--
CEEECCCCCCCCC--		37.6030266825
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 CPIN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPIN1_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 CPIN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM8A_HUMANRBM8Aphysical
22939629
ENY2_HUMANENY2physical
22939629
HSPB8_HUMANHSPB8physical
22939629
NEMO_HUMANIKBKGphysical
22939629
RAB5B_HUMANRAB5Bphysical
22939629
DCTP1_HUMANDCTPP1physical
22939629
IPP2_HUMANPPP1R2physical
22939629
SSA27_HUMANSSSCA1physical
22939629
CPIN1_HUMANCIAPIN1physical
20802492
CACB3_HUMANCACNB3physical
26186194
GLRX3_HUMANGLRX3physical
26186194
NDOR1_HUMANNDOR1physical
26186194
BOLA1_HUMANBOLA1physical
26186194
SYAC_HUMANAARSphysical
26344197
AIMP1_HUMANAIMP1physical
26344197
AIMP2_HUMANAIMP2physical
26344197
VATA_HUMANATP6V1Aphysical
26344197
VATB2_HUMANATP6V1B2physical
26344197
VATD_HUMANATP6V1Dphysical
26344197
CUL2_HUMANCUL2physical
26344197
SYDC_HUMANDARSphysical
26344197
MCA3_HUMANEEF1E1physical
26344197
SYEP_HUMANEPRSphysical
26344197
GARS_HUMANGARSphysical
26344197
GUAD_HUMANGDAphysical
26344197
SYIC_HUMANIARSphysical
26344197
SYK_HUMANKARSphysical
26344197
SYLC_HUMANLARSphysical
26344197
SYMC_HUMANMARSphysical
26344197
MSH2_HUMANMSH2physical
26344197
NMD3_HUMANNMD3physical
26344197
RANG_HUMANRANBP1physical
26344197
BRE1A_HUMANRNF20physical
26344197
BRE1B_HUMANRNF40physical
26344197
STAT1_HUMANSTAT1physical
26344197
TWF1_HUMANTWF1physical
26344197
UBA1_HUMANUBA1physical
26344197
UCHL5_HUMANUCHL5physical
26344197
XPP1_HUMANXPNPEP1physical
26344197
NDOR1_HUMANNDOR1physical
28514442
GLRX3_HUMANGLRX3physical
28514442
CACB3_HUMANCACNB3physical
28514442
BOLA1_HUMANBOLA1physical
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 CPIN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-183; SER-305AND SER-307, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-185 ANDSER-307, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.

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