NUBP2_HUMAN - dbPTM
NUBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUBP2_HUMAN
UniProt AC Q9Y5Y2
Protein Name Cytosolic Fe-S cluster assembly factor NUBP2 {ECO:0000255|HAMAP-Rule:MF_03039}
Gene Name NUBP2 {ECO:0000255|HAMAP-Rule:MF_03039}
Organism Homo sapiens (Human).
Sequence Length 271
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm . Cytoplasm, cytoskeleton, cilium axoneme . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cytoplasm, cytoskeleton, microtubule organ
Protein Description Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure..
Protein Sequence MEAAAEPGNLAGVRHIILVLSGKGGVGKSTISTELALALRHAGKKVGILDVDLCGPSIPRMLGAQGRAVHQCDRGWAPVFLDREQSISLMSVGFLLEKPDEAVVWRGPKKNALIKQFVSDVAWGELDYLVVDTPPGTSDEHMATIEALRPYQPLGALVVTTPQAVSVGDVRRELTFCRKTGLRVMGIVENMSGFTCPHCTECTSVFSRGGGEELAQLAGVPFLGSVPLDPALMRTLEEGHDFIQEFPGSPAFAALTSIAQKILDATPACLP
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
1Acetylation-------MEAAAEPG
-------CCCCCCCC		7.7422223895
23AcetylationIILVLSGKGGVGKST
EEEEEECCCCCCHHH		49.4619812249
23UbiquitinationIILVLSGKGGVGKST
EEEEEECCCCCCHHH		49.46-
28UbiquitinationSGKGGVGKSTISTEL
ECCCCCCHHHHHHHH		41.86-
29PhosphorylationGKGGVGKSTISTELA
CCCCCCHHHHHHHHH		25.6620860994
30PhosphorylationKGGVGKSTISTELAL
CCCCCHHHHHHHHHH		23.5620860994
32PhosphorylationGVGKSTISTELALAL
CCCHHHHHHHHHHHH		18.8720860994
45UbiquitinationALRHAGKKVGILDVD
HHHHCCCCEEEEEEE		44.79-
45AcetylationALRHAGKKVGILDVD
HHHHCCCCEEEEEEE		44.7919806673
54GlutathionylationGILDVDLCGPSIPRM
EEEEEECCCCCHHHH		6.9722555962
67MethylationRMLGAQGRAVHQCDR
HHHCCCCCHHEECCC		22.74115485699
74MethylationRAVHQCDRGWAPVFL
CHHEECCCCCCCEEE		50.62115485693
86O-linked_GlycosylationVFLDREQSISLMSVG
EEECHHHHEEEEEEE		14.9129351928
88O-linked_GlycosylationLDREQSISLMSVGFL
ECHHHHEEEEEEEEE		24.2229351928
175PhosphorylationGDVRRELTFCRKTGL
HHHHHHHHEHHHHCC		18.8828555341
225PhosphorylationAGVPFLGSVPLDPAL
HCCCCCCCCCCCHHH		23.7829457462
249PhosphorylationFIQEFPGSPAFAALT
HHHHCCCCHHHHHHH		17.19-
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 NUBP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUBP2_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 NUBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEX19_HUMANPEX19physical
22939629
PFD3_HUMANVBP1physical
22939629
PFD6_HUMANPFDN6physical
22939629
RBBP6_HUMANRBBP6physical
22939629
RHOA_HUMANRHOAphysical
22939629
THADA_HUMANTHADAphysical
22939629
UBXN7_HUMANUBXN7physical
22939629
PAIP1_HUMANPAIP1physical
22939629
PP2AA_HUMANPPP2CAphysical
22939629
PTMA_HUMANPTMAphysical
22939629
SRSF2_HUMANSRSF2physical
22939629
STAT6_HUMANSTAT6physical
22939629
CHIP_HUMANSTUB1physical
22939629
TADBP_HUMANTARDBPphysical
22939629
NUDC_HUMANNUDCphysical
22939629
PFD1_HUMANPFDN1physical
22939629
PP14B_HUMANPPP1R14Bphysical
22939629
PP4R2_HUMANPPP4R2physical
22939629
PSMD6_HUMANPSMD6physical
22939629
RD23B_HUMANRAD23Bphysical
22939629
YAP1_HUMANYAP1physical
22939629
PABP4_HUMANPABPC4physical
22939629
PSMD4_HUMANPSMD4physical
22939629
PSME1_HUMANPSME1physical
22939629
PTMS_HUMANPTMSphysical
22939629
S10A9_HUMANS100A9physical
22939629
SC24A_HUMANSEC24Aphysical
22939629
USP9X_HUMANUSP9Xphysical
22939629
ZRAB2_HUMANZRANB2physical
22939629
NUBP1_HUMANNUBP1physical
22863883
UBA6_HUMANUBA6physical
22863883
TNS2_HUMANTENC1physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
CDK5_HUMANCDK5physical
26344197
UCK1_HUMANUCK1physical
26344197
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 NUBP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.

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