NUBP1_HUMAN - dbPTM
NUBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUBP1_HUMAN
UniProt AC P53384
Protein Name Cytosolic Fe-S cluster assembly factor NUBP1 {ECO:0000255|HAMAP-Rule:MF_03038}
Gene Name NUBP1 {ECO:0000255|HAMAP-Rule:MF_03038}
Organism Homo sapiens (Human).
Sequence Length 320
Subcellular Localization Cytoplasm . Nucleus . Cell projection . Cytoplasm, cytoskeleton, cilium axoneme . Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm, cytoskeleton, microtubule organizing center . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, cen
Protein Description Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. [PubMed: 18573874 Required for maturation of extramitochondrial Fe-S proteins]
Protein Sequence MEEVPHDCPGADSAQAGRGASCQGCPNQRLCASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVMSVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLATAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPPTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPATLAYRSIIQRIQEFCNLHQSKEENLISS
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-------MEEVPHDC
-------CCCCCCCC		10.0122223895
13PhosphorylationHDCPGADSAQAGRGA
CCCCCCCHHCCCCCC		23.0322210691
33PhosphorylationPNQRLCASGAGATPD
CCCCCCCCCCCCCCC		28.3429083192
38PhosphorylationCASGAGATPDTAIEE
CCCCCCCCCCHHHHH		22.3025850435
41PhosphorylationGAGATPDTAIEEIKE
CCCCCCCHHHHHHHH		30.6425850435
47 (in isoform 2)Ubiquitination-55.3421906983
47 (in isoform 1)Ubiquitination-55.3421906983
47UbiquitinationDTAIEEIKEKMKTVK
CHHHHHHHHHHCCCC		55.3422817900
49UbiquitinationAIEEIKEKMKTVKHK
HHHHHHHHHCCCCEE		40.4722817900
51UbiquitinationEEIKEKMKTVKHKIL
HHHHHHHCCCCEEEE		62.3222817900
63UbiquitinationKILVLSGKGGVGKST
EEEEEECCCCCCHHH		49.4629967540
63AcetylationKILVLSGKGGVGKST
EEEEEECCCCCCHHH		49.4626051181
189PhosphorylationSVVRYLATAHIDGAV
HHHHHHHHCCCCCEE		19.0425332170
191UbiquitinationVRYLATAHIDGAVII
HHHHHHCCCCCEEEE		17.8322505724
200PhosphorylationDGAVIITTPQEVSLQ
CCEEEECCCCCCCHH		16.7425332170
211UbiquitinationVSLQDVRKEINFCRK
CCHHHHHHHCHHHHH		63.90-
217UbiquitinationRKEINFCRKVKLPII
HHHCHHHHHCCCCEE		42.5422505724
229UbiquitinationPIIGVVENMSGFICP
CEEEEEECCCCCCCC		20.5022505724
240UbiquitinationFICPKCKKESQIFPP
CCCCCCCCHHHCCCC		72.5622505724
252UbiquitinationFPPTTGGAELMCQDL
CCCCCCCCEEEECCC		14.2227667366
264UbiquitinationQDLEVPLLGRVPLDP
CCCCCCCCCCCCCCC		3.1827667366
275UbiquitinationPLDPLIGKNCDKGQS
CCCCCCCCCCCCCCC		47.6227667366
275AcetylationPLDPLIGKNCDKGQS
CCCCCCCCCCCCCCC		47.6227452117
279UbiquitinationLIGKNCDKGQSFFID
CCCCCCCCCCCEEEE		62.14-
279AcetylationLIGKNCDKGQSFFID
CCCCCCCCCCCEEEE		62.1426051181
290PhosphorylationFFIDAPDSPATLAYR
EEEECCCCHHHHHHH		18.5128348404
312PhosphorylationEFCNLHQSKEENLIS
HHHHHHHHHHHHCCC		31.1523898821
313UbiquitinationFCNLHQSKEENLISS
HHHHHHHHHHHCCCC		63.58-
319PhosphorylationSKEENLISS------
HHHHHCCCC------		32.9123186163
320PhosphorylationKEENLISS-------
HHHHCCCC-------		36.9330108239
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 NUBP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUBP1_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 NUBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RCCD1_HUMANRCCD1physical
22939629
DCTP1_HUMANDCTPP1physical
22863883
GNPI1_HUMANGNPDA1physical
22863883
HXK2_HUMANHK2physical
22863883
NOL3_HUMANNOL3physical
22863883
UBQL1_HUMANUBQLN1physical
22863883
XPP1_HUMANXPNPEP1physical
22863883
AIMP1_HUMANAIMP1physical
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 NUBP1_HUMAN

loading...

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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory