NBP35_YEAST - dbPTM
NBP35_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NBP35_YEAST
UniProt AC P52920
Protein Name Cytosolic Fe-S cluster assembly factor NBP35 {ECO:0000255|HAMAP-Rule:MF_03038}
Gene Name NBP35 {ECO:0000255|HAMAP-Rule:MF_03038}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 328
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export..
Protein Sequence MTEILPHVNDEVLPAEYELNQPEPEHCPGPESDMAGKSDACGGCANKEICESLPKGPDPDIPLITDNLSGIEHKILVLSGKGGVGKSTFAAMLSWALSADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVTDNLATMSIQYMLPEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMRESGIDGALVVTTPQEVALLDVRKEIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKATTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPDSPASSAVLNVVEALRDAVGDV
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

Oops, there are no PTM records of NBP35_YEAST !!

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 NBP35_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NBP35_YEAST !!

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 NBP35_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAO3_YEASTTAO3physical
11805826
DPOD_YEASTPOL3genetic
12759774
CFD1_YEASTCFD1physical
22362766
NBP35_YEASTNBP35physical
22362766
CFD1_YEASTCFD1physical
23798678
SEC18_YEASTSEC18genetic
27708008
DPOD_YEASTPOL3genetic
27708008
SCC2_YEASTSCC2genetic
27708008
TFB1_YEASTTFB1genetic
27708008
UTP5_YEASTUTP5genetic
27708008
GPI19_YEASTGPI19genetic
27708008
SMC1_YEASTSMC1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
YHS2_YEASTCIA2genetic
27708008
DNA2_YEASTDNA2genetic
27708008
CTF8_YEASTCTF8genetic
27708008
MET30_YEASTMET30genetic
27708008
SMC3_YEASTSMC3genetic
27708008
DPB11_YEASTDPB11genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
ESS1_YEASTESS1genetic
27708008
ABF1_YEASTABF1genetic
27708008
RSC4_YEASTRSC4genetic
27708008
SSL1_YEASTSSL1genetic
27708008
SMC4_YEASTSMC4genetic
27708008
RFC4_YEASTRFC4genetic
27708008
ARP7_YEASTARP7genetic
27708008
SWC5_YEASTSWC5genetic
27708008
DCC1_YEASTDCC1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
MNN10_YEASTMNN10genetic
27708008
VPS72_YEASTVPS72genetic
27708008
AIM11_YEASTAIM11genetic
27708008
NPR3_YEASTNPR3genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
FEN1_YEASTRAD27genetic
27708008
ORN_YEASTREX2genetic
27708008
ARP6_YEASTARP6genetic
27708008
ROM2_YEASTROM2genetic
27708008
CTF18_YEASTCTF18genetic
27708008
PET8_YEASTPET8genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
ULS1_YEASTULS1genetic
27708008
CTF4_YEASTCTF4genetic
27708008
CFD1_YEASTCFD1physical
26195633
NBP35_YEASTNBP35physical
26195633

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NBP35_YEAST

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Related Literatures of Post-Translational Modification

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