UBI4P_SCHPO - dbPTM
UBI4P_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBI4P_SCHPO
UniProt AC P0CG72
Protein Name Polyubiquitin
Gene Name ubi4
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 382
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity)..
Protein Sequence MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGLF
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
6Ubiquitination--MQIFVKTLTGKTI
--CEEEEEECCCCEE
27.37-
11UbiquitinationFVKTLTGKTITLEVE
EEEECCCCEEEEEEE
31.36-
27UbiquitinationSDTIDNVKSKIQDKE
CCCHHHHHHHCCCCC
52.89-
33UbiquitinationVKSKIQDKEGIPPDQ
HHHHCCCCCCCCHHH
41.27-
55PhosphorylationKQLEDGRTLSDYNIQ
EECCCCCCCCCCCCC
35.8224763107
57PhosphorylationLEDGRTLSDYNIQKE
CCCCCCCCCCCCCCH
37.1228889911
131PhosphorylationKQLEDGRTLSDYNIQ
EECCCCCCCCCCCCC
35.8224763107
133PhosphorylationLEDGRTLSDYNIQKE
CCCCCCCCCCCCCCH
37.1228889911
207PhosphorylationKQLEDGRTLSDYNIQ
EECCCCCCCCCCCCC
35.8224763107
209PhosphorylationLEDGRTLSDYNIQKE
CCCCCCCCCCCCCCH
37.1228889911
283PhosphorylationKQLEDGRTLSDYNIQ
EECCCCCCCCCCCCC
35.8224763107
285PhosphorylationLEDGRTLSDYNIQKE
CCCCCCCCCCCCCCH
37.1228889911
359PhosphorylationKQLEDGRTLSDYNIQ
EECCCCCCCCCCCCC
35.8224763107
361PhosphorylationLEDGRTLSDYNIQKE
CCCCCCCCCCCCCCH
37.1228889911

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 UBI4P_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBI4P_SCHPO !!

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 UBI4P_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMP2_SCHPOimp2physical
19139265
AAT1_SCHPOaat1physical
22194353
ZIP1_SCHPOzip1physical
15660136
MEI2_SCHPOmei2physical
11702950
AP1_SCHPOpap1physical
23209828
MIK1_SCHPOmik1physical
10637286
SLP1_SCHPOslp1physical
23442800
PCNA_SCHPOpcn1physical
16641370
AAT1_SCHPOaat1physical
24454826
MEI2_SCHPOmei2physical
24741065
CENPA_SCHPOcnp1physical
25298518

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBI4P_SCHPO

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Related Literatures of Post-Translational Modification

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