IMB3_SCHPO - dbPTM
IMB3_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMB3_SCHPO
UniProt AC O74476
Protein Name Importin subunit beta-3 {ECO:0000250|UniProtKB:P32337}
Gene Name sal3 {ECO:0000303|PubMed:12399381}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1095
Subcellular Localization Cytoplasm . Nucleus envelope . Nucleus .
Protein Description Involved in the nuclear import of cdc25 and mcs1.; Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Involved in the nuclear import of cdc25 and mcs1. [PubMed: 12399381 Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity]
Protein Sequence MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLPGDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVFRTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLADCLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDVAGDPEDEAEELQEWLNTDDLDQDESDANHVVAEQAMDRLSRKLGGKTILPPSFTWLPRLIPSQKWSERHAALMAISSIAEGAEKLMKKELSRVLDMVLPLLADPHPRVRWAACNAVGQMSTDFAPDMQVKYPSRILEALVPVLESPESRVQAHAAAAMVNFSEEADNKVLEPYLDDILQRLLTLLQSPKRYVQEQAVTTIATVADAAAKKFEKYFDAIMPLLFNVLQQADGKEFRTLRGKTMECATLIALAVGKQRFLPVSQELIQILGNIQMGITDSDDPQASYLISAWGRICRVLGSDFVPFLSSVMPPLLVAATSKPDFTIIDDEVDESKYSEQDGWEFIPVHGQQVGIRTSTLEDKCTATEMLVCYAAELKADFDPYVNEVLTSVVLPGLKFFFHDGVRSACCKCIPQLLNARILASNRDPAKVNELWEPILRKLLDHIQNEPSVEMLADYFECFYQSLEISGLNLSPSSMEALVAAVDLQLKGFISRVQQREEEAKNGDIDIEEDEDMILAVENDQNLLNEINKTFSVVLKIHKTAFCPFWERLLPYMDGFLSGNDTVAKQWALCMMDDLIEFTGPDSWNYKDHFLPYLAEGIQSSEPEIRQAASYGIGVAAQHGGELYAEICSSALPALFKMLELPDARDEEQIYATENICVAICKICRFCSQRVQDLDKVVTYWINTLPVTHDEDDAPYAYTFLAELMEQNHVAVASQMPTIITILAETFASGVLRGRTLTRLMEASKVYLARFPADQVNSVIATLSVDNQRALSAHF
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
655PhosphorylationEVDESKYSEQDGWEF
CCCHHHCCCCCCCEE
32.3021712547

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 IMB3_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMB3_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 IMB3_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPIP_SCHPOcdc25genetic
12399381
RDP1_SCHPOrdp1physical
22268381
FLP1_SCHPOclp1physical
23297348
PHP4_SCHPOphp4physical
25330182

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IMB3_SCHPO

loading...

Related Literatures of Post-Translational Modification

TOP