dbPTM

IMB1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMB1_SCHPO
UniProt AC	O13864
Protein Name	Importin subunit beta-1 {ECO:0000250\|UniProtKB:Q06142}
Gene Name	kap95 {ECO:0000250\|UniProtKB:Q06142}
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	863
Subcellular Localization	Cytoplasm . Nucleus envelope . Nucleus, nuclear pore complex .
Protein Description	Importin beta subunit that functions in nuclear protein import through association with the importin alpha subunit, which binds to the clasical nuclear localization signal (cNLS) in cargo substrates. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by importin beta through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binds to importin beta and the three components separate, leading to release of the cargo. Importin alpha and beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin beta. 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..
Protein Sequence	MNAGEFLAQTLSPDANVRLNAEKQLENAARTDFAQYMVLLAQELANDNSMPYIRMAAGLALKNAITAREEARKLEYQQLWQSLPVEIKQQVKSLALQTLGSSEHQAGQSAAQLVAAIAAYELATNQWPDLMVTLVANVGEGQPSALKQHSLQTIGYICESVSPEVLSAQSNAILTAVVAGARKEEPDAAVRLAALGALYDSLEFVRENFNNEYERNYIMQVVCEATQSPEASIQTAAFGCLVKIMHLYYDTMPFYMEKALFALTTQGMYNTNEQVALQAVEFWSTVCEEEIEVNLEIQEAQDLNEVPARQNHGFARAAAADILPVLLKLLCNQDEDADEDDWNISMAAATCLQLFAQVVGDLIVNPVLAFVEQNIQNPDWHQREAAVMAFGSVLEGPNVAMLTPLVNQALPVLINMMVDPVIFVKDTTAWALGQISSFVADAINPEIHLSPMVSALLQGLTDNPRIVANCCWAFMNLVCHFAPVDNHQTSVMTPFYEAIIGSLLHVTDQKGNENNSRTSGYETLGTLITFSSDSVLPMIANVLSIILTRLETSIQMQSQILDVEDRANHDELQSNLCNVLTSIIRRFGPDIRTSSDQIMNLLLQTMQTAPKQSVVHEDVLLAIGAMMNSLEEQFEVYVPSFVPFLSSALSNEQEYQLCSVAVGLVGDLARALNAKILPYCDDFMTRLVQDLQSSVLDRNVKPAILSCFSDIALAIGAAFQTYLEAVMVLLQQASSVQAPPGANFSMIDYVDALRLGIVEAYVGITQAVRTDNRLDLIQPYVHSMFTLLNMITADPECSESLTRAALGLLGDLAESFPKGELKSYFAADWVAALLNSGKTKISSQQTKDLARWATEQVKRQARA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
12	Phosphorylation	EFLAQTLSPDANVRL HHHHHHCCCCCCHHC	24.91	29996109

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 IMB1_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMB1_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 IMB1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IMB1_SCHPO !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IMB1_SCHPO

Related Literatures of Post-Translational Modification