dbPTM

IMB2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IMB2_SCHPO
UniProt AC	O14089
Protein Name	Importin subunit beta-2 {ECO:0000250\|UniProtKB:Q92973}
Gene Name	kap104 {ECO:0000303\|PubMed:15116432}
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	910
Subcellular Localization	Cytoplasm . Nucleus envelope .
Protein Description	Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for arginine/glycine-rich nuclear localization signals (rg-NLS) and PY-NLS in cargo substrates. Its predominant cargo substrate seems to be mRNA-binding proteins. 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..
Protein Sequence	MGDNPWVLQEQVLVELSEVIKNSLSENSQTRNAALNLLEKAKDIPDLNNYLTCILINATELSVSIRSAAGLLLKNNVRVSSLESGSGLQSLDYTKSTVIRGLCDPEQLIRGISGNVITTIISRWGISTWPEVLPQLMEMLSSPASTTQEGAFSALTKICEDSAQELDRDFNGTRPLDFMIPRFIELARHENPKIRTDALFCLNQFVLIQSQSLYAHIDTFLETCYALATDVSPNVRKNVCQALVYLLDVRPDKIAPSLGSIVEYMLYSTQDSDQNVALEACEFWLAIAEQPDLCSALGPYLDKIVPMLLQGMVYSDMDLLLLGNDADDYDVEDREEDIRPQHAKGKSRITLNTQGPITQQGSSNADADELEDEDEDDDEFDEDDDAFMDWNLRKCSAAALDVLSSFWKQRLLEIILPHLKQSLTSEDWKVQEAGVLAVGAIAEGCMDGMVQYLPELYPYFLSLLDSKKPLVRTITCWTLGRYSKWASCLESEEDRQKYFVPLLQGLLRMVVDNNKKVQEAGCSAFAILEEQAGPSLVPYLEPILTNLAFAFQKYQRKNVLILYDAVQTLADYVGSALNDKRYIELLITPLLQKWSMIPDDDPNLFPLFECLSSVAVALRDGFAPFAAETYARTFRILRNTLYLITTAQNDPTVDVPDRDFLVTTLDLVSGIIQALGSQVSPLLAQADPPLGQIIGICAKDEVPEVRQSAYALLGDMCMYCFDQIRPYCDALLVDMLPQMQLPLLHVSASNNAIWSAGEMALQLGKDMQQWVKPLLERLICILKSKKSNTTVLENVAITIGRLGVYNPELVAPHLELFYQPWFEIIKTVGENEEKDSAFRGFCNILACNPQALSYLLPMFVLCVAEYENPSAELRDMFQKILQGSVELFNGKASWQASPEVLAQIQAQYGV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
28	Phosphorylation	KNSLSENSQTRNAAL HHHCCCCHHHHHHHH	28.95	21712547

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 IMB2_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IMB2_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 IMB2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IMB2_SCHPO !!

Drug and Disease Associations

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

Regulatory Network of IMB2_SCHPO

Related Literatures of Post-Translational Modification