IMB1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IMB1_RAT
• UniProt AC: P52296
• Protein Name: Importin subunit beta-1
• Gene Name: Kpnb1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 875
• Subcellular Localization: Cytoplasm . Nucleus envelope .
• Protein Description: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 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, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are 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. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with IPO7 mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports SNAI1 and PRKCI into the nucleus (By similarity)..
• Protein Sequence: MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIRLLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPNQLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLWKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAECQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDITLAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA

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
1	Acetylation	-------MELITILE -------CCCCHHHH	9.49	-
5	Phosphorylation	---MELITILEKTVS ---CCCCHHHHHCCC	31.94	25575281
10	Phosphorylation	LITILEKTVSPDRLE CCHHHHHCCCCCHHH	19.48	25575281
12	Phosphorylation	TILEKTVSPDRLELE HHHHHCCCCCHHHHH	26.72	25575281
210	Acetylation	FTKANFDKESERHFI HHHHCCCCHHHHHHH	60.03	-
834	Acetylation	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	-
866	Acetylation	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	22902405

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of IMB1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IMB1_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IMB1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of IMB1_RAT !!

Drug and Disease Associations

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