IMB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IMB1_MOUSE
• UniProt AC: P70168
• Protein Name: Importin subunit beta-1
• Gene Name: Kpnb1
• Organism: Mus musculus (Mouse).
• Sequence Length: 876
• 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: MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPNQLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA

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	-
10	Phosphorylation	LITILEKTVSPDRLE CCHHHHHCCCCCHHH	19.48	26643407
12	Phosphorylation	TILEKTVSPDRLELE HHHHHCCCCCHHHHH	26.72	26643407
23	Acetylation	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	23236377
23	Ubiquitination	LELEAAQKFLERAAV HHHHHHHHHHHHHHH	47.38	22790023
62	Ubiquitination	VAAGLQIKNSLTSKD HHHCCEECCCCCCCC	27.76	22790023
62	Acetylation	VAAGLQIKNSLTSKD HHHCCEECCCCCCCC	27.76	23954790
68	Ubiquitination	IKNSLTSKDPDIKAQ ECCCCCCCCCCHHHH	68.96	22790023
170	Phosphorylation	PEQLQDKSNEILTAI HHHHHHHHHHHHHHH	48.24	29109428
183	Acetylation	AIIQGMRKEEPSNNV HHHHHHCCCCCCCHH	58.50	22826441
206	Acetylation	LNSLEFTKANFDKES HHHHHHHHHCCCCHH	46.80	22826441
211	Acetylation	FTKANFDKESERHFI HHHHCCCCHHHHHHH	60.03	23954790
213	Phosphorylation	KANFDKESERHFIMQ HHCCCCHHHHHHHHH	45.75	23684622
223	S-nitrosylation	HFIMQVVCEATQCPD HHHHHHHHHHHCCCC	2.86	20925432
223	S-nitrosocysteine	HFIMQVVCEATQCPD HHHHHHHHHHHCCCC	2.86	-
376	Ubiquitination	PFIKEHIKNPDWRYR HHHHHHCCCCCCHHH	65.42	22790023
403	Acetylation	GPEPNQLKPLVIQAM CCCCCCCHHHHHHHH	26.92	15216279
537	Ubiquitination	ESLMEIVKNSAKDCY HHHHHHHHHCHHHCH	51.34	22790023
537	Acetylation	ESLMEIVKNSAKDCY HHHHHHHHHCHHHCH	51.34	22826441
541	Acetylation	EIVKNSAKDCYPAVQ HHHHHCHHHCHHHHH	48.42	23806337
541	Succinylation	EIVKNSAKDCYPAVQ HHHHHCHHHCHHHHH	48.42	23806337
585	S-nitrosocysteine	NDLQSLLCATLQNVL HHHHHHHHHHHHHHH	3.09	-
585	S-nitrosylation	NDLQSLLCATLQNVL HHHHHHHHHHHHHHH	3.09	20925432
633	Phosphorylation	EDALMAVSTLVEVLG HHHHHHHHHHHHHHC	13.39	-
634	Phosphorylation	DALMAVSTLVEVLGG HHHHHHHHHHHHHCH	28.37	-
651	Acetylation	LKYMEAFKPFLGIGL HHHHHHHCCHHCCCC	41.74	22826441
710	Ubiquitination	ENVHRSVKPQILSVF CCHHHCCCHHHHHHH	32.24	-
730	Acetylation	AIGGEFKKYLEVVLN HHCCHHHHHHHHHHH	61.46	22826441
765	Glutathionylation	LNELRESCLEAYTGI HHHHHHHHHHHHHHH	3.22	24333276
765	S-palmitoylation	LNELRESCLEAYTGI HHHHHHHHHHHHHHH	3.22	28526873
835	Ubiquitination	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	22790023
835	Acetylation	AFGKDVLKLVEARPM HHCHHHHHHHHHHHH	50.78	22826441
867	Malonylation	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	26320211
867	Acetylation	TLATWATKELRKLKN HHHHHHHHHHHHHHH	47.18	23806337

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

Oops, there are no upstream regulatory protein records of IMB1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IMB1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IMB1_HUMAN	KPNB1	physical	20360068
SOX9_MOUSE	Sox9	physical	15889150
PLCB1_RAT	Plcb1	physical	23665500
IMA1_MOUSE	Kpna2	physical	23665500

Drug and Disease Associations

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