CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000067
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Importin-5 
Protein Synonyms/Alias
 Imp5; Importin subunit beta-3; Karyopherin beta-3; Ran-binding protein 5; RanBP5 
Gene Name
 IPO5 
Gene Synonyms/Alias
 KPNB3; RANBP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45SPDNVVRKQAEETYEubiquitination[1]
125ETQSSMRKKVCDIAAubiquitination[1]
126TQSSMRKKVCDIAAEubiquitination[1, 2]
371MACGLGGKLVLPMIKubiquitination[1]
455FAPGFQKKFHEKVIAubiquitination[1]
521KLQELIQKGTKLVLEubiquitination[2]
574ELRLLRGKTIECISLubiquitination[1]
631SAWARMCKILGKEFQubiquitination[2]
696KTAGLEEKSTACQMLubiquitination[1]
708QMLVCYAKELKEGFVubiquitination[1, 2, 3]
711VCYAKELKEGFVEYTubiquitination[1]
818LGGILKAKLEEHFKNubiquitination[1]
824AKLEEHFKNQELRQVubiquitination[1]
981QSADSKTKENVNATEubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin 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 the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. 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). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. 
Sequence Annotation
 DOMAIN 28 99 Importin N-terminal.
 REPEAT 212 249 HEAT 1.
 REPEAT 395 432 HEAT 2.
 REPEAT 437 475 HEAT 3.
 REPEAT 859 897 HEAT 4.
 REPEAT 901 938 HEAT 5.
 REPEAT 942 979 HEAT 6.
 REGION 325 375 Ran-GTP binding (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 827 827 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1097 AA 
Protein Sequence
MPEDQVGKLE ATENTISAMA AAAAEQQQFY LLLGNLLSPD NVVRKQAEET YENIPGQSKI 60
TFLLQAIRNT TAAEEARQMA AVLLRRLLSS AFDEVYPALP SDVQTAIKSE LLMIIQMETQ 120
SSMRKKVCDI AAELARNLID EDGNNQWPEG LKFLFDSVSS QNVGLREAAL HIFWNFPGIF 180
GNQQQHYLDV IKRMLVQCMQ DQEHPSIRTL SARATAAFIL ANEHNVALFK HFADLLPGFL 240
QAVNDSCYQN DDSVLKSLVE IADTVPKYLR PHLEATLQLS LKLCGDTSLN NMQRQLALEV 300
IVTLSETAAA MLRKHTNIVA QTIPQMLAMM VDLEEDEDWA NADELEDDDF DSNAVAGESA 360
LDRMACGLGG KLVLPMIKEH IMQMLQNPDW KYRHAGLMAL SAIGEGCHQQ MEGILNEIVN 420
FVLLFLQDPH PRVRYAACNA VGQMATDFAP GFQKKFHEKV IAALLQTMED QGNQRVQAHA 480
AAALINFTED CPKSLLIPYL DNLVKHLHSI MVLKLQELIQ KGTKLVLEQV VTSIASVADT 540
AEEKFVPYYD LFMPSLKHIV ENAVQKELRL LRGKTIECIS LIGLAVGKEK FMQDASDVMQ 600
LLLKTQTDFN DMEDDDPQIS YMISAWARMC KILGKEFQQY LPVVMGPLMK TASIKPEVAL 660
LDTQDMENMS DDDGWEFVNL GDQQSFGIKT AGLEEKSTAC QMLVCYAKEL KEGFVEYTEQ 720
VVKLMVPLLK FYFHDGVRVA AAESMPLLLE CARVRGPEYL TQMWHFMCDA LIKAIGTEPD 780
SDVLSEIMHS FAKCIEVMGD GCLNNEHFEE LGGILKAKLE EHFKNQELRQ VKRQDEDYDE 840
QVEESLQDED DNDVYILTKV SDILHSIFSS YKEKVLPWFE QLLPLIVNLI CPHRPWPDRQ 900
WGLCIFDDVI EHCSPASFKY AEYFLRPMLQ YVCDNSPEVR QAAAYGLGVM AQYGGDNYRP 960
FCTEALPLLV RVIQSADSKT KENVNATENC ISAVGKIMKF KPDCVNVEEV LPHWLSWLPL 1020
HEDKEEAVQT FNYLCDLIES NHPIVLGPNN TNLPKIFSII AEGEMHEAIK HEDPCAKRLA 1080
NVVRQVQTSG GLWTECIAQL SPEQQAAIQE LLNSA 1115 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005643; C:nuclear pore; TAS:ProtInc.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc.
 GO:0008565; F:protein transporter activity; ISS:UniProtKB.
 GO:0008536; F:Ran GTPase binding; TAS:ProtInc.
 GO:0006607; P:NLS-bearing substrate import into nucleus; ISS:UniProtKB.
 GO:0006610; P:ribosomal protein import into nucleus; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR000357; HEAT.
 IPR001494; Importin-beta_N. 
Pfam
 PF02985; HEAT 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT
 PS50166; IMPORTIN_B_NT 
PRINTS