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P52294

- IMA5_HUMAN

UniProt

P52294 - IMA5_HUMAN

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Protein
Importin subunit alpha-5
Gene
KPNA1, RCH2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. 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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.

GO - Molecular functioni

  1. nuclear localization sequence binding Source: ProtInc
  2. protein binding Source: UniProtKB
  3. protein transporter activity Source: InterPro

GO - Biological processi

  1. NLS-bearing protein import into nucleus Source: ProtInc
  2. apoptotic DNA fragmentation Source: Reactome
  3. apoptotic process Source: Reactome
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  5. cytokine-mediated signaling pathway Source: Reactome
  6. intracellular transport of virus Source: Reactome
  7. positive regulation of protein import into nucleus Source: UniProtKB
  8. regulation of DNA recombination Source: ProtInc
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_13462. Activation of DNA fragmentation factor.
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_7991. Vpr-mediated nuclear import of PICs.
SignaLinkiP52294.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-5
Alternative name(s):
Karyopherin subunit alpha-1
Nucleoprotein interactor 1
Short name:
NPI-1
RAG cohort protein 2
SRP1-beta
Cleaved into the following chain:
Gene namesi
Name:KPNA1
Synonyms:RCH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6394. KPNA1.

Subcellular locationi

Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. dendrite Source: UniProtKB
  4. nuclear pore Source: ProtInc
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Importin subunit alpha-5
PRO_0000120719Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 538537Importin subunit alpha-5, N-terminally processed
PRO_0000424491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylthreonine; in Importin subunit alpha-5, N-terminally processed1 Publication

Post-translational modificationi

Polyubiquitinated in the presence of RAG1 (in vitro).

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiP52294.
PaxDbiP52294.
PRIDEiP52294.

PTM databases

PhosphoSiteiP52294.

Miscellaneous databases

PMAP-CutDBP52294.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

ArrayExpressiP52294.
BgeeiP52294.
CleanExiHS_KPNA1.
GenevestigatoriP52294.

Organism-specific databases

HPAiHPA053627.

Interactioni

Subunit structurei

Heterodimer; with KPNB1. Interacts with ANP32E. Interacts with ZIC3 By similarity. Interacts with NSMF; the interaction occurs in a calcium-independent manner after synaptic NMDA receptor stimulation and is required for nuclear import of NSMF but is competed by CABP1 By similarity. Interacts with the nucleoprotein of influenza A viruses. Binds to HCMV (human cytomegalovirus) UL84, HIV-1 Vpr and to ebolavirus VP24. Interacts with APEX1 and RAG1. Interacts with CTNNBL1 (via its N-terminal). Interacts with AICDA (via its NLS). Interacts with SNAI1 (via zinc fingers).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX22EBI-358383,EBI-6863741From a different organism.
DCAF8Q5TAQ92EBI-358383,EBI-740686
GRM1Q132552EBI-358383,EBI-8527352

Protein-protein interaction databases

BioGridi110034. 62 interactions.
DIPiDIP-29296N.
IntActiP52294. 33 interactions.
MINTiMINT-240027.
STRINGi9606.ENSP00000343701.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 928
Helixi96 – 11116
Beta strandi112 – 1154
Helixi118 – 1225
Helixi127 – 1359
Helixi141 – 15515
Helixi159 – 1679
Helixi170 – 1778
Helixi183 – 19715
Helixi201 – 2099
Helixi213 – 2197
Helixi226 – 24015
Beta strandi243 – 2453
Helixi249 – 2513
Helixi253 – 2553
Helixi256 – 2627
Helixi268 – 28114
Beta strandi283 – 2853
Helixi286 – 2949
Turni295 – 2973
Helixi298 – 3047
Helixi310 – 32314
Helixi328 – 3358
Turni336 – 3383
Helixi339 – 3468
Helixi352 – 36514
Helixi370 – 3789
Helixi381 – 39111
Helixi394 – 41017
Helixi413 – 42210
Helixi425 – 4306
Helixi431 – 4333
Helixi437 – 46024
Beta strandi461 – 4633
Helixi468 – 4769
Helixi478 – 4858
Helixi487 – 50418

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JDQX-ray2.20A/B66-512[»]
3TJ3X-ray2.70A/B66-512[»]
4B18X-ray2.52A66-512[»]
ProteinModelPortaliP52294.
SMRiP52294. Positions 10-509.

Miscellaneous databases

EvolutionaryTraceiP52294.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5757IBB
Add
BLAST
Repeati77 – 11741ARM 1; truncated
Add
BLAST
Repeati118 – 16144ARM 2
Add
BLAST
Repeati162 – 20645ARM 3
Add
BLAST
Repeati207 – 24539ARM 4
Add
BLAST
Repeati246 – 29045ARM 5
Add
BLAST
Repeati291 – 33040ARM 6
Add
BLAST
Repeati331 – 37242ARM 7
Add
BLAST
Repeati373 – 41240ARM 8
Add
BLAST
Repeati413 – 45745ARM 9
Add
BLAST
Repeati460 – 50445ARM 10; atypical
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni149 – 24193NLS binding site (major) By similarity
Add
BLAST
Regioni245 – 437193Binding to RAG1
Add
BLAST
Regioni318 – 40689NLS binding site (minor) By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi42 – 5110Nuclear localization signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi25 – 284Poly-Arg

Domaini

Consists of an N-terminal hydrophilic region, a hydrophobic central region composed of 10 repeats, and a short hydrophilic C-terminus. The N-terminal hydrophilic region contains the importin beta binding domain (IBB domain), which is sufficient for binding importin beta and essential for nuclear protein import.1 Publication
The IBB domain is thought to act as an intrasteric autoregulatory sequence by interacting with the internal autoinhibitory NLS. Binding of KPNB1 probably overlaps the internal NLS and contributes to a high affinity for cytoplasmic NLS-containing cargo substrates. After dissociation of the importin/substrate complex in the nucleus the internal autohibitory NLS contributes to a low affinity for nuclear NLS-containing proteins By similarity.1 Publication
The major and minor NLS binding sites are mainly involved in recognition of simple or bipartite NLS motifs. Structurally located within in a helical surface groove they contain several conserved Trp and Asn residues of the corresponding third helices (H3) of ARM repeats which mainly contribute to binding By similarity.1 Publication

Sequence similaritiesi

Belongs to the importin alpha family.
Contains 10 ARM repeats.
Contains 1 IBB domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5064.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52294.
KOiK15042.
OMAiETEPNPP.
OrthoDBiEOG7VHSWV.
PhylomeDBiP52294.
TreeFamiTF354205.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view]
PfamiPF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view]
PIRSFiPIRSF005673. Importin_alpha. 1 hit.
SMARTiSM00185. ARM. 8 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 4 hits.
PS51214. IBB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52294-1 [UniParc]FASTAAdd to Basket

« Hide

MTTPGKENFR LKSYKNKSLN PDEMRRRREE EGLQLRKQKR EEQLFKRRNV    50
ATAEEETEEE VMSDGGFHEA QISNMEMAPG GVITSDMIEM IFSKSPEQQL 100
SATQKFRKLL SKEPNPPIDE VISTPGVVAR FVEFLKRKEN CTLQFESAWV 150
LTNIASGNSL QTRIVIQAGA VPIFIELLSS EFEDVQEQAV WALGNIAGDS 200
TMCRDYVLDC NILPPLLQLF SKQNRLTMTR NAVWALSNLC RGKSPPPEFA 250
KVSPCLNVLS WLLFVSDTDV LADACWALSY LSDGPNDKIQ AVIDAGVCRR 300
LVELLMHNDY KVVSPALRAV GNIVTGDDIQ TQVILNCSAL QSLLHLLSSP 350
KESIKKEACW TISNITAGNR AQIQTVIDAN IFPALISILQ TAEFRTRKEA 400
AWAITNATSG GSAEQIKYLV ELGCIKPLCD LLTVMDSKIV QVALNGLENI 450
LRLGEQEAKR NGTGINPYCA LIEEAYGLDK IEFLQSHENQ EIYQKAFDLI 500
EHYFGTEDED SSIAPQVDLN QQQYIFQQCE APMEGFQL 538
Length:538
Mass (Da):60,222
Last modified:May 18, 2010 - v3
Checksum:iE8407A3352D6051C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731S → N.4 Publications
Corresponds to variant rs4678193 [ dbSNP | Ensembl ].
VAR_050002

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421T → S in AAC60648. 1 Publication
Sequence conflicti169 – 1691G → R in AAC60648. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S75295 mRNA. Translation: AAC60648.1.
BT006959 mRNA. Translation: AAP35605.1.
CR456743 mRNA. Translation: CAG33024.1.
AC083798 Genomic DNA. No translation available.
AC096861 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79482.1.
CH471052 Genomic DNA. Translation: EAW79483.1.
BC002374 mRNA. Translation: AAH02374.1.
BC003009 mRNA. Translation: AAH03009.1.
CCDSiCCDS3013.1.
PIRiI59931.
RefSeqiNP_002255.3. NM_002264.3.
XP_005247494.1. XM_005247437.2.
UniGeneiHs.161008.

Genome annotation databases

EnsembliENST00000344337; ENSP00000343701; ENSG00000114030.
GeneIDi3836.
KEGGihsa:3836.
UCSCiuc003efb.1. human.

Polymorphism databases

DMDMi296439328.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S75295 mRNA. Translation: AAC60648.1 .
BT006959 mRNA. Translation: AAP35605.1 .
CR456743 mRNA. Translation: CAG33024.1 .
AC083798 Genomic DNA. No translation available.
AC096861 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79482.1 .
CH471052 Genomic DNA. Translation: EAW79483.1 .
BC002374 mRNA. Translation: AAH02374.1 .
BC003009 mRNA. Translation: AAH03009.1 .
CCDSi CCDS3013.1.
PIRi I59931.
RefSeqi NP_002255.3. NM_002264.3.
XP_005247494.1. XM_005247437.2.
UniGenei Hs.161008.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JDQ X-ray 2.20 A/B 66-512 [» ]
3TJ3 X-ray 2.70 A/B 66-512 [» ]
4B18 X-ray 2.52 A 66-512 [» ]
ProteinModelPortali P52294.
SMRi P52294. Positions 10-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110034. 62 interactions.
DIPi DIP-29296N.
IntActi P52294. 33 interactions.
MINTi MINT-240027.
STRINGi 9606.ENSP00000343701.

PTM databases

PhosphoSitei P52294.

Polymorphism databases

DMDMi 296439328.

Proteomic databases

MaxQBi P52294.
PaxDbi P52294.
PRIDEi P52294.

Protocols and materials databases

DNASUi 3836.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344337 ; ENSP00000343701 ; ENSG00000114030 .
GeneIDi 3836.
KEGGi hsa:3836.
UCSCi uc003efb.1. human.

Organism-specific databases

CTDi 3836.
GeneCardsi GC03M122140.
HGNCi HGNC:6394. KPNA1.
HPAi HPA053627.
MIMi 600686. gene.
neXtProti NX_P52294.
PharmGKBi PA30185.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5064.
HOGENOMi HOG000167616.
HOVERGENi HBG001846.
InParanoidi P52294.
KOi K15042.
OMAi ETEPNPP.
OrthoDBi EOG7VHSWV.
PhylomeDBi P52294.
TreeFami TF354205.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_13462. Activation of DNA fragmentation factor.
REACT_6248. Transport of Ribonucleoproteins into the Host Nucleus.
REACT_7991. Vpr-mediated nuclear import of PICs.
SignaLinki P52294.

Miscellaneous databases

EvolutionaryTracei P52294.
GeneWikii Karyopherin_alpha_1.
GenomeRNAii 3836.
NextBioi 15079.
PMAP-CutDB P52294.
PROi P52294.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52294.
Bgeei P52294.
CleanExi HS_KPNA1.
Genevestigatori P52294.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR002652. Importin-a_IBB.
IPR024931. Importing_su_alpha.
[Graphical view ]
Pfami PF00514. Arm. 8 hits.
PF01749. IBB. 1 hit.
[Graphical view ]
PIRSFi PIRSF005673. Importin_alpha. 1 hit.
SMARTi SM00185. ARM. 8 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50176. ARM_REPEAT. 4 hits.
PS51214. IBB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein."
    O'Neill R.E., Palese P.
    Virology 206:116-125(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-73.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-73.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-73.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-73.
    Tissue: Lung.
  7. "RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1."
    Cortes P., Ye Z.-S., Baltimore D.
    Proc. Natl. Acad. Sci. U.S.A. 91:7633-7637(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAG1.
  8. "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes."
    Moroianu J., Blobel G., Radu A.
    Proc. Natl. Acad. Sci. U.S.A. 92:2008-2011(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence."
    Moroianu J., Blobel G., Radu A.
    Proc. Natl. Acad. Sci. U.S.A. 93:6572-6576(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 481-495, DOMAINS IBB.
  10. "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins."
    Moroianu J., Hijikata M., Blobel G., Radu A.
    Proc. Natl. Acad. Sci. U.S.A. 92:6532-6536(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT.
  11. "Viral protein R regulates nuclear import of the HIV-1 pre-integration complex."
    Popov S., Rexach M., Zybarth G., Reiling N., Lee M.A., Ratner L., Lane C.M., Moore M.S., Blobel G., Bukrinsky M.
    EMBO J. 17:909-917(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 VPR.
  12. "A nonconventional nuclear localization signal within the UL84 protein of human cytomegalovirus mediates nuclear import via the importin alpha/beta pathway."
    Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.
    J. Virol. 77:3734-3748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCMV UL84.
  13. "Analysis of nuclear transport signals in the human apurinic/apyrimidinic endonuclease (APE1/Ref1)."
    Jackson E.B., Theriot C.A., Chattopadhyay R., Mitra S., Izumi T.
    Nucleic Acids Res. 33:3303-3312(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APEX1.
  14. "Ebola virus VP24 binds karyopherin alpha-1 and blocks STAT1 nuclear accumulation."
    Reid S.P., Leung L.W., Hartman A.L., Martinez O., Shaw M.L., Carbonnelle C., Volchkov V.E., Nichol S.T., Basler C.F.
    J. Virol. 80:5156-5167(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EBOLAVIRUS VP24.
  15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Karyopherin alpha 1 is a putative substrate of the RAG1 ubiquitin ligase."
    Simkus C., Makiya M., Jones J.M.
    Mol. Immunol. 46:1319-1325(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Importin alpha protein acts as a negative regulator for Snail protein nuclear import."
    Sekimoto T., Miyamoto Y., Arai S., Yoneda Y.
    J. Biol. Chem. 286:15126-15131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1.
  19. "CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
    Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
    J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTNNBL1 AND AICDA.
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiIMA5_HUMAN
AccessioniPrimary (citable) accession number: P52294
Secondary accession number(s): D3DN93, Q6IBQ9, Q9BQ56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 18, 2010
Last modified: September 3, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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