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P52292

- IMA1_HUMAN

UniProt

P52292 - IMA1_HUMAN

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Protein

Importin subunit alpha-1

Gene

KPNA2

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.

GO - Molecular functioni

  1. histone deacetylase binding Source: BHF-UCL
  2. nuclear localization sequence binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein transporter activity Source: InterPro

GO - Biological processi

  1. cytokine-mediated signaling pathway Source: Reactome
  2. DNA metabolic process Source: ProtInc
  3. NLS-bearing protein import into nucleus Source: UniProtKB
  4. regulation of DNA recombination Source: ProtInc
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
SignaLinkiP52292.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-1
Alternative name(s):
Karyopherin subunit alpha-2
RAG cohort protein 1
SRP1-alpha
Gene namesi
Name:KPNA2
Synonyms:RCH1, SRP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6395. KPNA2.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 529528Importin subunit alpha-1PRO_0000120722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei62 – 621Phosphoserine5 Publications
Modified residuei490 – 4901Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52292.
PaxDbiP52292.
PeptideAtlasiP52292.
PRIDEiP52292.

2D gel databases

SWISS-2DPAGEP52292.

PTM databases

PhosphoSiteiP52292.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

BgeeiP52292.
CleanExiHS_KPNA2.
ExpressionAtlasiP52292. baseline and differential.
GenevestigatoriP52292.

Organism-specific databases

HPAiCAB015460.
HPA041270.

Interactioni

Subunit structurei

Heterodimer; with KPNB1. Interacts with ANP32E (By similarity). Component of a complex containing CSE1L, RAN and KPNA2. Interacts directly with CSE1L. Interacts with HIV-1 Vpr and PLAG1. Interacts with APEX1 (via N-terminus). Interacts with FRG1 (via N-terminus). Interacts with ARL4A, CTNNBL1 and NBN. Interacts with SNAI1 (via zinc fingers) and SNAI2 (via zinc fingers).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383983EBI-349938,EBI-349905
JUNP054122EBI-349938,EBI-852823
L1P031013EBI-349938,EBI-7362698From a different organism.
L2P031073EBI-349938,EBI-7362531From a different organism.
npm2Q6GQG62EBI-349938,EBI-8469111From a different organism.
RECQLP460632EBI-349938,EBI-2823728
S100A2P290345EBI-349938,EBI-752230
S100A6P067033EBI-349938,EBI-352877
SUN2Q9UH993EBI-349938,EBI-1044964

Protein-protein interaction databases

BioGridi110036. 131 interactions.
DIPiDIP-6205N.
IntActiP52292. 74 interactions.
MINTiMINT-94121.
STRINGi9606.ENSP00000332455.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Turni18 – 214Combined sources
Helixi30 – 4819Combined sources
Helixi78 – 858Combined sources
Helixi90 – 10415Combined sources
Beta strandi106 – 1083Combined sources
Helixi112 – 1176Combined sources
Helixi120 – 12910Combined sources
Helixi134 – 14714Combined sources
Helixi152 – 1609Combined sources
Helixi163 – 1708Combined sources
Helixi176 – 19015Combined sources
Helixi194 – 2029Combined sources
Helixi206 – 2116Combined sources
Helixi218 – 2203Combined sources
Helixi223 – 23614Combined sources
Helixi246 – 25914Combined sources
Helixi265 – 27915Combined sources
Helixi283 – 2919Combined sources
Helixi295 – 3017Combined sources
Helixi307 – 32014Combined sources
Helixi325 – 3339Combined sources
Helixi336 – 3449Combined sources
Helixi349 – 36214Combined sources
Helixi367 – 3759Combined sources
Helixi379 – 38810Combined sources
Helixi391 – 40717Combined sources
Helixi410 – 4189Combined sources
Helixi422 – 4276Combined sources
Helixi428 – 4303Combined sources
Helixi434 – 45320Combined sources
Helixi457 – 46610Combined sources
Helixi469 – 4757Combined sources
Helixi476 – 4783Combined sources
Helixi482 – 49514Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFXX-ray3.00C204-212[»]
1QGKX-ray2.50B11-54[»]
1QGRX-ray2.30B28-54[»]
3FEXX-ray3.55C70-529[»]
3FEYX-ray2.20C70-529[»]
4E4VX-ray2.53A/B70-529[»]
ProteinModelPortaliP52292.
SMRiP52292. Positions 11-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52292.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 6059IBBPROSITE-ProRule annotationAdd
BLAST
Repeati71 – 11141ARM 1; truncatedAdd
BLAST
Repeati112 – 15140ARM 2Add
BLAST
Repeati152 – 19342ARM 3Add
BLAST
Repeati200 – 24445ARM 4Add
BLAST
Repeati246 – 28237ARM 5Add
BLAST
Repeati283 – 32240ARM 6Add
BLAST
Repeati325 – 36440ARM 7Add
BLAST
Repeati367 – 40943ARM 8Add
BLAST
Repeati410 – 45647ARM 9Add
BLAST
Repeati457 – 49640ARM 10; atypicalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 23897NLS binding site (major)By similarityAdd
BLAST
Regioni315 – 40389NLS binding site (minor)By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5410Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 314Poly-Arg
Compositional biasi499 – 5024Poly-Glu

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).By similarity
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).By similarity

Sequence similaritiesi

Belongs to the importin alpha family.Curated
Contains 10 ARM repeats.PROSITE-ProRule annotation
Contains 1 IBB domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5064.
GeneTreeiENSGT00760000119094.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52292.
KOiK15043.
OMAiNETEKLC.
PhylomeDBiP52292.
TreeFamiTF101178.

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. 5 hits.
PS51214. IBB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P52292-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTNENANTP AARLHRFKNK GKDSTEMRRR RIEVNVELRK AKKDDQMLKR
60 70 80 90 100
RNVSSFPDDA TSPLQENRNN QGTVNWSVDD IVKGINSSNV ENQLQATQAA
110 120 130 140 150
RKLLSREKQP PIDNIIRAGL IPKFVSFLGR TDCSPIQFES AWALTNIASG
160 170 180 190 200
TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSVFRDLV
210 220 230 240 250
IKYGAVDPLL ALLAVPDMSS LACGYLRNLT WTLSNLCRNK NPAPPIDAVE
260 270 280 290 300
QILPTLVRLL HHDDPEVLAD TCWAISYLTD GPNERIGMVV KTGVVPQLVK
310 320 330 340 350
LLGASELPIV TPALRAIGNI VTGTDEQTQV VIDAGALAVF PSLLTNPKTN
360 370 380 390 400
IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVSVLSKAD FKTQKEAVWA
410 420 430 440 450
VTNYTSGGTV EQIVYLVHCG IIEPLMNLLT AKDTKIILVI LDAISNIFQA
460 470 480 490 500
AEKLGETEKL SIMIEECGGL DKIEALQNHE NESVYKASLS LIEKYFSVEE
510 520
EEDQNVVPET TSEGYTFQVQ DGAPGTFNF
Length:529
Mass (Da):57,862
Last modified:October 1, 1996 - v1
Checksum:iB0F94A0475B80EED
GO

Mass spectrometryi

Molecular mass is 57861.92 Da from positions 1 - 529. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571A → V.2 Publications
Corresponds to variant rs17850032 [ dbSNP | Ensembl ].
VAR_067625
Natural varianti165 – 1651P → R.1 Publication
Corresponds to variant rs11545989 [ dbSNP | Ensembl ].
VAR_013137
Natural varianti365 – 3651G → S.
Corresponds to variant rs1059558 [ dbSNP | Ensembl ].
VAR_067626
Natural varianti430 – 4301T → P.
Corresponds to variant rs1059538 [ dbSNP | Ensembl ].
VAR_014453
Natural varianti453 – 4531K → N.2 Publications
Corresponds to variant rs17850031 [ dbSNP | Ensembl ].
VAR_067627

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28386 mRNA. Translation: AAA69957.1.
AJ303086 Genomic DNA. Translation: CAC83080.1.
BT006665 mRNA. Translation: AAP35311.1.
CH471099 Genomic DNA. Translation: EAW89041.1.
BC005978 mRNA. Translation: AAH05978.1.
BC146905 mRNA. Translation: AAI46906.1.
U09559 mRNA. Translation: AAA65700.1.
CCDSiCCDS32713.1.
PIRiA56516.
RefSeqiNP_002257.1. NM_002266.2.
UniGeneiHs.594238.

Genome annotation databases

GeneIDi3838.
KEGGihsa:3838.
UCSCiuc002jgk.3. human.

Polymorphism databases

DMDMi1708480.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28386 mRNA. Translation: AAA69957.1 .
AJ303086 Genomic DNA. Translation: CAC83080.1 .
BT006665 mRNA. Translation: AAP35311.1 .
CH471099 Genomic DNA. Translation: EAW89041.1 .
BC005978 mRNA. Translation: AAH05978.1 .
BC146905 mRNA. Translation: AAI46906.1 .
U09559 mRNA. Translation: AAA65700.1 .
CCDSi CCDS32713.1.
PIRi A56516.
RefSeqi NP_002257.1. NM_002266.2.
UniGenei Hs.594238.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EFX X-ray 3.00 C 204-212 [» ]
1QGK X-ray 2.50 B 11-54 [» ]
1QGR X-ray 2.30 B 28-54 [» ]
3FEX X-ray 3.55 C 70-529 [» ]
3FEY X-ray 2.20 C 70-529 [» ]
4E4V X-ray 2.53 A/B 70-529 [» ]
ProteinModelPortali P52292.
SMRi P52292. Positions 11-499.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110036. 131 interactions.
DIPi DIP-6205N.
IntActi P52292. 74 interactions.
MINTi MINT-94121.
STRINGi 9606.ENSP00000332455.

Chemistry

BindingDBi P52292.
ChEMBLi CHEMBL1741187.

PTM databases

PhosphoSitei P52292.

Polymorphism databases

DMDMi 1708480.

2D gel databases

SWISS-2DPAGE P52292.

Proteomic databases

MaxQBi P52292.
PaxDbi P52292.
PeptideAtlasi P52292.
PRIDEi P52292.

Protocols and materials databases

DNASUi 3838.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3838.
KEGGi hsa:3838.
UCSCi uc002jgk.3. human.

Organism-specific databases

CTDi 3838.
GeneCardsi GC17P066031.
HGNCi HGNC:6395. KPNA2.
HPAi CAB015460.
HPA041270.
MIMi 600685. gene.
neXtProti NX_P52292.
PharmGKBi PA30186.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5064.
GeneTreei ENSGT00760000119094.
HOGENOMi HOG000167616.
HOVERGENi HBG001846.
InParanoidi P52292.
KOi K15043.
OMAi NETEKLC.
PhylomeDBi P52292.
TreeFami TF101178.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
SignaLinki P52292.

Miscellaneous databases

ChiTaRSi KPNA2. human.
EvolutionaryTracei P52292.
GeneWikii Karyopherin_alpha_2.
GenomeRNAii 3838.
NextBioi 15087.
PROi P52292.
SOURCEi Search...

Gene expression databases

Bgeei P52292.
CleanExi HS_KPNA2.
ExpressionAtlasi P52292. baseline and differential.
Genevestigatori P52292.

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. 5 hits.
PS51214. IBB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences."
    Weis K., Mattaj I.W., Lamond A.I.
    Science 268:1049-1053(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy repeat on chromosome 17q23-q24 and mutation analysis in patients with Russell-Silver syndrome."
    Doerr S., Schlicker M., Hansmann I.
    Hum. Genet. 109:479-486(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-165.
  3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-157 AND ASN-453.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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], VARIANTS VAL-157 AND ASN-453.
    Tissue: Bone marrow and Testis.
  6. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 69-101; 107-117; 239-258; 292-315; 354-388 AND 487-494, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hepatoma.
  7. "Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein."
    Cuomo C.A., Kirch S.A., Gyuris J., Brent R., Oettinger M.A.
    Proc. Natl. Acad. Sci. U.S.A. 91:6156-6160(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-529.
    Tissue: Cervix carcinoma.
  8. "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: SUBUNIT, SUBCELLULAR LOCATION.
  9. "The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import."
    Weis K., Ryder U., Lamond A.I.
    EMBO J. 15:1818-1825(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN IBB.
  10. "Export of importin-alpha from the nucleus is mediated by a specific nuclear transport factor."
    Kutay U., Bischoff F.R., Kostka S., Kraft R., Goerlich D.
    Cell 90:1061-1071(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH RAN AND CSE1L.
  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. "Determination of the functional domain organization of the importin alpha nuclear import factor."
    Herold A., Truant R., Wiegand H., Cullen B.R.
    J. Cell Biol. 143:309-318(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XPO2/CSE1L.
  13. "ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli."
    Lin C.Y., Huang P.H., Liao W.L., Cheng H.J., Huang C.F., Kuo J.C., Patton W.A., Massenburg D., Moss J., Lee F.J.
    J. Biol. Chem. 275:37815-37823(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARL4A.
  14. "Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal."
    Braem C.V., Kas K., Meyen E., Debiec-Rychter M., Van De Ven W.J.M., Voz M.L.
    J. Biol. Chem. 277:19673-19678(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLAG1.
  15. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  16. "Importin KPNA2 is required for proper nuclear localization and multiple functions of NBS1."
    Tseng S.-F., Chang C.-Y., Wu K.-J., Teng S.-C.
    J. Biol. Chem. 280:39594-39600(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBN.
  17. "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.
  18. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "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.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Characterization of Snail nuclear import pathways as representatives of C2H2 zinc finger transcription factors."
    Mingot J.M., Vega S., Maestro B., Sanz J.M., Nieto M.A.
    J. Cell Sci. 122:1452-1460(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1 AND SNAI2.
  25. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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.
  29. "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.
  30. "Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA-associated and actin-bundling protein."
    Sun C.Y., van Koningsbruggen S., Long S.W., Straasheijm K., Klooster R., Jones T.I., Bellini M., Levesque L., Brieher W.M., van der Maarel S.M., Jones P.L.
    J. Mol. Biol. 411:397-416(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRG1.
  31. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Structure of importin-beta bound to the IBB domain of importin-alpha."
    Cingolani G., Petosa C., Weis K., Muller C.W.
    Nature 399:221-229(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 11-54.

Entry informationi

Entry nameiIMA1_HUMAN
AccessioniPrimary (citable) accession number: P52292
Secondary accession number(s): B9EJD6, Q53YE3, Q9BRU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 174 of the entry and version 1 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 17
    Human chromosome 17: 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