Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Importin-5

Gene

IPO5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  1. GTPase inhibitor activity Source: ProtInc
  2. poly(A) RNA binding Source: UniProtKB
  3. protein transporter activity Source: UniProtKB
  4. Ran GTPase binding Source: ProtInc

GO - Biological processi

  1. cellular response to amino acid stimulus Source: UniProtKB
  2. negative regulation of catalytic activity Source: GOC
  3. NLS-bearing protein import into nucleus Source: UniProtKB
  4. positive regulation of protein import into nucleus Source: UniProtKB
  5. ribosomal protein import into nucleus Source: UniProtKB
  6. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_9434. vRNP Assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Importin-5
Short name:
Imp5
Alternative name(s):
Importin subunit beta-3
Karyopherin beta-3
Ran-binding protein 5
Short name:
RanBP5
Gene namesi
Name:IPO5
Synonyms:KPNB3, RANBP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:6402. IPO5.

Subcellular locationi

Cytoplasm. Nucleus. Nucleusnucleolus
Note: Nucleus; nuclear rim. Found particularly in the nuclear rim and nucleolus.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. membrane Source: UniProtKB
  5. nuclear membrane Source: HPA
  6. nuclear pore Source: ProtInc
  7. nucleolus Source: UniProtKB-SubCell
  8. nucleoplasm Source: HPA
  9. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 10971096Importin-5PRO_0000120771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei827 – 8271Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO00410.
PaxDbiO00410.
PRIDEiO00410.

PTM databases

PhosphoSiteiO00410.

Expressioni

Gene expression databases

BgeeiO00410.
CleanExiHS_IPO5.
ExpressionAtlasiO00410. baseline and differential.
GenevestigatoriO00410.

Organism-specific databases

HPAiCAB009110.
HPA040983.
HPA056548.

Interactioni

Subunit structurei

Binds RPL23A, RPS7 and RPL5. Interacts with H2A, H2B, H3 and H4 histones (By similarity). Binds to HIV-1 Rev.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279585EBI-356424,EBI-8753518From a different organism.
GABARAPO951666EBI-356424,EBI-712001
GABARAPL1Q9H0R84EBI-356424,EBI-746969
GABARAPL2P605205EBI-356424,EBI-720116
MAP1LC3BQ9GZQ82EBI-356424,EBI-373144
MAP1LC3CQ9BXW42EBI-356424,EBI-2603996
RPL7P181244EBI-356424,EBI-350806

Protein-protein interaction databases

BioGridi110041. 60 interactions.
DIPiDIP-41042N.
IntActiO00410. 26 interactions.
MINTiMINT-132356.
STRINGi9606.ENSP00000261574.

Structurei

3D structure databases

ProteinModelPortaliO00410.
SMRiO00410. Positions 14-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati5 – 3834HEAT 1By similarity1 PublicationAdd
BLAST
Domaini28 – 9972Importin N-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati43 – 7735HEAT 2By similarity1 PublicationAdd
BLAST
Repeati95 – 12228HEAT 3By similarity1 PublicationAdd
BLAST
Repeati130 – 15728HEAT 4By similarity1 PublicationAdd
BLAST
Repeati167 – 20135HEAT 5By similarity1 PublicationAdd
BLAST
Repeati210 – 24637HEAT 6By similarity1 PublicationAdd
BLAST
Repeati254 – 28936HEAT 7By similarity1 PublicationAdd
BLAST
Repeati298 – 35053HEAT 8By similarity1 PublicationAdd
BLAST
Repeati352 – 38635HEAT 9By similarity1 PublicationAdd
BLAST
Repeati390 – 43041HEAT 10By similarity1 PublicationAdd
BLAST
Repeati432 – 47241HEAT 11By similarity1 PublicationAdd
BLAST
Repeati475 – 52349HEAT 12By similarity1 PublicationAdd
BLAST
Repeati525 – 56844HEAT 13By similarity1 PublicationAdd
BLAST
Repeati570 – 61546HEAT 14By similarity1 PublicationAdd
BLAST
Repeati617 – 69276HEAT 15By similarity1 PublicationAdd
BLAST
Repeati695 – 73743HEAT 16By similarity1 PublicationAdd
BLAST
Repeati741 – 78040HEAT 17By similarity1 PublicationAdd
BLAST
Repeati787 – 85367HEAT 18By similarity1 PublicationAdd
BLAST
Repeati856 – 89540HEAT 19By similarity1 PublicationAdd
BLAST
Repeati903 – 93533HEAT 20By similarity1 PublicationAdd
BLAST
Repeati943 – 98341HEAT 21By similarity1 PublicationAdd
BLAST
Repeati990 – 102132HEAT 22By similarity1 PublicationAdd
BLAST
Repeati1032 – 106736HEAT 23By similarity1 PublicationAdd
BLAST
Repeati1070 – 109324HEAT 24By similarity1 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni325 – 37551Ran-GTP bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 65Poly-Ala
Compositional biasi460 – 4656Poly-Ala

Sequence similaritiesi

Contains 24 HEAT repeats.By similarity1 Publication
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5215.
GeneTreeiENSGT00550000074773.
HOGENOMiHOG000209725.
HOVERGENiHBG006156.
InParanoidiO00410.
OMAiDTNLNNM.
OrthoDBiEOG7Q5HCD.
PhylomeDBiO00410.
TreeFamiTF300344.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF02985. HEAT. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00410-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGQS KITFLLQAIR
60 70 80 90 100
NTTAAEEARQ MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME
110 120 130 140 150
TQSSMRKKVC DIAAELARNL IDEDGNNQWP EGLKFLFDSV SSQNVGLREA
160 170 180 190 200
ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC MQDQEHPSIR TLSARATAAF
210 220 230 240 250
ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL VEIADTVPKY
260 270 280 290 300
LRPHLEATLQ LSLKLCGDTS LNNMQRQLAL EVIVTLSETA AAMLRKHTNI
310 320 330 340 350
VAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL
360 370 380 390 400
GGKLVLPMIK EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI
410 420 430 440 450
VNFVLLFLQD PHPRVRYAAC NAVGQMATDF APGFQKKFHE KVIAALLQTM
460 470 480 490 500
EDQGNQRVQA HAAAALINFT EDCPKSLLIP YLDNLVKHLH SIMVLKLQEL
510 520 530 540 550
IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH IVENAVQKEL
560 570 580 590 600
RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ
610 620 630 640 650
ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN
660 670 680 690 700
MSDDDGWEFV NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT
710 720 730 740 750
EQVVKLMVPL LKFYFHDGVR VAAAESMPLL LECARVRGPE YLTQMWHFMC
760 770 780 790 800
DALIKAIGTE PDSDVLSEIM HSFAKCIEVM GDGCLNNEHF EELGGILKAK
810 820 830 840 850
LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT KVSDILHSIF
860 870 880 890 900
SSYKEKVLPW FEQLLPLIVN LICPHRPWPD RQWGLCIFDD VIEHCSPASF
910 920 930 940 950
KYAEYFLRPM LQYVCDNSPE VRQAAAYGLG VMAQYGGDNY RPFCTEALPL
960 970 980 990 1000
LVRVIQSADS KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL
1010 1020 1030 1040 1050
PLHEDKEEAV QTFNYLCDLI ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA
1060 1070 1080 1090
IKHEDPCAKR LANVVRQVQT SGGLWTECIA QLSPEQQAAI QELLNSA
Length:1,097
Mass (Da):123,630
Last modified:January 23, 2007 - v4
Checksum:i1864AD23513F2DE1
GO
Isoform 2 (identifier: O00410-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:1,037
Mass (Da):116,982
Checksum:i7D9A925F7DBC1DE0
GO
Isoform 3 (identifier: O00410-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPEDQVGKLEATENTISAM

Show »
Length:1,115
Mass (Da):125,545
Checksum:i5296EF23A427A0FB
GO

Sequence cautioni

The sequence CAA70103.1 differs from that shown. Reason: Frameshift at position 18. Curated
Isoform 3 : The sequence CAA70103.1 differs from that shown. Reason: Frameshift at position 18. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti538 – 5381L → R in AAH45640 (PubMed:15489334).Curated
Sequence conflicti826 – 8272ES → GT in AAC51317 (PubMed:9114010).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti286 – 2861L → I.
Corresponds to variant rs1053814 [ dbSNP | Ensembl ].
VAR_012029
Natural varianti525 – 5251E → K.
Corresponds to variant rs632729 [ dbSNP | Ensembl ].
VAR_012030
Natural varianti549 – 5491E → K.
Corresponds to variant rs484770 [ dbSNP | Ensembl ].
VAR_012031
Natural varianti905 – 9051Y → C.
Corresponds to variant rs1804740 [ dbSNP | Ensembl ].
VAR_012032
Natural varianti969 – 9691T → I.
Corresponds to variant rs1804741 [ dbSNP | Ensembl ].
VAR_012033

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060Missing in isoform 2. 1 PublicationVSP_037587Add
BLAST
Alternative sequencei1 – 11M → MPEDQVGKLEATENTISAM in isoform 3. 2 PublicationsVSP_037774

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72761 mRNA. Translation: AAC51317.1.
Y08890 mRNA. Translation: CAA70103.1. Frameshift.
AK302812 mRNA. Translation: BAG64012.1.
AL356580, AL137120 Genomic DNA. Translation: CAI13757.1.
AL137120, AL356580 Genomic DNA. Translation: CAI16520.1.
CH471085 Genomic DNA. Translation: EAX08980.1.
BC001497 mRNA. Translation: AAH01497.1.
BC019309 mRNA. Translation: AAH19309.1.
BC045640 mRNA. Translation: AAH45640.1.
CCDSiCCDS31999.1. [O00410-3]
RefSeqiNP_002262.3. NM_002271.4. [O00410-3]
XP_005254106.1. XM_005254049.1. [O00410-3]
XP_005254109.1. XM_005254052.1. [O00410-3]
XP_005254110.1. XM_005254053.1. [O00410-3]
UniGeneiHs.712598.

Genome annotation databases

EnsembliENST00000261574; ENSP00000261574; ENSG00000065150. [O00410-3]
ENST00000357602; ENSP00000350219; ENSG00000065150. [O00410-1]
ENST00000490680; ENSP00000418393; ENSG00000065150. [O00410-1]
GeneIDi3843.
KEGGihsa:3843.
UCSCiuc001vne.3. human. [O00410-3]
uc001vnf.1. human. [O00410-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72761 mRNA. Translation: AAC51317.1.
Y08890 mRNA. Translation: CAA70103.1. Frameshift.
AK302812 mRNA. Translation: BAG64012.1.
AL356580, AL137120 Genomic DNA. Translation: CAI13757.1.
AL137120, AL356580 Genomic DNA. Translation: CAI16520.1.
CH471085 Genomic DNA. Translation: EAX08980.1.
BC001497 mRNA. Translation: AAH01497.1.
BC019309 mRNA. Translation: AAH19309.1.
BC045640 mRNA. Translation: AAH45640.1.
CCDSiCCDS31999.1. [O00410-3]
RefSeqiNP_002262.3. NM_002271.4. [O00410-3]
XP_005254106.1. XM_005254049.1. [O00410-3]
XP_005254109.1. XM_005254052.1. [O00410-3]
XP_005254110.1. XM_005254053.1. [O00410-3]
UniGeneiHs.712598.

3D structure databases

ProteinModelPortaliO00410.
SMRiO00410. Positions 14-607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110041. 60 interactions.
DIPiDIP-41042N.
IntActiO00410. 26 interactions.
MINTiMINT-132356.
STRINGi9606.ENSP00000261574.

PTM databases

PhosphoSiteiO00410.

Proteomic databases

MaxQBiO00410.
PaxDbiO00410.
PRIDEiO00410.

Protocols and materials databases

DNASUi3843.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261574; ENSP00000261574; ENSG00000065150. [O00410-3]
ENST00000357602; ENSP00000350219; ENSG00000065150. [O00410-1]
ENST00000490680; ENSP00000418393; ENSG00000065150. [O00410-1]
GeneIDi3843.
KEGGihsa:3843.
UCSCiuc001vne.3. human. [O00410-3]
uc001vnf.1. human. [O00410-1]

Organism-specific databases

CTDi3843.
GeneCardsiGC13P098605.
H-InvDBHIX0174410.
HGNCiHGNC:6402. IPO5.
HPAiCAB009110.
HPA040983.
HPA056548.
MIMi602008. gene.
neXtProtiNX_O00410.
PharmGKBiPA30193.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5215.
GeneTreeiENSGT00550000074773.
HOGENOMiHOG000209725.
HOVERGENiHBG006156.
InParanoidiO00410.
OMAiDTNLNNM.
OrthoDBiEOG7Q5HCD.
PhylomeDBiO00410.
TreeFamiTF300344.

Enzyme and pathway databases

ReactomeiREACT_9434. vRNP Assembly.

Miscellaneous databases

ChiTaRSiIPO5. human.
GeneWikiiRANBP5.
GenomeRNAii3843.
NextBioi15125.
PROiO00410.
SOURCEiSearch...

Gene expression databases

BgeeiO00410.
CleanExiHS_IPO5.
ExpressionAtlasiO00410. baseline and differential.
GenevestigatoriO00410.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF02985. HEAT. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of human karyopherin beta3."
    Yaseen N.R., Blobel G.
    Proc. Natl. Acad. Sci. U.S.A. 94:4451-4456(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    Tissue: Bone marrow.
  2. "Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1."
    Deane R., Schaeffer W., Zimmermann H.-P., Mueller L., Goerlich D., Prehn S., Ponstingl H., Bischoff F.R.
    Mol. Cell. Biol. 17:5087-5096(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 3).
    Tissue: Lung and Testis.
  7. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  8. "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells."
    Jaekel S., Goerlich D.
    EMBO J. 17:4491-4502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL RECOGNITION, INTERACTION WITH RPL23A; RPS7 AND RPL5.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Multiple importins function as nuclear transport receptors for the Rev protein of human immunodeficiency virus type 1."
    Arnold M., Nath A., Hauber J., Kehlenbach R.H.
    J. Biol. Chem. 281:20883-20890(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 REV.
  11. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  19. "Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p."
    Kobayashi J., Matsuura Y.
    J. Mol. Biol. 425:1852-1868(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REPEAT STRUCTURE.

Entry informationi

Entry nameiIPO5_HUMAN
AccessioniPrimary (citable) accession number: O00410
Secondary accession number(s): B4DZA0
, O15257, Q5T578, Q86XC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 148 of the entry and version 4 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.