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Protein

Importin subunit alpha-1

Gene

Kpna2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Importin subunit alpha-1
Alternative name(s):
Importin alpha P1
Karyopherin subunit alpha-2
Pendulin
Pore targeting complex 58 kDa subunit
Short name:
PTAC58
RAG cohort protein 1
SRP1-alpha
Gene namesi
Name:Kpna2
Synonyms:Rch1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componentsi: Chromosome 11, Chromosome 17

Organism-specific databases

MGIiMGI:103561. Kpna2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 529528Importin subunit alpha-1PRO_0000120723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei62 – 621PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52293.
PaxDbiP52293.
PRIDEiP52293.

PTM databases

PhosphoSiteiP52293.

Expressioni

Tissue specificityi

Slightly detected in brain but not in cerebellum and skeletal muscle, highly expressed in testis and spleen.

Gene expression databases

BgeeiP52293.
CleanExiMM_KPNA2.
ExpressionAtlasiP52293. baseline and differential.
GenevisibleiP52293. MM.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
P030703EBI-3043908,EBI-617698From a different organism.
Dvir\GJ10455B4LTG56EBI-3043908,EBI-9821342From a different organism.
IfngP015805EBI-3043908,EBI-7892102
S100A2P290342EBI-3043908,EBI-752230From a different organism.
TNPO1Q3SYU73EBI-3043908,EBI-8469003From a different organism.

Protein-protein interaction databases

BioGridi201007. 12 interactions.
IntActiP52293. 10 interactions.
STRINGi10090.ENSMUSP00000137310.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi71 – 733Combined sources
Helixi78 – 858Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 10516Combined sources
Beta strandi106 – 1094Combined sources
Helixi112 – 1176Combined sources
Helixi121 – 1288Combined sources
Helixi131 – 1333Combined sources
Helixi134 – 14815Combined sources
Helixi152 – 1609Combined sources
Helixi163 – 1708Combined sources
Helixi176 – 19116Combined sources
Helixi194 – 2029Combined sources
Helixi206 – 2116Combined sources
Helixi218 – 2203Combined sources
Helixi223 – 23614Combined sources
Helixi246 – 25914Combined sources
Helixi265 – 27814Combined sources
Beta strandi280 – 2823Combined sources
Helixi283 – 2908Combined sources
Turni291 – 2933Combined sources
Helixi295 – 3028Combined sources
Helixi307 – 32014Combined sources
Helixi325 – 3339Combined sources
Helixi336 – 3394Combined sources
Helixi340 – 3434Combined sources
Helixi349 – 36214Combined sources
Helixi367 – 3759Combined sources
Helixi378 – 38710Combined sources
Helixi391 – 40717Combined sources
Helixi410 – 4189Combined sources
Helixi422 – 4276Combined sources
Helixi428 – 4303Combined sources
Helixi434 – 45421Combined sources
Helixi457 – 46610Combined sources
Helixi469 – 4768Combined sources
Beta strandi479 – 4813Combined sources
Helixi482 – 49514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJLX-ray2.80I70-529[»]
1EJYX-ray2.90I70-529[»]
1IALX-ray2.50A44-496[»]
1IQ1X-ray2.80A/B44-54[»]
C70-529[»]
1PJMX-ray2.50B70-529[»]
1PJNX-ray2.50B70-529[»]
1Q1SX-ray2.30C70-529[»]
1Q1TX-ray2.50C70-529[»]
1Y2AX-ray2.20C70-497[»]
2C1MX-ray2.20A75-498[»]
2YNRX-ray2.30A72-496[»]
3BTRX-ray2.60C70-496[»]
3KNDX-ray2.15A70-529[»]
3L3QX-ray2.30A71-497[»]
3OQSX-ray2.00A70-529[»]
3Q5UX-ray2.50A70-529[»]
3RZ9X-ray2.29A70-529[»]
3RZXX-ray2.61A70-529[»]
3TPMX-ray2.10A75-496[»]
3TPOX-ray2.10A1-529[»]
3UKWX-ray2.10B70-529[»]
3UKXX-ray2.20B70-529[»]
3UKYX-ray2.35B70-529[»]
3UKZX-ray2.30B70-529[»]
3UL0X-ray2.00B70-529[»]
3UL1X-ray1.90B70-529[»]
3UVUX-ray2.38A70-529[»]
3VE6X-ray2.83A71-496[»]
3ZINX-ray2.00A72-496[»]
3ZIOX-ray2.10A72-496[»]
3ZIPX-ray2.40A72-497[»]
3ZIQX-ray2.10A72-497[»]
3ZIRX-ray2.30A72-497[»]
4BA3X-ray2.10A70-529[»]
4HTVX-ray3.00A70-528[»]
4MZ5X-ray2.10E70-528[»]
4MZ6X-ray1.88E70-528[»]
4OIHX-ray2.10A70-529[»]
4U54X-ray2.41A74-498[»]
4U58X-ray2.56A72-497[»]
4U5LX-ray2.53A72-497[»]
4U5NX-ray2.31A72-497[»]
4U5OX-ray2.00A72-497[»]
4U5SX-ray2.12A72-497[»]
4U5UX-ray1.96A72-497[»]
4U5VX-ray1.97A72-497[»]
4UAFX-ray1.70B69-529[»]
ProteinModelPortaliP52293.
SMRiP52293. Positions 11-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52293.

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)Add
BLAST
Regioni315 – 40389NLS binding site (minor)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi45 – 5410Nuclear localization signal2 Publications

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.
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.
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.

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.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52293.
KOiK15043.
OMAiNETEKLC.
OrthoDBiEOG7VHSWV.
PhylomeDBiP52293.
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. 6 hits.
PS51214. IBB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P52293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTNENANLP AARLNRFKNK GKDSTEMRRR RIEVNVELRK AKKDEQMLKR
60 70 80 90 100
RNVSSFPDDA TSPLQENRNN QGTVNWSVED IVKGINSNNL ESQLQATQAA
110 120 130 140 150
RKLLSREKQP PIDNIIRAGL IPKFVSFLGK TDCSPIQFES AWALTNIASG
160 170 180 190 200
TSEQTKAVVD GGAIPAFISL LASPHAHISE QAVWALGNIA GDGSAFRDLV
210 220 230 240 250
IKHGAIDPLL ALLAVPDLST LACGYLRNLT WTLSNLCRNK NPAPPLDAVE
260 270 280 290 300
QILPTLVRLL HHNDPEVLAD SCWAISYLTD GPNERIEMVV KKGVVPQLVK
310 320 330 340 350
LLGATELPIV TPALRAIGNI VTGTDEQTQK VIDAGALAVF PSLLTNPKTN
360 370 380 390 400
IQKEATWTMS NITAGRQDQI QQVVNHGLVP FLVGVLSKAD FKTQKEAAWA
410 420 430 440 450
ITNYTSGGTV EQIVYLVHCG IIEPLMNLLS AKDTKIIQVI LDAISNIFQA
460 470 480 490 500
AEKLGETEKL SIMIEECGGL DKIEALQRHE NESVYKASLN LIEKYFSVEE
510 520
EEDQNVVPET TSEGFAFQVQ DGAPGTFNF
Length:529
Mass (Da):57,928
Last modified:November 1, 1997 - v2
Checksum:i19E64AA3E9C3C7B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421P → S in AAA85281 (PubMed:7565597).Curated
Sequence conflicti418 – 4181H → P in AAA85281 (PubMed:7565597).Curated
Sequence conflicti420 – 4201G → R in AAA85281 (PubMed:7565597).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55720 mRNA. Translation: BAA09536.1.
U12270 mRNA. Translation: AAA85281.1.
U34229 mRNA. Translation: AAC52451.1.
BC003274 mRNA. Translation: AAH03274.1.
BC006720 mRNA. Translation: AAH06720.1.
CCDSiCCDS25565.1.
PIRiS57345.
S57873.
S62116.
RefSeqiNP_034785.1. NM_010655.3.
UniGeneiMm.12508.
Mm.391577.
Mm.423000.

Genome annotation databases

EnsembliENSMUST00000018506; ENSMUSP00000018506; ENSMUSG00000018362.
ENSMUST00000086423; ENSMUSP00000137310; ENSMUSG00000066878.
GeneIDi16647.
KEGGimmu:16647.
UCSCiuc007lzz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55720 mRNA. Translation: BAA09536.1.
U12270 mRNA. Translation: AAA85281.1.
U34229 mRNA. Translation: AAC52451.1.
BC003274 mRNA. Translation: AAH03274.1.
BC006720 mRNA. Translation: AAH06720.1.
CCDSiCCDS25565.1.
PIRiS57345.
S57873.
S62116.
RefSeqiNP_034785.1. NM_010655.3.
UniGeneiMm.12508.
Mm.391577.
Mm.423000.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJLX-ray2.80I70-529[»]
1EJYX-ray2.90I70-529[»]
1IALX-ray2.50A44-496[»]
1IQ1X-ray2.80A/B44-54[»]
C70-529[»]
1PJMX-ray2.50B70-529[»]
1PJNX-ray2.50B70-529[»]
1Q1SX-ray2.30C70-529[»]
1Q1TX-ray2.50C70-529[»]
1Y2AX-ray2.20C70-497[»]
2C1MX-ray2.20A75-498[»]
2YNRX-ray2.30A72-496[»]
3BTRX-ray2.60C70-496[»]
3KNDX-ray2.15A70-529[»]
3L3QX-ray2.30A71-497[»]
3OQSX-ray2.00A70-529[»]
3Q5UX-ray2.50A70-529[»]
3RZ9X-ray2.29A70-529[»]
3RZXX-ray2.61A70-529[»]
3TPMX-ray2.10A75-496[»]
3TPOX-ray2.10A1-529[»]
3UKWX-ray2.10B70-529[»]
3UKXX-ray2.20B70-529[»]
3UKYX-ray2.35B70-529[»]
3UKZX-ray2.30B70-529[»]
3UL0X-ray2.00B70-529[»]
3UL1X-ray1.90B70-529[»]
3UVUX-ray2.38A70-529[»]
3VE6X-ray2.83A71-496[»]
3ZINX-ray2.00A72-496[»]
3ZIOX-ray2.10A72-496[»]
3ZIPX-ray2.40A72-497[»]
3ZIQX-ray2.10A72-497[»]
3ZIRX-ray2.30A72-497[»]
4BA3X-ray2.10A70-529[»]
4HTVX-ray3.00A70-528[»]
4MZ5X-ray2.10E70-528[»]
4MZ6X-ray1.88E70-528[»]
4OIHX-ray2.10A70-529[»]
4U54X-ray2.41A74-498[»]
4U58X-ray2.56A72-497[»]
4U5LX-ray2.53A72-497[»]
4U5NX-ray2.31A72-497[»]
4U5OX-ray2.00A72-497[»]
4U5SX-ray2.12A72-497[»]
4U5UX-ray1.96A72-497[»]
4U5VX-ray1.97A72-497[»]
4UAFX-ray1.70B69-529[»]
ProteinModelPortaliP52293.
SMRiP52293. Positions 11-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201007. 12 interactions.
IntActiP52293. 10 interactions.
STRINGi10090.ENSMUSP00000137310.

PTM databases

PhosphoSiteiP52293.

Proteomic databases

MaxQBiP52293.
PaxDbiP52293.
PRIDEiP52293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018506; ENSMUSP00000018506; ENSMUSG00000018362.
ENSMUST00000086423; ENSMUSP00000137310; ENSMUSG00000066878.
GeneIDi16647.
KEGGimmu:16647.
UCSCiuc007lzz.1. mouse.

Organism-specific databases

CTDi3838.
MGIiMGI:103561. Kpna2.

Phylogenomic databases

eggNOGiCOG5064.
HOGENOMiHOG000167616.
HOVERGENiHBG001846.
InParanoidiP52293.
KOiK15043.
OMAiNETEKLC.
OrthoDBiEOG7VHSWV.
PhylomeDBiP52293.
TreeFamiTF101178.

Miscellaneous databases

EvolutionaryTraceiP52293.
NextBioi290325.
PROiP52293.
SOURCEiSearch...

Gene expression databases

BgeeiP52293.
CleanExiMM_KPNA2.
ExpressionAtlasiP52293. baseline and differential.
GenevisibleiP52293. MM.

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. 6 hits.
PS51214. IBB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import."
    Imamoto N., Shimamoto T., Takao T., Tachibana T., Kose S., Matsubae M., Sekimoto T., Shimonishi Y., Yoneda Y.
    EMBO J. 14:3617-3626(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis."
    Kuessel P., Frasch M.
    Mol. Gen. Genet. 248:351-363(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  3. "The nuclear localization signal of lymphoid enhancer factor-1 is recognized by two differentially expressed Srp1-nuclear localization sequence receptor proteins."
    Prieve M.G., Guttridge K.L., Waterman M.L.
    J. Biol. Chem. 271:7654-7658(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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].
  5. "Characterization of the nuclear transport of a novel leucine-rich acidic nuclear protein-like protein."
    Matsubae M., Kurihara T., Tachibana T., Imamoto N., Yoneda Y.
    FEBS Lett. 468:171-175(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANP32E.
  6. "Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha."
    Fontes M.R., Teh T., Kobe B.
    J. Mol. Biol. 297:1183-1194(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 72-497, NUCLEAR LOCALIZATION SIGNAL RECOGNITION.
  7. "Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha."
    Kobe B.
    Nat. Struct. Biol. 6:388-397(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 44-496, NUCLEAR LOCALIZATION SIGNAL, AUTOINHIBITION.
  8. "Biophysical characterization of interactions involving importin-alpha during nuclear import."
    Catimel B., Teh T., Fontes M.R., Jennings I.G., Jans D.A., Howlett G.J., Nice E.C., Kobe B.
    J. Biol. Chem. 276:34189-34198(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 47-54, AUTOINHIBITION.
  9. "Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling."
    Matsuura Y., Stewart M.
    EMBO J. 24:3681-3689(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 75-498 IN COMPLEX WITH NUP50.
  10. "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: INTERACTS WITH SNAI1.

Entry informationi

Entry nameiIMA1_MOUSE
AccessioniPrimary (citable) accession number: P52293
Secondary accession number(s): Q64292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.