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Protein

Platelet-activating factor acetylhydrolase IB subunit alpha

Gene

Pafah1b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position.UniRule annotation13 Publications

GO - Molecular functioni

  • dynein binding Source: MGI
  • microtubule binding Source: MGI
  • phosphoprotein binding Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • acrosome assembly Source: MGI
  • actin cytoskeleton organization Source: MGI
  • adult locomotory behavior Source: MGI
  • ameboidal-type cell migration Source: MGI
  • auditory receptor cell development Source: CACAO
  • brain morphogenesis Source: MGI
  • cell migration Source: MGI
  • cerebral cortex development Source: MGI
  • cerebral cortex neuron differentiation Source: Ensembl
  • chemical synaptic transmission Source: MGI
  • cochlea development Source: CACAO
  • corpus callosum morphogenesis Source: MGI
  • cortical microtubule organization Source: CACAO
  • establishment of centrosome localization Source: Ensembl
  • establishment of mitotic spindle orientation Source: MGI
  • establishment of planar polarity of embryonic epithelium Source: CACAO
  • hippocampus development Source: MGI
  • layer formation in cerebral cortex Source: MGI
  • learning or memory Source: MGI
  • lipid catabolic process Source: UniProtKB-KW
  • maintenance of centrosome location Source: MGI
  • microtubule-based process Source: MGI
  • microtubule cytoskeleton organization Source: MGI
  • microtubule cytoskeleton organization involved in establishment of planar polarity Source: CACAO
  • microtubule organizing center organization Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of JNK cascade Source: MGI
  • negative regulation of neuron projection development Source: Ensembl
  • neuroblast proliferation Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • neuron migration Source: MGI
  • nuclear envelope disassembly Source: MGI
  • nuclear migration Source: GO_Central
  • osteoclast development Source: MGI
  • positive regulation of axon extension Source: Ensembl
  • positive regulation of cellular component organization Source: CACAO
  • positive regulation of cytokine-mediated signaling pathway Source: MGI
  • positive regulation of dendritic spine morphogenesis Source: CACAO
  • positive regulation of embryonic development Source: CACAO
  • positive regulation of mitotic cell cycle Source: Ensembl
  • protein secretion Source: MGI
  • regulation of GTPase activity Source: MGI
  • regulation of microtubule cytoskeleton organization Source: CACAO
  • regulation of microtubule motor activity Source: GO_Central
  • retrograde axonal transport Source: MGI
  • stem cell division Source: Ensembl
  • transmission of nerve impulse Source: MGI
  • vesicle transport along microtubule Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Lipid degradation, Lipid metabolism, Mitosis, Neurogenesis, Transport

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet-activating factor acetylhydrolase IB subunit alphaUniRule annotation
Alternative name(s):
Lissencephaly-1 proteinUniRule annotation
Short name:
LIS-1UniRule annotation
PAF acetylhydrolase 45 kDa subunitUniRule annotation
Short name:
PAF-AH 45 kDa subunitUniRule annotation
PAF-AH alphaUniRule annotation
Short name:
PAFAH alphaUniRule annotation
Gene namesi
Name:Pafah1b1
Synonyms:Lis-1, Lis1, Pafaha
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:109520. Pafah1b1.

Subcellular locationi

GO - Cellular componenti

  • astral microtubule Source: MGI
  • axon cytoplasm Source: GOC
  • cell cortex Source: MGI
  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
  • extracellular exosome Source: MGI
  • growth cone Source: Ensembl
  • kinesin complex Source: Ensembl
  • kinetochore Source: MGI
  • microtubule Source: GO_Central
  • microtubule associated complex Source: MGI
  • microtubule cytoskeleton Source: MGI
  • motile cilium Source: MGI
  • neuronal cell body Source: Ensembl
  • nuclear envelope Source: MGI
  • nuclear membrane Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: MGI
  • stereocilium Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15I → R: Impairs self-association and reduces protein stability. 1 Publication1
Mutagenesisi19L → R: Impairs self-association, reduces protein stability and promotes localization to actin fibers. 1 Publication1
Mutagenesisi31F → S: Abrogates interaction with NDLE1, NUDC, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability. 1 Publication1
Mutagenesisi149H → R: Abrogates self-association and interaction with DAB1, dynein, NDEL1, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability. 4 Publications1
Mutagenesisi152S → W: Abrogates interaction with NDEL1. 1 Publication1
Mutagenesisi162G → S: Abrogates interaction with PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability. 1 Publication1
Mutagenesisi169S → P: Abrogates interaction with NDEL1, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability. 2 Publications1
Mutagenesisi238R → A: Abrogates interaction with PAFAH1B2. 1 Publication1
Mutagenesisi317D → H: Abrogates interaction with NDEL1, PAFAH1B3 and RSN. Also impairs localization to centrosomes and microtubule plus ends. Reduces protein stability. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000510631 – 410Platelet-activating factor acetylhydrolase IB subunit alphaAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysineBy similarity1
Modified residuei109PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP63005.
PaxDbiP63005.
PeptideAtlasiP63005.
PRIDEiP63005.

2D gel databases

REPRODUCTION-2DPAGEP63005.

PTM databases

iPTMnetiP63005.
PhosphoSitePlusiP63005.

Expressioni

Tissue specificityi

Highly expressed in brain, particularly the hippocampus and the olfactory bulb. Also highly expressed in testis, including all seminiferous tubule cell types, all types of spermatogenic and Sertoli cells, and meiotically dividing and elongating spermatids. Expressed at lower levels in heart, kidney, large intestine, liver, lung, ovary, small intestine and spleen.3 Publications

Developmental stagei

Embryonic expression begins prior to the blastocyst stage, when maternally expressed protein is depleted. By E10.5, expression is abundant in the developing central and peripheral nervous systems. Major sites of expression include the neuroepithelium of the fore-, mid-, and hindbrain, the spinal cord, the dorsal root and the cranial ganglia. By E13.5, highly expressed in neuroblasts as well as postmitotic neurons of the cortical plate. After completion of neuronal migration expression remains high in the cortex. Also expressed in the testis from P8.8 Publications

Gene expression databases

BgeeiENSMUSG00000020745.
ExpressionAtlasiP63005. baseline and differential.
GenevisibleiP63005. MM.

Interactioni

Subunit structurei

Interacts with DISC1, and this interaction is enhanced by NDEL1 (By similarity). Component of cytosolic PAF-AH IB, which is composed of PAFAH1B1 (alpha), PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Trimer formation is not essential for the catalytic activity of the enzyme which is contributed solely by the PAFAH1B2 (beta) and PAFAH1B3 (gamma) subunits. Can self-associate. Interacts with DCX, dynein, dynactin, IQGAP1, KATNB1, NDE1, NDEL1, NUDC, and RSN. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling. Interacts with ASUN.By similarity19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ndel1Q9ERR17EBI-917499,EBI-646668
Pafah1b3Q612052EBI-917499,EBI-1007637

GO - Molecular functioni

  • dynein binding Source: MGI
  • microtubule binding Source: MGI
  • phosphoprotein binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi202013. 46 interactors.
DIPiDIP-29555N.
IntActiP63005. 41 interactors.
MINTiMINT-267632.
STRINGi10090.ENSMUSP00000021091.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 21Combined sources17
Helixi25 – 34Combined sources10
Helixi41 – 47Combined sources7
Helixi50 – 55Combined sources6
Helixi58 – 74Combined sources17
Beta strandi103 – 105Combined sources3
Beta strandi111 – 116Combined sources6
Beta strandi118 – 130Combined sources13
Beta strandi132 – 136Combined sources5
Turni137 – 139Combined sources3
Beta strandi144 – 146Combined sources3
Beta strandi153 – 158Combined sources6
Beta strandi162 – 169Combined sources8
Beta strandi176 – 178Combined sources3
Beta strandi184 – 186Combined sources3
Beta strandi195 – 198Combined sources4
Beta strandi202 – 211Combined sources10
Beta strandi214 – 220Combined sources7
Turni221 – 223Combined sources3
Beta strandi226 – 231Combined sources6
Beta strandi237 – 242Combined sources6
Beta strandi246 – 253Combined sources8
Beta strandi258 – 262Combined sources5
Turni263 – 265Combined sources3
Beta strandi268 – 272Combined sources5
Beta strandi279 – 284Combined sources6
Helixi289 – 295Combined sources7
Beta strandi310 – 315Combined sources6
Beta strandi318 – 324Combined sources7
Turni325 – 328Combined sources4
Beta strandi329 – 335Combined sources7
Beta strandi341 – 346Combined sources6
Beta strandi348 – 351Combined sources4
Beta strandi353 – 357Combined sources5
Turni358 – 360Combined sources3
Beta strandi361 – 365Combined sources5
Beta strandi374 – 377Combined sources4
Beta strandi383 – 388Combined sources6
Beta strandi390 – 393Combined sources4
Beta strandi395 – 399Combined sources5
Beta strandi402 – 407Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UUJX-ray1.75A/B/C/D1-86[»]
1VYHX-ray3.40C/D/G/H/K/L/O/P/S/T1-410[»]
ProteinModelPortaliP63005.
SMRiP63005.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63005.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 39LisHUniRule annotationAdd BLAST33
Repeati106 – 147WD 1Add BLAST42
Repeati148 – 187WD 2Add BLAST40
Repeati190 – 229WD 3Add BLAST40
Repeati232 – 271WD 4Add BLAST40
Repeati274 – 333WD 5Add BLAST60
Repeati336 – 377WD 6Add BLAST42
Repeati378 – 410WD 7Add BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 102Interaction with NDEL1Add BLAST102
Regioni1 – 66Interaction with NDE1UniRule annotationAdd BLAST66
Regioni1 – 38Required for self-association and interaction with PAFAH1B2 and PAFAH1B3Add BLAST38
Regioni83 – 410Interaction with dynein and dynactinUniRule annotationAdd BLAST328
Regioni367 – 409Interaction with DCXUniRule annotationAdd BLAST43
Regioni388 – 410Interaction with NDEL1Add BLAST23

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili56 – 82UniRule annotationAdd BLAST27

Domaini

Dimerization mediated by the LisH domain may be required to activate dynein.UniRule annotation2 Publications

Sequence similaritiesi

Belongs to the WD repeat LIS1/nudF family.UniRule annotation
Contains 1 LisH domain.UniRule annotation
Contains 7 WD repeats.UniRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0295. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000184015.
HOVERGENiHBG006271.
InParanoidiP63005.
KOiK16794.
OMAiNWVRALV.
OrthoDBiEOG091G07Q1.
PhylomeDBiP63005.
TreeFamiTF105741.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03141. lis1. 1 hit.
InterProiIPR017252. Dynein_regulator_LIS1.
IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PIRSFiPIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P63005-1) [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
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDMN EELDKKYAGL
60 70 80 90 100
LEKKWTSVIR LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE
110 120 130 140 150
KYALSGHRSP VTRVIFHPVF SVMVSASEDA TIKVWDYETG DFERTLKGHT
160 170 180 190 200
DSVQDISFDH SGKLLASCSA DMTIKLWDFQ GFECIRTMHG HDHNVSSVAI
210 220 230 240 250
MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV RPNQDGTLIA
260 270 280 290 300
SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
310 320 330 340 350
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG
360 370 380 390 400
KFILSCADDK TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV
410
DQTVKVWECR
Length:410
Mass (Da):46,670
Last modified:January 23, 2007 - v2
Checksum:i4DBF6A24A6B131CD
GO
Isoform 2 (identifier: P63005-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     387-410: DFHKTAPYVVTGSVDQTVKVWECR → GMYTL

Show »
Length:391
Mass (Da):44,488
Checksum:iA8662C60C66684AD
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_006778387 – 410DFHKT…VWECR → GMYTL in isoform 2. 1 PublicationAdd BLAST24

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95116 mRNA. Translation: AAC04610.1.
U95120, U95119 Genomic DNA. Translation: AAC63099.1.
U95120, U95119 Genomic DNA. Translation: AAC63098.1.
L25109 mRNA. Translation: AAD23059.1.
AY189217 mRNA. Translation: AAO41716.1.
AY189218 mRNA. Translation: AAO41717.1.
BC014831 mRNA. Translation: AAH14831.1.
BC026141 mRNA. Translation: AAH26141.1.
CCDSiCCDS25035.1.
RefSeqiNP_038653.1. NM_013625.4. [P63005-1]
UniGeneiMm.397111.

Genome annotation databases

EnsembliENSMUST00000021091; ENSMUSP00000021091; ENSMUSG00000020745. [P63005-1]
ENSMUST00000102520; ENSMUSP00000099578; ENSMUSG00000020745. [P63005-1]
GeneIDi18472.
KEGGimmu:18472.
UCSCiuc007kce.2. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95116 mRNA. Translation: AAC04610.1.
U95120, U95119 Genomic DNA. Translation: AAC63099.1.
U95120, U95119 Genomic DNA. Translation: AAC63098.1.
L25109 mRNA. Translation: AAD23059.1.
AY189217 mRNA. Translation: AAO41716.1.
AY189218 mRNA. Translation: AAO41717.1.
BC014831 mRNA. Translation: AAH14831.1.
BC026141 mRNA. Translation: AAH26141.1.
CCDSiCCDS25035.1.
RefSeqiNP_038653.1. NM_013625.4. [P63005-1]
UniGeneiMm.397111.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UUJX-ray1.75A/B/C/D1-86[»]
1VYHX-ray3.40C/D/G/H/K/L/O/P/S/T1-410[»]
ProteinModelPortaliP63005.
SMRiP63005.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202013. 46 interactors.
DIPiDIP-29555N.
IntActiP63005. 41 interactors.
MINTiMINT-267632.
STRINGi10090.ENSMUSP00000021091.

PTM databases

iPTMnetiP63005.
PhosphoSitePlusiP63005.

2D gel databases

REPRODUCTION-2DPAGEP63005.

Proteomic databases

EPDiP63005.
PaxDbiP63005.
PeptideAtlasiP63005.
PRIDEiP63005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021091; ENSMUSP00000021091; ENSMUSG00000020745. [P63005-1]
ENSMUST00000102520; ENSMUSP00000099578; ENSMUSG00000020745. [P63005-1]
GeneIDi18472.
KEGGimmu:18472.
UCSCiuc007kce.2. mouse.

Organism-specific databases

CTDi5048.
MGIiMGI:109520. Pafah1b1.

Phylogenomic databases

eggNOGiKOG0295. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000184015.
HOVERGENiHBG006271.
InParanoidiP63005.
KOiK16794.
OMAiNWVRALV.
OrthoDBiEOG091G07Q1.
PhylomeDBiP63005.
TreeFamiTF105741.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiPafah1b1. mouse.
EvolutionaryTraceiP63005.
PROiP63005.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020745.
ExpressionAtlasiP63005. baseline and differential.
GenevisibleiP63005. MM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03141. lis1. 1 hit.
InterProiIPR017252. Dynein_regulator_LIS1.
IPR020472. G-protein_beta_WD-40_rep.
IPR006594. LisH.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF08513. LisH. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PIRSFiPIRSF037647. Dynein_regulator_Lis1. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00667. LisH. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50896. LISH. 1 hit.
PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIS1_MOUSE
AccessioniPrimary (citable) accession number: P63005
Secondary accession number(s): O35592
, P43035, P81692, Q9R2A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 143 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, Direct protein sequencing, 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

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 one 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.