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Protein

Platelet-activating factor acetylhydrolase IB subunit alpha

Gene

PAFAH1B1

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

Functioni

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. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet-activating factor (PAF) by removing the acetyl group at the SN-2 position (By similarity). 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. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing.By similarity1 Publication

GO - Molecular functioni

  • dynactin binding Source: BHF-UCL
  • dynein binding Source: UniProtKB
  • heparin binding Source: BHF-UCL
  • microtubule binding Source: BHF-UCL
  • phospholipase A2 activity Source: Reactome
  • phospholipase binding Source: BHF-UCL
  • phosphoprotein binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • acrosome assembly Source: BHF-UCL
  • actin cytoskeleton organization Source: BHF-UCL
  • adult locomotory behavior Source: BHF-UCL
  • ameboidal-type cell migration Source: Ensembl
  • auditory receptor cell development Source: Ensembl
  • brain morphogenesis Source: BHF-UCL
  • cerebral cortex development Source: BHF-UCL
  • cerebral cortex neuron differentiation Source: Ensembl
  • chemical synaptic transmission Source: BHF-UCL
  • cochlea development Source: Ensembl
  • corpus callosum morphogenesis Source: BHF-UCL
  • cortical microtubule organization Source: Ensembl
  • establishment of centrosome localization Source: Ensembl
  • establishment of mitotic spindle orientation Source: UniProtKB
  • establishment of planar polarity of embryonic epithelium Source: Ensembl
  • G2/M transition of mitotic cell cycle Source: Reactome
  • germ cell development Source: GO_Central
  • hippocampus development Source: BHF-UCL
  • layer formation in cerebral cortex Source: BHF-UCL
  • learning or memory Source: BHF-UCL
  • lipid catabolic process Source: UniProtKB-KW
  • maintenance of centrosome location Source: Ensembl
  • microtubule-based process Source: UniProtKB
  • microtubule cytoskeleton organization Source: BHF-UCL
  • microtubule cytoskeleton organization involved in establishment of planar polarity Source: Ensembl
  • microtubule organizing center organization Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of JNK cascade Source: Ensembl
  • negative regulation of neuron projection development Source: Ensembl
  • neuroblast proliferation Source: BHF-UCL
  • neuromuscular process controlling balance Source: BHF-UCL
  • neuron migration Source: UniProtKB
  • nuclear envelope disassembly Source: Ensembl
  • nuclear migration Source: GO_Central
  • osteoclast development Source: Ensembl
  • platelet activating factor metabolic process Source: BHF-UCL
  • positive regulation of axon extension Source: Ensembl
  • positive regulation of cytokine-mediated signaling pathway Source: Ensembl
  • positive regulation of dendritic spine morphogenesis Source: Ensembl
  • positive regulation of embryonic development Source: Ensembl
  • positive regulation of mitotic cell cycle Source: Ensembl
  • protein secretion Source: Ensembl
  • regulation of GTPase activity Source: Ensembl
  • regulation of microtubule cytoskeleton organization Source: Ensembl
  • regulation of microtubule motor activity Source: GO_Central
  • retrograde axonal transport Source: BHF-UCL
  • sister chromatid cohesion Source: Reactome
  • stem cell division Source: Ensembl
  • transmission of nerve impulse Source: BHF-UCL
  • vesicle transport along microtubule Source: BHF-UCL
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

BioCyciZFISH:ENSG00000007168-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8854518. AURKA Activation by TPX2.
SignaLinkiP43034.

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:PAFAH1B1UniRule annotation
Synonyms:LIS1UniRule annotation, MDCR, MDS, PAFAHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:8574. PAFAH1B1.

Subcellular locationi

  • Cytoplasmcytoskeleton
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
  • Cytoplasmcytoskeletonspindle UniRule annotation
  • Nucleus membrane UniRule annotation

  • Note: Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes (By similarity). Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

Lissencephaly 1 (LIS1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA classical lissencephaly. It is characterized by agyria or pachygyria and disorganization of the clear neuronal lamination of normal six-layered cortex. The cortex is abnormally thick and poorly organized with 4 primitive layers. Associated with enlarged and dysmorphic ventricles and often hypoplasia of the corpus callosum.
See also OMIM:607432
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01539831F → S in LIS1. 1 PublicationCorresponds to variant rs121434486dbSNPEnsembl.1
Natural variantiVAR_007724149H → R in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 3 PublicationsCorresponds to variant rs121434482dbSNPEnsembl.1
Natural variantiVAR_015399162G → S in LIS1. 1 PublicationCorresponds to variant rs28936410dbSNPEnsembl.1
Natural variantiVAR_037301277H → P in LIS1. 1 PublicationCorresponds to variant rs121434490dbSNPEnsembl.1
Natural variantiVAR_015400317D → H in LIS1; reduces neuronal migration in vitro. 2 PublicationsCorresponds to variant rs28936689dbSNPEnsembl.1
Subcortical band heterotopia (SBH)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSBH is a mild brain malformation of the lissencephaly spectrum. It is characterized by bilateral and symmetric plates or bands of gray matter found in the central white matter between the cortex and cerebral ventricles, cerebral convolutions usually appearing normal.
See also OMIM:607432
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010203169S → P in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 3 PublicationsCorresponds to variant rs121434484dbSNPEnsembl.1
Natural variantiVAR_037300241R → P in SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells. 1 PublicationCorresponds to variant rs28936411dbSNPEnsembl.1
Miller-Dieker lissencephaly syndrome (MDLS)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA contiguous gene deletion syndrome of chromosome 17p13.3, characterized by classical lissencephaly and distinct facial features. Additional congenital malformations can be part of the condition.
See also OMIM:247200

Keywords - Diseasei

Disease mutation, Lissencephaly

Organism-specific databases

DisGeNETi5048.
MalaCardsiPAFAH1B1.
MIMi247200. phenotype.
607432. phenotype.
OpenTargetsiENSG00000007168.
Orphaneti217385. 17p13.3 microduplication syndrome.
95232. Lissencephaly due to LIS1 mutation.
531. Miller-Dieker syndrome.
99796. Subcortical band heterotopia.
PharmGKBiPA32905.

Polymorphism and mutation databases

BioMutaiPAFAH1B1.
DMDMi1170794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000510611 – 410Platelet-activating factor acetylhydrolase IB subunit alphaAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei53N6-acetyllysineCombined sources1
Modified residuei109PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP43034.
MaxQBiP43034.
PaxDbiP43034.
PeptideAtlasiP43034.
PRIDEiP43034.

PTM databases

iPTMnetiP43034.
PhosphoSitePlusiP43034.

Expressioni

Tissue specificityi

Fairly ubiquitous expression in both the frontal and occipital areas of the brain.

Gene expression databases

BgeeiENSG00000007168.
CleanExiHS_PAFAH1B1.
ExpressionAtlasiP43034. baseline and differential.
GenevisibleiP43034. HS.

Organism-specific databases

HPAiCAB004489.
HPA020036.

Interactioni

Subunit structurei

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. Interacts with IQGAP1, KATNB1 and NUDC. Interacts with DAB1 when DAB1 is phosphorylated in response to RELN/reelin signaling (By similarity). Can self-associate. Interacts with DCX, dynein, dynactin, NDE1, NDEL1 and RSN. Interacts with DISC1, and this interaction is enhanced by NDEL1. Interacts with ASUN.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nde1Q9CZA66EBI-720620,EBI-309934From a different organism.
NDEL1Q9GZM83EBI-720620,EBI-928842

GO - Molecular functioni

  • dynactin binding Source: BHF-UCL
  • dynein binding Source: UniProtKB
  • microtubule binding Source: BHF-UCL
  • phospholipase binding Source: BHF-UCL
  • phosphoprotein binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi111085. 66 interactors.
DIPiDIP-35691N.
IntActiP43034. 28 interactors.
MINTiMINT-5004233.
STRINGi9606.ENSP00000380378.

Structurei

3D structure databases

ProteinModelPortaliP43034.
SMRiP43034.
ModBaseiSearch...
MobiDBiSearch...

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 NDEL1UniRule annotationAdd BLAST102
Regioni1 – 66Interaction with NDE1UniRule annotationAdd BLAST66
Regioni1 – 38Required for self-association and interaction with PAFAH1B2 and PAFAH1B3UniRule annotationAdd BLAST38
Regioni83 – 410Interaction with dynein and dynactinAdd BLAST328
Regioni367 – 409Interaction with DCX1 PublicationAdd BLAST43
Regioni388 – 410Interaction with NDEL1UniRule annotationAdd 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 annotation

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.
InParanoidiP43034.
KOiK16794.
OMAiNWVRALV.
OrthoDBiEOG091G07Q1.
PhylomeDBiP43034.
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: P43034-1) [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 FKKEAELDVN 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):46,638
Last modified:January 23, 2007 - v2
Checksum:i3AB68D2641BA31C9
GO
Isoform 2 (identifier: P43034-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     12-64: Missing.
     134-170: Missing.
     237-237: V → I
     238-410: Missing.

Note: No experimental confirmation available.
Show »
Length:147
Mass (Da):16,869
Checksum:iB594509D159C7657
GO

Sequence cautioni

The sequence AAA02882 differs from that shown. Chimeric cDNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21S → P in AAL34972 (Ref. 3) Curated1
Sequence conflicti21S → P in AAL34973 (Ref. 3) Curated1
Sequence conflicti93E → G in AAL34973 (Ref. 3) Curated1
Sequence conflicti177W → R in AAL34973 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01539831F → S in LIS1. 1 PublicationCorresponds to variant rs121434486dbSNPEnsembl.1
Natural variantiVAR_007724149H → R in LIS1; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 3 PublicationsCorresponds to variant rs121434482dbSNPEnsembl.1
Natural variantiVAR_015399162G → S in LIS1. 1 PublicationCorresponds to variant rs28936410dbSNPEnsembl.1
Natural variantiVAR_010203169S → P in SBH; abrogates interaction with NDE1 and reduces neuronal migration in vitro. 3 PublicationsCorresponds to variant rs121434484dbSNPEnsembl.1
Natural variantiVAR_037300241R → P in SBH; somatic mosaicism in 18% of lymphocytes and 21% of hair root cells. 1 PublicationCorresponds to variant rs28936411dbSNPEnsembl.1
Natural variantiVAR_037301277H → P in LIS1. 1 PublicationCorresponds to variant rs121434490dbSNPEnsembl.1
Natural variantiVAR_015400317D → H in LIS1; reduces neuronal migration in vitro. 2 PublicationsCorresponds to variant rs28936689dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01937612 – 64Missing in isoform 2. 1 PublicationAdd BLAST53
Alternative sequenceiVSP_019377134 – 170Missing in isoform 2. 1 PublicationAdd BLAST37
Alternative sequenceiVSP_019378237V → I in isoform 2. 1 Publication1
Alternative sequenceiVSP_019379238 – 410Missing in isoform 2. 1 PublicationAdd BLAST173

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13385 mRNA. Translation: AAA02880.1.
L13386 mRNA. Translation: AAA02881.1.
L13387 mRNA. Translation: AAA02882.1. Sequence problems.
U72342
, U72334, U72335, U72336, U72337, U72338, U72339, U72340, U72341 Genomic DNA. Translation: AAC51111.1.
AF208837 mRNA. Translation: AAL34972.1.
AF208838 mRNA. Translation: AAL34973.1.
AF400434 mRNA. Translation: AAK92483.1.
AK313078 mRNA. Translation: BAG35904.1.
BX538346 mRNA. Translation: CAD98141.1.
CH471108 Genomic DNA. Translation: EAW90536.1.
BC064638 mRNA. Translation: AAH64638.1.
CCDSiCCDS32528.1. [P43034-1]
PIRiS36113.
RefSeqiNP_000421.1. NM_000430.3. [P43034-1]
XP_016880188.1. XM_017024699.1. [P43034-1]
XP_016880189.1. XM_017024700.1. [P43034-1]
XP_016880190.1. XM_017024701.1. [P43034-1]
UniGeneiHs.77318.

Genome annotation databases

EnsembliENST00000397195; ENSP00000380378; ENSG00000007168. [P43034-1]
GeneIDi5048.
KEGGihsa:5048.
UCSCiuc002fuw.5. human. [P43034-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13385 mRNA. Translation: AAA02880.1.
L13386 mRNA. Translation: AAA02881.1.
L13387 mRNA. Translation: AAA02882.1. Sequence problems.
U72342
, U72334, U72335, U72336, U72337, U72338, U72339, U72340, U72341 Genomic DNA. Translation: AAC51111.1.
AF208837 mRNA. Translation: AAL34972.1.
AF208838 mRNA. Translation: AAL34973.1.
AF400434 mRNA. Translation: AAK92483.1.
AK313078 mRNA. Translation: BAG35904.1.
BX538346 mRNA. Translation: CAD98141.1.
CH471108 Genomic DNA. Translation: EAW90536.1.
BC064638 mRNA. Translation: AAH64638.1.
CCDSiCCDS32528.1. [P43034-1]
PIRiS36113.
RefSeqiNP_000421.1. NM_000430.3. [P43034-1]
XP_016880188.1. XM_017024699.1. [P43034-1]
XP_016880189.1. XM_017024700.1. [P43034-1]
XP_016880190.1. XM_017024701.1. [P43034-1]
UniGeneiHs.77318.

3D structure databases

ProteinModelPortaliP43034.
SMRiP43034.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111085. 66 interactors.
DIPiDIP-35691N.
IntActiP43034. 28 interactors.
MINTiMINT-5004233.
STRINGi9606.ENSP00000380378.

PTM databases

iPTMnetiP43034.
PhosphoSitePlusiP43034.

Polymorphism and mutation databases

BioMutaiPAFAH1B1.
DMDMi1170794.

Proteomic databases

EPDiP43034.
MaxQBiP43034.
PaxDbiP43034.
PeptideAtlasiP43034.
PRIDEiP43034.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397195; ENSP00000380378; ENSG00000007168. [P43034-1]
GeneIDi5048.
KEGGihsa:5048.
UCSCiuc002fuw.5. human. [P43034-1]

Organism-specific databases

CTDi5048.
DisGeNETi5048.
GeneCardsiPAFAH1B1.
GeneReviewsiPAFAH1B1.
HGNCiHGNC:8574. PAFAH1B1.
HPAiCAB004489.
HPA020036.
MalaCardsiPAFAH1B1.
MIMi247200. phenotype.
601545. gene.
607432. phenotype.
neXtProtiNX_P43034.
OpenTargetsiENSG00000007168.
Orphaneti217385. 17p13.3 microduplication syndrome.
95232. Lissencephaly due to LIS1 mutation.
531. Miller-Dieker syndrome.
99796. Subcortical band heterotopia.
PharmGKBiPA32905.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0295. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000184015.
HOVERGENiHBG006271.
InParanoidiP43034.
KOiK16794.
OMAiNWVRALV.
OrthoDBiEOG091G07Q1.
PhylomeDBiP43034.
TreeFamiTF105741.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000007168-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8854518. AURKA Activation by TPX2.
SignaLinkiP43034.

Miscellaneous databases

ChiTaRSiPAFAH1B1. human.
GeneWikiiPAFAH1B1.
GenomeRNAii5048.
PROiP43034.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000007168.
CleanExiHS_PAFAH1B1.
ExpressionAtlasiP43034. baseline and differential.
GenevisibleiP43034. HS.

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.
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Entry informationi

Entry nameiLIS1_HUMAN
AccessioniPrimary (citable) accession number: P43034
Secondary accession number(s): B2R7Q7, Q8WZ88, Q8WZ89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 176 of the entry and version 2 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, 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. 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.