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Platelet-activating factor acetylhydrolase IB subunit alpha (Lissencephaly-1 protein) (LIS-1) (PAF acetylhydrolase 45 kDa subunit) (PAF-AH 45 kDa subunit) (PAF-AH alpha) (PAFAH alpha)

 LIS1_HUMAN              Reviewed;         410 AA.
P43034; B2R7Q7; Q8WZ88; Q8WZ89;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 186.
RecName: Full=Platelet-activating factor acetylhydrolase IB subunit alpha {ECO:0000255|HAMAP-Rule:MF_03141};
AltName: Full=Lissencephaly-1 protein {ECO:0000255|HAMAP-Rule:MF_03141};
Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
AltName: Full=PAF acetylhydrolase 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141};
Short=PAF-AH 45 kDa subunit {ECO:0000255|HAMAP-Rule:MF_03141};
AltName: Full=PAF-AH alpha {ECO:0000255|HAMAP-Rule:MF_03141};
Short=PAFAH alpha {ECO:0000255|HAMAP-Rule:MF_03141};
Name=PAFAH1B1 {ECO:0000255|HAMAP-Rule:MF_03141};
Synonyms=LIS1 {ECO:0000255|HAMAP-Rule:MF_03141}, MDCR, MDS, PAFAHA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Kidney;
PubMed=8355785; DOI=10.1038/364717a0;
Reiner O., Carrozzo R., Shen Y., Wehnert M., Faustinella F.,
Dobyns W.B., Caskey C.T., Ledbetter D.H.;
"Isolation of a Miller-Dieker lissencephaly gene containing G protein
beta-subunit-like repeats.";
Nature 364:717-721(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LIS1 ARG-149.
PubMed=9063735; DOI=10.1093/hmg/6.2.157;
Lo Nigro C., Chong S.S., Smith A.C.M., Dobyns W.B., Carrozzo R.,
Ledbetter D.H.;
"Point mutations and an intragenic deletion in LIS1, the lissencephaly
causative gene in isolated lissencephaly sequence and Miller-Dieker
syndrome.";
Hum. Mol. Genet. 6:157-164(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Zhao M.J., Xia S.L., Li T.P.;
"High expression of the lissencephaly gene in hepatocarcinoma
patients.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Feng Z., Zhang B., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH DCX.
PubMed=11001923; DOI=10.1093/oxfordjournals.hmg.a018911;
Caspi M., Atlas R., Kantor A., Sapir T., Reiner O.;
"Interaction between LIS1 and doublecortin, two lissencephaly gene
products.";
Hum. Mol. Genet. 9:2205-2213(2000).
[10]
INTERACTION WITH NDE1, AND CHARACTERIZATION OF VARIANTS LIS1 ARG-149
AND SBH PRO-169.
PubMed=11163258; DOI=10.1016/S0896-6273(00)00145-8;
Feng Y., Olson E.C., Stukenberg P.T., Flanagan L.A., Kirschner M.W.,
Walsh C.A.;
"LIS1 regulates CNS lamination by interacting with mNudE, a central
component of the centrosome.";
Neuron 28:665-679(2000).
[11]
SELF-ASSOCIATION, INTERACTION WITH RSN; DYNEIN AND DYNACTIN, AND
SUBCELLULAR LOCATION.
PubMed=11889140; DOI=10.1083/jcb.200109046;
Tai C.-Y., Dujardin D.L., Faulkner N.E., Vallee R.B.;
"Role of dynein, dynactin, and CLIP-170 interactions in LIS1
kinetochore function.";
J. Cell Biol. 156:959-968(2002).
[12]
SUBCELLULAR LOCATION.
PubMed=11940666; DOI=10.1128/MCB.22.9.3089-3102.2002;
Coquelle F.M., Caspi M., Cordelieres F.P., Dompierre J.P.,
Dujardin D.L., Koifman C., Martin P., Hoogenraad C.C., Akhmanova A.,
Galjart N., De Mey J.R., Reiner O.;
"LIS1, CLIP-170's key to the dynein/dynactin pathway.";
Mol. Cell. Biol. 22:3089-3102(2002).
[13]
INTERACTION WITH NDEL1.
PubMed=12556484; DOI=10.1128/MCB.23.4.1239-1250.2003;
Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X.;
"Human Nudel and NudE as regulators of cytoplasmic dynein in poleward
protein transport along the mitotic spindle.";
Mol. Cell. Biol. 23:1239-1250(2003).
[14]
INTERACTION WITH NDEL1.
PubMed=14970193; DOI=10.1083/jcb.200308058;
Liang Y., Yu W., Li Y., Yang Z., Yan X., Huang Q., Zhu X.;
"Nudel functions in membrane traffic mainly through association with
Lis1 and cytoplasmic dynein.";
J. Cell Biol. 164:557-566(2004).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS LIS1
ARG-149; SBH PRO-169 AND LIS1 HIS-317.
PubMed=15173193; DOI=10.1083/jcb.200309025;
Tanaka T., Serneo F.F., Higgins C., Gambello M.J., Wynshaw-Boris A.,
Gleeson J.G.;
"Lis1 and doublecortin function with dynein to mediate coupling of the
nucleus to the centrosome in neuronal migration.";
J. Cell Biol. 165:709-721(2004).
[16]
INTERACTION WITH DISC1.
PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
Whiting P.J.;
"Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
regulated protein complex: implications for schizophrenia and other
major neurological disorders.";
Mol. Cell. Neurosci. 25:42-55(2004).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
FUNCTION.
PubMed=22956769; DOI=10.1091/mbc.E12-03-0210;
Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A.,
Grigoriev I., Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A.,
Hoogenraad C.C., King S.J., Akhmanova A.;
"BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment
to cellular structures.";
Mol. Biol. Cell 23:4226-4241(2012).
[20]
INTERACTION WITH ASUN.
PubMed=23097494; DOI=10.1091/mbc.E12-07-0558;
Jodoin J.N., Shboul M., Sitaram P., Zein-Sabatto H., Reversade B.,
Lee E., Lee L.A.;
"Human Asunder promotes dynein recruitment and centrosomal tethering
to the nucleus at mitotic entry.";
Mol. Biol. Cell 23:4713-4724(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
VARIANT SBH PRO-169.
PubMed=10441340; DOI=10.1093/hmg/8.9.1757;
Pilz D.T., Kuc J., Matsumoto N., Bodurtha J., Bernadi B.,
Tassinari C.A., Dobyns W.B., Ledbetter D.H.;
"Subcortical band heterotopia in rare affected males can be caused by
missense mutations in DCX (XLIS) or LIS1.";
Hum. Mol. Genet. 8:1757-1760(1999).
[23]
VARIANTS LIS1 SER-31; SER-162 AND HIS-317.
PubMed=11502906; DOI=10.1212/WNL.57.3.416;
Leventer R.J., Cardoso C., Ledbetter D.H., Dobyns W.B.;
"LIS1 missense mutations cause milder lissencephaly phenotypes
including a child with normal IQ.";
Neurology 57:416-422(2001).
[24]
VARIANT SBH PRO-241.
PubMed=14581661; DOI=10.1212/WNL.61.8.1042;
Sicca F., Kelemen A., Genton P., Das S., Mei D., Moro F., Dobyns W.B.,
Guerrini R.;
"Mosaic mutations of the LIS1 gene cause subcortical band
heterotopia.";
Neurology 61:1042-1046(2003).
[25]
VARIANT LIS1 PRO-277.
PubMed=15007136; DOI=10.1212/01.WNL.0000113725.46254.FD;
Torres F.R., Montenegro M.A., Marques-de-Faria A.P., Guerreiro M.M.,
Cendes F., Lopes-Cendes I.;
"Mutation screening in a cohort of patients with lissencephaly and
subcortical band heterotopia.";
Neurology 62:799-802(2004).
-!- FUNCTION: 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. Required for dynein
recruitment to microtubule plus ends and BICD2-bound cargos
(PubMed:22956769). {ECO:0000250|UniProtKB:P63005,
ECO:0000269|PubMed:15173193, ECO:0000269|PubMed:22956769}.
-!- SUBUNIT: 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. {ECO:0000250, ECO:0000269|PubMed:11001923,
ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11889140,
ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14962739,
ECO:0000269|PubMed:14970193, ECO:0000269|PubMed:23097494}.
-!- INTERACTION:
P07900:HSP90AA1; NbExp=5; IntAct=EBI-720620, EBI-296047;
Q9CZA6:Nde1 (xeno); NbExp=6; IntAct=EBI-720620, EBI-309934;
Q9GZM8:NDEL1; NbExp=3; IntAct=EBI-720620, EBI-928842;
Q8WVJ2:NUDCD2; NbExp=8; IntAct=EBI-720620, EBI-1052153;
Q8IVD9:NUDCD3; NbExp=2; IntAct=EBI-720620, EBI-744342;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-
Rule:MF_03141}. Nucleus membrane {ECO:0000255|HAMAP-
Rule:MF_03141}. 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. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P43034-1; Sequence=Displayed;
Name=2;
IsoId=P43034-2; Sequence=VSP_019376, VSP_019377, VSP_019378,
VSP_019379;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Fairly ubiquitous expression in both the
frontal and occipital areas of the brain.
-!- DOMAIN: Dimerization mediated by the LisH domain may be required
to activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
-!- DISEASE: Lissencephaly 1 (LIS1) [MIM:607432]: A 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.
{ECO:0000269|PubMed:11163258, ECO:0000269|PubMed:11502906,
ECO:0000269|PubMed:15007136, ECO:0000269|PubMed:15173193,
ECO:0000269|PubMed:9063735}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Subcortical band heterotopia (SBH) [MIM:607432]: SBH 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. {ECO:0000269|PubMed:10441340,
ECO:0000269|PubMed:14581661}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Miller-Dieker lissencephaly syndrome (MDLS) [MIM:247200]:
A 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. Note=The disease is caused by mutations affecting the
gene represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
{ECO:0000255|HAMAP-Rule:MF_03141}.
-!- SEQUENCE CAUTION:
Sequence=AAA02882.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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EMBL; L13385; AAA02880.1; -; mRNA.
EMBL; L13386; AAA02881.1; -; mRNA.
EMBL; L13387; AAA02882.1; ALT_SEQ; mRNA.
EMBL; U72342; AAC51111.1; -; Genomic_DNA.
EMBL; U72334; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72335; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72336; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72337; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72338; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72339; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72340; AAC51111.1; JOINED; Genomic_DNA.
EMBL; U72341; AAC51111.1; JOINED; Genomic_DNA.
EMBL; AF208837; AAL34972.1; -; mRNA.
EMBL; AF208838; AAL34973.1; -; mRNA.
EMBL; AF400434; AAK92483.1; -; mRNA.
EMBL; AK313078; BAG35904.1; -; mRNA.
EMBL; BX538346; CAD98141.1; -; mRNA.
EMBL; CH471108; EAW90536.1; -; Genomic_DNA.
EMBL; BC064638; AAH64638.1; -; mRNA.
CCDS; CCDS32528.1; -. [P43034-1]
PIR; S36113; S36113.
RefSeq; NP_000421.1; NM_000430.3. [P43034-1]
RefSeq; XP_016880188.1; XM_017024699.1. [P43034-1]
RefSeq; XP_016880189.1; XM_017024700.1. [P43034-1]
RefSeq; XP_016880190.1; XM_017024701.1. [P43034-1]
UniGene; Hs.77318; -.
ProteinModelPortal; P43034; -.
SMR; P43034; -.
BioGrid; 111085; 76.
DIP; DIP-35691N; -.
IntAct; P43034; 33.
MINT; MINT-5004233; -.
STRING; 9606.ENSP00000380378; -.
iPTMnet; P43034; -.
PhosphoSitePlus; P43034; -.
BioMuta; PAFAH1B1; -.
DMDM; 1170794; -.
EPD; P43034; -.
MaxQB; P43034; -.
PaxDb; P43034; -.
PeptideAtlas; P43034; -.
PRIDE; P43034; -.
Ensembl; ENST00000397195; ENSP00000380378; ENSG00000007168. [P43034-1]
GeneID; 5048; -.
KEGG; hsa:5048; -.
UCSC; uc002fuw.5; human. [P43034-1]
CTD; 5048; -.
DisGeNET; 5048; -.
EuPathDB; HostDB:ENSG00000007168.12; -.
GeneCards; PAFAH1B1; -.
GeneReviews; PAFAH1B1; -.
HGNC; HGNC:8574; PAFAH1B1.
HPA; CAB004489; -.
HPA; HPA020036; -.
MalaCards; PAFAH1B1; -.
MIM; 247200; phenotype.
MIM; 601545; gene.
MIM; 607432; phenotype.
neXtProt; NX_P43034; -.
OpenTargets; ENSG00000007168; -.
Orphanet; 217385; 17p13.3 microduplication syndrome.
Orphanet; 95232; Lissencephaly due to LIS1 mutation.
Orphanet; 531; Miller-Dieker syndrome.
Orphanet; 99796; Subcortical band heterotopia.
PharmGKB; PA32905; -.
eggNOG; KOG0295; Eukaryota.
eggNOG; ENOG410XP3K; LUCA.
GeneTree; ENSGT00810000125363; -.
HOGENOM; HOG000184015; -.
HOVERGEN; HBG006271; -.
InParanoid; P43034; -.
KO; K16794; -.
OMA; DAHGHFV; -.
OrthoDB; EOG091G07Q1; -.
PhylomeDB; P43034; -.
TreeFam; TF105741; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SignaLink; P43034; -.
SIGNOR; P43034; -.
ChiTaRS; PAFAH1B1; human.
GeneWiki; PAFAH1B1; -.
GenomeRNAi; 5048; -.
PRO; PR:P43034; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000007168; -.
CleanEx; HS_PAFAH1B1; -.
ExpressionAtlas; P43034; baseline and differential.
Genevisible; P43034; HS.
GO; GO:0000235; C:astral microtubule; IDA:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0090724; C:central region of growth cone; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005871; C:kinesin complex; IEA:Ensembl.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
GO; GO:0031514; C:motile cilium; ISS:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
GO; GO:0032420; C:stereocilium; IEA:Ensembl.
GO; GO:0034452; F:dynactin binding; ISS:BHF-UCL.
GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
GO; GO:0045505; F:dynein intermediate chain binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; ISS:BHF-UCL.
GO; GO:0008017; F:microtubule binding; ISS:BHF-UCL.
GO; GO:0004623; F:phospholipase A2 activity; TAS:Reactome.
GO; GO:0043274; F:phospholipase binding; ISS:BHF-UCL.
GO; GO:0051219; F:phosphoprotein binding; ISS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
GO; GO:0001675; P:acrosome assembly; ISS:BHF-UCL.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IMP:BHF-UCL.
GO; GO:0001667; P:ameboidal-type cell migration; IEA:Ensembl.
GO; GO:0060117; P:auditory receptor cell development; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; IMP:BHF-UCL.
GO; GO:0021987; P:cerebral cortex development; IMP:BHF-UCL.
GO; GO:0021895; P:cerebral cortex neuron differentiation; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0090102; P:cochlea development; IEA:Ensembl.
GO; GO:0021540; P:corpus callosum morphogenesis; IMP:BHF-UCL.
GO; GO:0043622; P:cortical microtubule organization; IEA:Ensembl.
GO; GO:0051660; P:establishment of centrosome localization; IEA:Ensembl.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007281; P:germ cell development; IBA:GO_Central.
GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL.
GO; GO:0021819; P:layer formation in cerebral cortex; ISS:BHF-UCL.
GO; GO:0007611; P:learning or memory; ISS:BHF-UCL.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0051661; P:maintenance of centrosome location; IEA:Ensembl.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:BHF-UCL.
GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IEA:Ensembl.
GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
GO; GO:0007017; P:microtubule-based process; IDA:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0007405; P:neuroblast proliferation; ISS:BHF-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
GO; GO:0051081; P:nuclear envelope disassembly; IEA:Ensembl.
GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
GO; GO:0046469; P:platelet activating factor metabolic process; ISS:BHF-UCL.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:0040019; P:positive regulation of embryonic development; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0009306; P:protein secretion; IEA:Ensembl.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
GO; GO:2000574; P:regulation of microtubule motor activity; IBA:GO_Central.
GO; GO:0008090; P:retrograde axonal transport; ISS:BHF-UCL.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0017145; P:stem cell division; IEA:Ensembl.
GO; GO:0019226; P:transmission of nerve impulse; ISS:BHF-UCL.
GO; GO:0047496; P:vesicle transport along microtubule; ISS:BHF-UCL.
HAMAP; MF_03141; lis1; 1.
InterPro; IPR017252; Dynein_regulator_LIS1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR037190; LIS1_N.
InterPro; IPR006594; LisH.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF08513; LisH; 1.
Pfam; PF00400; WD40; 7.
PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00667; LisH; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF109925; SSF109925; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50896; LISH; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 7.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell cycle; Cell division;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Disease mutation;
Lipid degradation; Lipid metabolism; Lissencephaly; Membrane;
Microtubule; Mitosis; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transport; WD repeat.
CHAIN 1 410 Platelet-activating factor
acetylhydrolase IB subunit alpha.
/FTId=PRO_0000051061.
DOMAIN 7 39 LisH. {ECO:0000255|HAMAP-Rule:MF_03141}.
REPEAT 106 147 WD 1.
REPEAT 148 187 WD 2.
REPEAT 190 229 WD 3.
REPEAT 232 271 WD 4.
REPEAT 274 333 WD 5.
REPEAT 336 377 WD 6.
REPEAT 378 410 WD 7.
REGION 1 102 Interaction with NDEL1.
{ECO:0000255|HAMAP-Rule:MF_03141}.
REGION 1 66 Interaction with NDE1.
{ECO:0000255|HAMAP-Rule:MF_03141}.
REGION 1 38 Required for self-association and
interaction with PAFAH1B2 and PAFAH1B3.
{ECO:0000255|HAMAP-Rule:MF_03141}.
REGION 83 410 Interaction with dynein and dynactin.
REGION 367 409 Interaction with DCX.
{ECO:0000269|PubMed:11001923}.
REGION 388 410 Interaction with NDEL1.
{ECO:0000255|HAMAP-Rule:MF_03141}.
COILED 56 82 {ECO:0000255|HAMAP-Rule:MF_03141}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 12 64 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_019376.
VAR_SEQ 134 170 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_019377.
VAR_SEQ 237 237 V -> I (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_019378.
VAR_SEQ 238 410 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_019379.
VARIANT 31 31 F -> S (in LIS1; dbSNP:rs121434486).
{ECO:0000269|PubMed:11502906}.
/FTId=VAR_015398.
VARIANT 149 149 H -> R (in LIS1; abrogates interaction
with NDE1 and reduces neuronal migration
in vitro; dbSNP:rs121434482).
{ECO:0000269|PubMed:11163258,
ECO:0000269|PubMed:15173193,
ECO:0000269|PubMed:9063735}.
/FTId=VAR_007724.
VARIANT 162 162 G -> S (in LIS1; dbSNP:rs121434487).
{ECO:0000269|PubMed:11502906}.
/FTId=VAR_015399.
VARIANT 169 169 S -> P (in SBH; abrogates interaction
with NDE1 and reduces neuronal migration
in vitro; dbSNP:rs121434484).
{ECO:0000269|PubMed:10441340,
ECO:0000269|PubMed:11163258,
ECO:0000269|PubMed:15173193}.
/FTId=VAR_010203.
VARIANT 241 241 R -> P (in SBH; somatic mosaicism in 18%
of lymphocytes and 21% of hair root
cells; dbSNP:rs121434488).
{ECO:0000269|PubMed:14581661}.
/FTId=VAR_037300.
VARIANT 277 277 H -> P (in LIS1; dbSNP:rs121434490).
{ECO:0000269|PubMed:15007136}.
/FTId=VAR_037301.
VARIANT 317 317 D -> H (in LIS1; reduces neuronal
migration in vitro; dbSNP:rs121434485).
{ECO:0000269|PubMed:11502906,
ECO:0000269|PubMed:15173193}.
/FTId=VAR_015400.
CONFLICT 21 21 S -> P (in Ref. 3; AAL34972/AAL34973).
{ECO:0000305}.
CONFLICT 93 93 E -> G (in Ref. 3; AAL34973).
{ECO:0000305}.
CONFLICT 177 177 W -> R (in Ref. 3; AAL34973).
{ECO:0000305}.
SEQUENCE 410 AA; 46638 MW; 3AB68D2641BA31C9 CRC64;
MVLSQRQRDE LNRAIADYLR SNGYEEAYSV FKKEAELDVN EELDKKYAGL LEKKWTSVIR
LQKKVMELES KLNEAKEEFT SGGPLGQKRD PKEWIPRPPE KYALSGHRSP VTRVIFHPVF
SVMVSASEDA TIKVWDYETG DFERTLKGHT DSVQDISFDH SGKLLASCSA DMTIKLWDFQ
GFECIRTMHG HDHNVSSVAI MPNGDHIVSA SRDKTIKMWE VQTGYCVKTF TGHREWVRMV
RPNQDGTLIA SCSNDQTVRV WVVATKECKA ELREHEHVVE CISWAPESSY SSISEATGSE
TKKSGKPGPF LLSGSRDKTI KMWDVSTGMC LMTLVGHDNW VRGVLFHSGG KFILSCADDK
TLRVWDYKNK RCMKTLNAHE HFVTSLDFHK TAPYVVTGSV DQTVKVWECR


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