CE120_HUMAN
ID CE120_HUMAN Reviewed; 986 AA.
AC Q8N960; Q6AI52; Q6AW89; Q8IWB5; Q8N9Y0; Q8NDE8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Centrosomal protein of 120 kDa;
DE Short=Cep120;
DE AltName: Full=Coiled-coil domain-containing protein 100;
GN Name=CEP120; Synonyms=CCDC100;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-870 (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 401-986 (ISOFORMS 1/2), AND VARIANT VAL-602.
RC TISSUE=Brain, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-346 AND 498-986 (ISOFORMS
RP 1/2).
RC TISSUE=Salivary gland, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INVOLVEMENT IN SRTD13, AND VARIANT SRTD13 PRO-199.
RX PubMed=25361962; DOI=10.1093/hmg/ddu555;
RG UK10K Consortium;
RA Shaheen R., Schmidts M., Faqeih E., Hashem A., Lausch E., Holder I.,
RA Superti-Furga A., Mitchison H.M., Almoisheer A., Alamro R., Alshiddi T.,
RA Alzahrani F., Beales P.L., Alkuraya F.S.;
RT "A founder CEP120 mutation in Jeune asphyxiating thoracic dystrophy expands
RT the role of centriolar proteins in skeletal ciliopathies.";
RL Hum. Mol. Genet. 24:1410-1419(2015).
RN [9]
RP FUNCTION.
RX PubMed=27185865; DOI=10.1242/jcs.186338;
RA Chang C.W., Hsu W.B., Tsai J.J., Tang C.J., Tang T.K.;
RT "CEP295 interacts with microtubules and is required for centriole
RT elongation.";
RL J. Cell Sci. 129:2501-2513(2016).
RN [10]
RP INVOLVEMENT IN JBTS31, VARIANTS JBTS31 ALA-194; VAL-549; PHE-712 AND
RP PRO-726, AND VARIANTS PRO-199 AND SER-975.
RX PubMed=27208211; DOI=10.1136/jmedgenet-2016-103832;
RA Roosing S., Romani M., Isrie M., Rosti R.O., Micalizzi A., Musaev D.,
RA Mazza T., Al-Gazali L., Altunoglu U., Boltshauser E., D'Arrigo S.,
RA De Keersmaecker B., Kayserili H., Brandenberger S., Kraoua I., Mark P.R.,
RA McKanna T., Van Keirsbilck J., Moerman P., Poretti A., Puri R.,
RA Van Esch H., Gleeson J.G., Valente E.M.;
RT "Mutations in CEP120 cause Joubert syndrome as well as complex ciliopathy
RT phenotypes.";
RL J. Med. Genet. 53:608-615(2016).
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors and for proper positioning of neurons during brain
CC development. Also implicated in the migration and selfrenewal of neural
CC progenitors. Required for centriole duplication and maturation during
CC mitosis and subsequent ciliogenesis (By similarity). Required for the
CC recruitment of CEP295 to the proximal end of new-born centrioles at the
CC centriolar microtubule wall during early S phase in a PLK4-dependent
CC manner (PubMed:27185865). {ECO:0000250|UniProtKB:Q7TSG1,
CC ECO:0000269|PubMed:27185865}.
CC -!- SUBUNIT: Interacts with TACC2, TACC3, CCDC52, TALPID3.
CC {ECO:0000250|UniProtKB:Q7TSG1}.
CC -!- INTERACTION:
CC Q8N960; Q5TB80: CEP162; NbExp=6; IntAct=EBI-2563015, EBI-1059012;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843}. Note=Regulates the
CC localization of TACC3 to the centrosome in neural progenitors in vivo.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N960-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N960-2; Sequence=VSP_035123;
CC Name=3;
CC IsoId=Q8N960-3; Sequence=VSP_035124, VSP_035125;
CC -!- DISEASE: Short-rib thoracic dysplasia 13 with or without polydactyly
CC (SRTD13) [MIM:616300]: A form of short-rib thoracic dysplasia, a group
CC of autosomal recessive ciliopathies that are characterized by a
CC constricted thoracic cage, short ribs, shortened tubular bones, and a
CC 'trident' appearance of the acetabular roof. Polydactyly is variably
CC present. Non-skeletal involvement can include cleft lip/palate as well
CC as anomalies of major organs such as the brain, eye, heart, kidneys,
CC liver, pancreas, intestines, and genitalia. Some forms of the disease
CC are lethal in the neonatal period due to respiratory insufficiency
CC secondary to a severely restricted thoracic cage, whereas others are
CC compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC Saldino syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:25361962}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Joubert syndrome 31 (JBTS31) [MIM:617761]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. JBTS31 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:27208211}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CEP120 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04155.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10561.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC010369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040527; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK093409; BAC04155.1; ALT_INIT; mRNA.
DR EMBL; AK095646; BAC04596.1; -; mRNA.
DR EMBL; AL833929; CAD38785.2; -; mRNA.
DR EMBL; BX648687; CAH10561.1; ALT_INIT; mRNA.
DR EMBL; CR627324; CAH10371.1; -; mRNA.
DR CCDS; CCDS4134.2; -. [Q8N960-1]
DR CCDS; CCDS54890.1; -. [Q8N960-2]
DR RefSeq; NP_001159698.1; NM_001166226.1. [Q8N960-2]
DR RefSeq; NP_694955.2; NM_153223.3. [Q8N960-1]
DR RefSeq; XP_011541487.1; XM_011543185.2. [Q8N960-2]
DR RefSeq; XP_011541488.1; XM_011543186.2.
DR RefSeq; XP_016864574.1; XM_017009085.1.
DR PDB; 4ICW; X-ray; 2.20 A; A=1-151.
DR PDB; 4ICX; X-ray; 2.70 A; A/B/C=1-151.
DR PDB; 6FLJ; X-ray; 1.75 A; A=1-151.
DR PDB; 6FLK; X-ray; 1.60 A; A/B=450-610.
DR PDBsum; 4ICW; -.
DR PDBsum; 4ICX; -.
DR PDBsum; 6FLJ; -.
DR PDBsum; 6FLK; -.
DR AlphaFoldDB; Q8N960; -.
DR SMR; Q8N960; -.
DR BioGRID; 127486; 105.
DR IntAct; Q8N960; 97.
DR STRING; 9606.ENSP00000303058; -.
DR MoonDB; Q8N960; Predicted.
DR iPTMnet; Q8N960; -.
DR PhosphoSitePlus; Q8N960; -.
DR BioMuta; CEP120; -.
DR DMDM; 205696377; -.
DR EPD; Q8N960; -.
DR jPOST; Q8N960; -.
DR MassIVE; Q8N960; -.
DR MaxQB; Q8N960; -.
DR PaxDb; Q8N960; -.
DR PeptideAtlas; Q8N960; -.
DR PRIDE; Q8N960; -.
DR ProteomicsDB; 72491; -. [Q8N960-1]
DR ProteomicsDB; 72492; -. [Q8N960-2]
DR ProteomicsDB; 72493; -. [Q8N960-3]
DR Antibodypedia; 25668; 79 antibodies from 17 providers.
DR DNASU; 153241; -.
DR Ensembl; ENST00000306467.10; ENSP00000303058.6; ENSG00000168944.17. [Q8N960-1]
DR Ensembl; ENST00000306481.11; ENSP00000307419.6; ENSG00000168944.17. [Q8N960-2]
DR Ensembl; ENST00000328236.10; ENSP00000327504.5; ENSG00000168944.17. [Q8N960-1]
DR Ensembl; ENST00000508442.7; ENSP00000421620.3; ENSG00000168944.17. [Q8N960-2]
DR Ensembl; ENST00000513565.6; ENSP00000422089.2; ENSG00000168944.17. [Q8N960-3]
DR GeneID; 153241; -.
DR KEGG; hsa:153241; -.
DR MANE-Select; ENST00000306467.10; ENSP00000303058.6; NM_001375405.1; NP_001362334.1.
DR UCSC; uc003ktk.4; human. [Q8N960-1]
DR CTD; 153241; -.
DR DisGeNET; 153241; -.
DR GeneCards; CEP120; -.
DR GeneReviews; CEP120; -.
DR HGNC; HGNC:26690; CEP120.
DR HPA; ENSG00000168944; Low tissue specificity.
DR MalaCards; CEP120; -.
DR MIM; 613446; gene.
DR MIM; 616300; phenotype.
DR MIM; 617761; phenotype.
DR neXtProt; NX_Q8N960; -.
DR OpenTargets; ENSG00000168944; -.
DR Orphanet; 474; Jeune syndrome.
DR Orphanet; 475; Joubert syndrome.
DR Orphanet; 220493; Joubert syndrome with ocular defect.
DR PharmGKB; PA164717857; -.
DR VEuPathDB; HostDB:ENSG00000168944; -.
DR eggNOG; ENOG502QPT0; Eukaryota.
DR GeneTree; ENSGT00390000009378; -.
DR HOGENOM; CLU_723528_0_0_1; -.
DR InParanoid; Q8N960; -.
DR OMA; DELETWK; -.
DR OrthoDB; 277001at2759; -.
DR PhylomeDB; Q8N960; -.
DR TreeFam; TF329430; -.
DR PathwayCommons; Q8N960; -.
DR SignaLink; Q8N960; -.
DR BioGRID-ORCS; 153241; 33 hits in 1080 CRISPR screens.
DR ChiTaRS; CEP120; human.
DR GeneWiki; CEP120; -.
DR GenomeRNAi; 153241; -.
DR Pharos; Q8N960; Tbio.
DR PRO; PR:Q8N960; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N960; protein.
DR Bgee; ENSG00000168944; Expressed in calcaneal tendon and 181 other tissues.
DR ExpressionAtlas; Q8N960; baseline and differential.
DR Genevisible; Q8N960; HS.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0030953; P:astral microtubule organization; IEA:Ensembl.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0022027; P:interkinetic nuclear migration; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB.
DR GO; GO:0010825; P:positive regulation of centrosome duplication; ISS:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:1904951; P:positive regulation of establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039893; CEP120-like.
DR InterPro; IPR022136; DUF3668.
DR PANTHER; PTHR21574; PTHR21574; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF12416; DUF3668; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Ciliopathy; Coiled coil; Cytoplasm;
KW Cytoskeleton; Disease variant; Joubert syndrome; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..986
FT /note="Centrosomal protein of 120 kDa"
FT /id="PRO_0000348262"
FT DOMAIN 1..112
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 433..566
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 350..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 669..925
FT /evidence="ECO:0000255"
FT COMPBIAS 351..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TSG1"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035123"
FT VAR_SEQ 347..380
FT /note="SLIELKTQNEHEPEHSKKKVLTPIKEKTLTGPKS -> DAFWYSALDIIFPL
FT FIFLFLVLDAIRKFANYEEK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035124"
FT VAR_SEQ 381..986
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035125"
FT VARIANT 194
FT /note="V -> A (in JBTS31; unknown pathological
FT significance; dbSNP:rs1554104276)"
FT /evidence="ECO:0000269|PubMed:27208211"
FT /id="VAR_077553"
FT VARIANT 199
FT /note="A -> P (in SRTD13; also found in a patient with more
FT complex ciliopathy; dbSNP:rs367600930)"
FT /evidence="ECO:0000269|PubMed:25361962,
FT ECO:0000269|PubMed:27208211"
FT /id="VAR_073672"
FT VARIANT 549
FT /note="A -> V (in JBTS31; unknown pathological
FT significance; dbSNP:rs775080726)"
FT /evidence="ECO:0000269|PubMed:27208211"
FT /id="VAR_077554"
FT VARIANT 602
FT /note="L -> V (in dbSNP:rs6595440)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_046126"
FT VARIANT 712
FT /note="L -> F (in JBTS31; unknown pathological
FT significance; dbSNP:rs114280473)"
FT /evidence="ECO:0000269|PubMed:27208211"
FT /id="VAR_077555"
FT VARIANT 726
FT /note="L -> P (in JBTS31; unknown pathological
FT significance; dbSNP:rs1554102026)"
FT /evidence="ECO:0000269|PubMed:27208211"
FT /id="VAR_077556"
FT VARIANT 879
FT /note="Q -> H (in dbSNP:rs1047437)"
FT /id="VAR_046127"
FT VARIANT 936
FT /note="V -> I (in dbSNP:rs2303721)"
FT /id="VAR_046128"
FT VARIANT 947
FT /note="R -> H (in dbSNP:rs2303720)"
FT /id="VAR_046129"
FT VARIANT 975
FT /note="I -> S (found in a patient with Meckel syndrome;
FT unknown pathological significance; dbSNP:rs1554098663)"
FT /evidence="ECO:0000269|PubMed:27208211"
FT /id="VAR_077557"
FT CONFLICT 212
FT /note="L -> F (in Ref. 3; BAC04596)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="E -> G (in Ref. 3; BAC04596)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="H -> R (in Ref. 4; CAH10371)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="Q -> L (in Ref. 3; BAC04596)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:4ICX"
FT STRAND 8..19
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:6FLJ"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:6FLJ"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:6FLJ"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:6FLJ"
FT STRAND 452..465
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:6FLK"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 509..516
FT /evidence="ECO:0007829|PDB:6FLK"
FT HELIX 518..527
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 530..536
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 544..551
FT /evidence="ECO:0007829|PDB:6FLK"
FT HELIX 553..558
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 569..584
FT /evidence="ECO:0007829|PDB:6FLK"
FT STRAND 592..607
FT /evidence="ECO:0007829|PDB:6FLK"
SQ SEQUENCE 986 AA; 112640 MW; 97B96A09962B0862 CRC64;
MVSKSDQLLI VVSILEGRHF PKRPKHMLVV EAKFDGEQLA TDPVDHTDQP EFATELAWEI
DRKALHQHRL QRTPIKLQCF ALDPVTSAKE TIGYIVLDLR TAQETKQAPK WYQLLSNKYT
KFKSEIQISI ALETDTKPPV DSFKAKGAPP RDGKVPAILA GLDPRDIVAV LNEEGGYHQI
GPAEYCTDSF IMSVTIAFAT QLEQLIPCTM KLPERQPEFF FYYSLLGNDV TNEPFNDLIN
PNFEPERASV RIRSSVEILR VYLALQSKLQ IHLCCGDQSL GSTEIPLTGL LKKGSTEINQ
HPVTVEGAFT LDPPNRAKQK LAPIPVELAP TVGVSVALQR EGIDSQSLIE LKTQNEHEPE
HSKKKVLTPI KEKTLTGPKS PTVSPVPSHN QSPPTKDDAT ESEVESLQYD KDTKPNPKAS
SSVPASLAQL VTTSNASEVA SGQKIAVPAT SHHFCFSIDL RSIHALEIGF PINCILRYSY
PFFGSAAPIM TNPPVEVRKN MEVFLPQSYC AFDFATMPHQ LQDTFLRIPL LVELWHKDKM
SKDLLLGIAR IQLSNILSSE KTRFLGSNGE QCWRQTYSES VPVIAAQGSN NRIADLSYTV
TLEDYGLVKM REIFISDSSQ GVSAVQQKPS SLPPAPCPSE IQTEPRETLE YKAALELEMW
KEMQEDIFEN QLKQKELAHM QALAEEWKKR DRERESLVKK KVAEYTILEG KLQKTLIDLE
KREQQLASVE SELQREKKEL QSERQRNLQE LQDSIRRAKE DCIHQVELER LKIKQLEEDK
HRLQQQLNDA ENKYKILEKE FQQFKDQQNN KPEIRLQSEI NLLTLEKVEL ERKLESATKS
KLHYKQQWGR ALKELARLKQ REQESQMARL KKQQEELEQM RLRYLAAEEK DTVKTERQEL
LDIRNELNRL RQQEQKQYQD STEIASGKKD GPHGSVLEEG LDDYLTRLIE ERDTLMRTGV
YNHEDRIISE LDRQIREILA KSNASN
