SAS6_HUMAN
ID SAS6_HUMAN Reviewed; 657 AA.
AC Q6UVJ0; D3DT55; Q8N3K0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Spindle assembly abnormal protein 6 homolog {ECO:0000305};
DE Short=HsSAS-6 {ECO:0000303|PubMed:31722219};
GN Name=SASS6 {ECO:0000312|HGNC:HGNC:25403}; Synonyms=SAS6;
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 [MRNA].
RA Shan Y.X., Chen K., Yu L.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-657.
RC TISSUE=Amygdala;
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 SUBCELLULAR LOCATION.
RX PubMed=15572125; DOI=10.1016/j.devcel.2004.10.015;
RA Dammermann A., Mueller-Reichert T., Pelletier L., Habermann B., Desai A.,
RA Oegema K.;
RT "Centriole assembly requires both centriolar and pericentriolar material
RT proteins.";
RL Dev. Cell 7:815-829(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15665853; DOI=10.1038/ncb1220;
RA Leidel S., Delattre M., Cerutti L., Baumer K., Goenczy P.;
RT "SAS-6 defines a protein family required for centrosome duplication in C.
RT elegans and in human cells.";
RL Nat. Cell Biol. 7:115-125(2005).
RN [7]
RP FUNCTION.
RX PubMed=16244668; DOI=10.1038/ncb1320;
RA Habedanck R., Stierhof Y.-D., Wilkinson C.J., Nigg E.A.;
RT "The Polo kinase Plk4 functions in centriole duplication.";
RL Nat. Cell Biol. 7:1140-1146(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
RA Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D.,
RA Nigg E.A.;
RT "Plk4-induced centriole biogenesis in human cells.";
RL Dev. Cell 13:190-202(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, AND FORMATION OF A COMPLEX WITH CENPJ AND STIL.
RX PubMed=22020124; DOI=10.1038/emboj.2011.378;
RA Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C., Chang C.W.,
RA Wu K.S., Tang T.K.;
RT "The human microcephaly protein STIL interacts with CPAP and is required
RT for procentriole formation.";
RL EMBO J. 30:4790-4804(2011).
RN [15]
RP UBIQUITINATION, AND INTERACTION WITH FBXW5.
RX PubMed=21725316; DOI=10.1038/ncb2282;
RA Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U.,
RA Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P.,
RA Malek N.P.;
RT "The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6
RT to control centrosome duplication.";
RL Nat. Cell Biol. 13:1004-1009(2011).
RN [16]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-131.
RX PubMed=21273447; DOI=10.1126/science.1199325;
RA van Breugel M., Hirono M., Andreeva A., Yanagisawa H.A., Yamaguchi S.,
RA Nakazawa Y., Morgner N., Petrovich M., Ebong I.O., Robinson C.V.,
RA Johnson C.M., Veprintsev D., Zuber B.;
RT "Structures of SAS-6 suggest its organization in centrioles.";
RL Science 331:1196-1199(2011).
RN [17]
RP INTERACTION WITH NUP62 AND TUBG1, AND SUBCELLULAR LOCATION.
RX PubMed=24107630; DOI=10.4161/cc.26671;
RA Hashizume C., Moyori A., Kobayashi A., Yamakoshi N., Endo A., Wong R.W.;
RT "Nucleoporin Nup62 maintains centrosome homeostasis.";
RL Cell Cycle 12:3804-3816(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-615, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP SUBCELLULAR LOCATION, INTERACTION WITH CENATAC AND FZR1, AND
RP UBIQUITINATION.
RX PubMed=31722219; DOI=10.1016/j.celrep.2019.10.028;
RA Wang T., Zou Y., Huang N., Teng J., Chen J.;
RT "CCDC84 Acetylation Oscillation Regulates Centrosome Duplication by
RT Modulating HsSAS-6 Degradation.";
RL Cell Rep. 29:2078-2091.e5(2019).
RN [20]
RP INVOLVEMENT IN MCPH14, VARIANT MCPH14 THR-62, AND CHARACTERIZATION OF
RP VARIANT MCPH14 THR-62.
RX PubMed=24951542; DOI=10.1093/hmg/ddu318;
RA Khan M.A., Rupp V.M., Orpinell M., Hussain M.S., Altmueller J.,
RA Steinmetz M.O., Enzinger C., Thiele H., Hoehne W., Nuernberg G., Baig S.M.,
RA Ansar M., Nuernberg P., Vincent J.B., Speicher M.R., Goenczy P.,
RA Windpassinger C.;
RT "A missense mutation in the PISA domain of HsSAS-6 causes autosomal
RT recessive primary microcephaly in a large consanguineous Pakistani
RT family.";
RL Hum. Mol. Genet. 23:5940-5949(2014).
CC -!- FUNCTION: Central scaffolding component of the centrioles ensuring
CC their 9-fold symmetry. Required for centrosome biogenesis and
CC duplication: required both for mother-centriole-dependent centriole
CC duplication and deuterosome-dependent centriole amplification in
CC multiciliated cells. Overexpression results in excess foci-bearing
CC centriolar markers. Required for the recruitment of STIL to the
CC procentriole and for STIL-mediated centriole amplification
CC (PubMed:22020124). {ECO:0000269|PubMed:15665853,
CC ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:17681131,
CC ECO:0000269|PubMed:22020124}.
CC -!- SUBUNIT: Nine homodimers form a cartwheel structure with an internal
CC diameter of 23 nM and radial spokes connecting to the microtubule
CC triplets (By similarity). Interacts with FBXW5 (PubMed:21725316). Forms
CC a complex with CENPJ and STIL (PubMed:22020124). Interacts with NUP62
CC and TUBG1 at the centrosome (PubMed:24107630). Interacts with CENATAC;
CC the interaction increases with CENATAC acetylation (PubMed:31722219).
CC Interacts with FZR1; the interaction is regulated by CENATAC and leads
CC to SASS6 proteasomal degradation (PubMed:31722219).
CC {ECO:0000250|UniProtKB:Q7ZVT3, ECO:0000269|PubMed:21725316,
CC ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:24107630,
CC ECO:0000269|PubMed:31722219}.
CC -!- INTERACTION:
CC Q6UVJ0; Q92870-2: APBB2; NbExp=3; IntAct=EBI-1570153, EBI-21535880;
CC Q6UVJ0; Q66GS9: CEP135; NbExp=8; IntAct=EBI-1570153, EBI-1046993;
CC Q6UVJ0; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-1570153, EBI-11958845;
CC Q6UVJ0; P42858: HTT; NbExp=15; IntAct=EBI-1570153, EBI-466029;
CC Q6UVJ0; Q7Z412: PEX26; NbExp=3; IntAct=EBI-1570153, EBI-752057;
CC Q6UVJ0; D3DTS7: PMP22; NbExp=3; IntAct=EBI-1570153, EBI-25882629;
CC Q6UVJ0; Q15468: STIL; NbExp=4; IntAct=EBI-1570153, EBI-7488405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15665853,
CC ECO:0000269|PubMed:24107630, ECO:0000269|PubMed:31722219}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:15572125, ECO:0000269|PubMed:15665853,
CC ECO:0000269|PubMed:17681131}. Note=Component of the deuterosome, a
CC structure that promotes de novo centriole amplification in
CC multiciliated cells that can generate more than 100 centrioles (By
CC similarity). Component of the centrosome. Associated only transiently
CC with nascent procentrioles during centriole biogenesis.
CC {ECO:0000250|UniProtKB:Q80UK7}.
CC -!- DOMAIN: The 35 nM long coiled-coil domain mediates homodimerization
CC while the globular N-terminus links the dimers at an angle of 40
CC degrees to form the inner ring. {ECO:0000250|UniProtKB:Q7ZVT3}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase
CC complex during S phase, leading to its degradation and preventing
CC centriole reduplication. Ubiquitinated by the anaphase promoting
CC complex/cyclosome (APC/C) E3 ubiquitin-protein ligase complex, leading
CC to its degradation and preventing centriole reduplication
CC (PubMed:31722219). {ECO:0000269|PubMed:21725316,
CC ECO:0000269|PubMed:31722219}.
CC -!- DISEASE: Microcephaly 14, primary, autosomal recessive (MCPH14)
CC [MIM:616402]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small.
CC {ECO:0000269|PubMed:24951542}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AY359522; AAQ57128.1; -; mRNA.
DR EMBL; AC093019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72974.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72975.1; -; Genomic_DNA.
DR EMBL; AL834265; CAD38940.1; -; mRNA.
DR CCDS; CCDS764.1; -.
DR RefSeq; NP_001291758.1; NM_001304829.1.
DR RefSeq; NP_919268.1; NM_194292.2.
DR PDB; 6YS4; X-ray; 2.11 A; A/B/C/D/E/F=211-312.
DR PDB; 6Z4A; X-ray; 1.46 A; A=1-152.
DR PDBsum; 6YS4; -.
DR PDBsum; 6Z4A; -.
DR AlphaFoldDB; Q6UVJ0; -.
DR SMR; Q6UVJ0; -.
DR BioGRID; 127880; 152.
DR ComplexPortal; CPX-1159; CPAP-STIL complex.
DR IntAct; Q6UVJ0; 84.
DR MINT; Q6UVJ0; -.
DR STRING; 9606.ENSP00000287482; -.
DR GlyGen; Q6UVJ0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UVJ0; -.
DR MetOSite; Q6UVJ0; -.
DR PhosphoSitePlus; Q6UVJ0; -.
DR BioMuta; SASS6; -.
DR DMDM; 62511032; -.
DR EPD; Q6UVJ0; -.
DR jPOST; Q6UVJ0; -.
DR MassIVE; Q6UVJ0; -.
DR MaxQB; Q6UVJ0; -.
DR PaxDb; Q6UVJ0; -.
DR PeptideAtlas; Q6UVJ0; -.
DR PRIDE; Q6UVJ0; -.
DR ProteomicsDB; 67430; -.
DR Antibodypedia; 33691; 138 antibodies from 20 providers.
DR DNASU; 163786; -.
DR Ensembl; ENST00000287482.6; ENSP00000287482.5; ENSG00000156876.10.
DR GeneID; 163786; -.
DR KEGG; hsa:163786; -.
DR MANE-Select; ENST00000287482.6; ENSP00000287482.5; NM_194292.3; NP_919268.1.
DR UCSC; uc001dsu.4; human.
DR CTD; 163786; -.
DR DisGeNET; 163786; -.
DR GeneCards; SASS6; -.
DR HGNC; HGNC:25403; SASS6.
DR HPA; ENSG00000156876; Low tissue specificity.
DR MalaCards; SASS6; -.
DR MIM; 609321; gene.
DR MIM; 616402; phenotype.
DR neXtProt; NX_Q6UVJ0; -.
DR OpenTargets; ENSG00000156876; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA142670950; -.
DR VEuPathDB; HostDB:ENSG00000156876; -.
DR eggNOG; ENOG502QQ4W; Eukaryota.
DR GeneTree; ENSGT00390000006932; -.
DR HOGENOM; CLU_018291_1_0_1; -.
DR InParanoid; Q6UVJ0; -.
DR OMA; YHLQFVE; -.
DR OrthoDB; 345225at2759; -.
DR PhylomeDB; Q6UVJ0; -.
DR TreeFam; TF326199; -.
DR PathwayCommons; Q6UVJ0; -.
DR SignaLink; Q6UVJ0; -.
DR SIGNOR; Q6UVJ0; -.
DR BioGRID-ORCS; 163786; 574 hits in 1089 CRISPR screens.
DR ChiTaRS; SASS6; human.
DR GeneWiki; SASS6; -.
DR GenomeRNAi; 163786; -.
DR Pharos; Q6UVJ0; Tbio.
DR PRO; PR:Q6UVJ0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6UVJ0; protein.
DR Bgee; ENSG00000156876; Expressed in oocyte and 113 other tissues.
DR Genevisible; Q6UVJ0; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR GO; GO:0120099; C:procentriole replication complex; IPI:ComplexPortal.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
DR GO; GO:0046601; P:positive regulation of centriole replication; IDA:ComplexPortal.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:ComplexPortal.
DR GO; GO:1905832; P:positive regulation of spindle assembly; IC:ComplexPortal.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IC:ComplexPortal.
DR Gene3D; 2.170.210.20; -; 1.
DR InterPro; IPR032396; SAS-6_N.
DR InterPro; IPR038558; SAS-6_N_sf.
DR InterPro; IPR041513; SAS6_CC.
DR Pfam; PF16531; SAS-6_N; 1.
DR Pfam; PF18594; Sas6_CC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Phosphoprotein; Primary microcephaly; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..657
FT /note="Spindle assembly abnormal protein 6 homolog"
FT /id="PRO_0000189972"
FT DOMAIN 39..91
FT /note="PISA"
FT REGION 487..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..471
FT /evidence="ECO:0000255"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VARIANT 62
FT /note="I -> T (in MCPH14; impairs the centriole-forming
FT function of the protein; dbSNP:rs876661307)"
FT /evidence="ECO:0000269|PubMed:24951542"
FT /id="VAR_073833"
FT VARIANT 259
FT /note="A -> V (in dbSNP:rs13375867)"
FT /id="VAR_021590"
FT MUTAGEN 131
FT /note="F->D: Fails to multimerize via N-terminus."
FT /evidence="ECO:0000269|PubMed:21273447"
FT STRAND 1..15
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 20..35
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:6Z4A"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:6Z4A"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:6Z4A"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6Z4A"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:6Z4A"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6Z4A"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:6Z4A"
FT HELIX 211..310
FT /evidence="ECO:0007829|PDB:6YS4"
SQ SEQUENCE 657 AA; 74397 MW; 6D19696BC748849F CRC64;
MSQVLFHQLV PLQVKCKDCE ERRVSIRMSI ELQSVSNPVH RKDLVIRLTD DTDPFFLYNL
VISEEDFQSL KFQQGLLVDF LAFPQKFIDL LQQCTQEHAK EIPRFLLQLV SPAAILDNSP
AFLNVVETNP FKHLTHLSLK LLPGNDVEIK KFLAGCLKCS KEEKLSLMQS LDDATKQLDF
TRKTLAEKKQ ELDKLRNEWA SHTAALTNKH SQELTNEKEK ALQAQVQYQQ QHEQQKKDLE
ILHQQNIHQL QNRLSELEAA NKDLTERKYK GDSTIRELKA KLSGVEEELQ RTKQEVLSLR
RENSTLDVEC HEKEKHVNQL QTKVAVLEQE IKDKDQLVLR TKEAFDTIQE QKVVLEENGE
KNQVQLGKLE ATIKSLSAEL LKANEIIKKL QGDLKTLMGK LKLKNTVTIQ QEKLLAEKEE
KLQKEQKELQ DVGQSLRIKE QEVCKLQEQL EATVKKLEES KQLLKNNEKL ITWLNKELNE
NQLVRKQDVL GPSTTPPAHS SSNTIRSGIS PNLNVVDGRL TYPTCGIGYP VSSAFAFQNT
FPHSISAKNT SHPGSGTKVQ FNLQFTKPNA SLGDVQSGAT ISMPCSTDKE NGENVGLESK
YLKKREDSIP LRGLSQNLFS NSDHQRDGTL GALHTSSKPT ALPSASSAYF PGQLPNS
