SSNA1_HUMAN
ID SSNA1_HUMAN Reviewed; 119 AA.
AC O43805; Q5VSG0; Q6FG70; Q9BVW8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Microtubule nucleation factor SSNA1 {ECO:0000250|UniProtKB:Q9JJ94};
DE AltName: Full=Nuclear autoantigen of 14 kDa {ECO:0000303|PubMed:9430706};
DE AltName: Full=Sjoegren syndrome nuclear autoantigen 1;
GN Name=SSNA1 {ECO:0000312|HGNC:HGNC:11321};
GN Synonyms=NA14 {ECO:0000303|PubMed:9430706};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9430706; DOI=10.1074/jbc.273.3.1634;
RA Ramos-Morales F., Infante C., Fedriani C., Bornens M., Rios R.M.;
RT "NA14 is a novel nuclear autoantigen with a coiled-coil domain.";
RL J. Biol. Chem. 273:1634-1639(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12640030; DOI=10.1242/jcs.00337;
RA Pfannenschmid F., Wimmer V.C., Rios R.M., Geimer S., Kroeckel U.,
RA Leiherer A., Haller K., Nemcova Y., Mages W.;
RT "Chlamydomonas DIP13 and human NA14: a new class of proteins associated
RT with microtubule structures is involved in cell division.";
RL J. Cell Sci. 116:1449-1462(2003).
RN [8]
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 [9]
RP INTERACTION WITH SPAST.
RX PubMed=15269182; DOI=10.1093/hmg/ddh223;
RA Errico A., Claudiani P., D'Addio M., Rugarli E.I.;
RT "Spastin interacts with the centrosomal protein NA14, and is enriched in
RT the spindle pole, the midbody and the distal axon.";
RL Hum. Mol. Genet. 13:2121-2132(2004).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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 [12]
RP SUBUNIT, AND MUTAGENESIS OF CYS-18; CYS-23 AND CYS-30.
RX PubMed=22008182; DOI=10.1093/protein/gzr050;
RA Rodriguez-Rodriguez M., Trevino M.A., Laurents D.V., Arranz R.,
RA Valpuesta J.M., Rico M., Bruix M., Jimenez M.A.;
RT "Characterization of the structure and self-recognition of the human
RT centrosomal protein NA14: implications for stability and function.";
RL Protein Eng. Des. Sel. 24:883-892(2011).
RN [13]
RP FUNCTION, INTERACTION WITH SPAST, AND SUBCELLULAR LOCATION.
RX PubMed=25390646; DOI=10.1371/journal.pone.0112428;
RA Goyal U., Renvoise B., Chang J., Blackstone C.;
RT "Spastin-interacting protein NA14/SSNA1 functions in cytokinesis and axon
RT development.";
RL PLoS ONE 9:e112428-e112428(2014).
RN [14]
RP FUNCTION, AND SUBUNIT.
RX PubMed=34970964; DOI=10.7554/elife.67282;
RA Lawrence E.J., Arpag G., Arnaiz C., Zanic M.;
RT "SSNA1 stabilizes dynamic microtubules and detects microtubule damage.";
RL Elife 10:0-0(2021).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-17.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Microtubule-binding protein which stabilizes dynamic
CC microtubules by slowing growth and shrinkage at both plus and minus
CC ends and serves as a sensor of microtubule damage, protecting
CC microtubules from the microtubule-severing enzyme SPAST
CC (PubMed:34970964). Induces microtubule branching which is mediated by
CC the formation of long SSNA1 fibrils which guide microtubule
CC protofilaments to split apart from the mother microtubule and form
CC daughter microtubules (By similarity). Plays a role in axon outgrowth
CC and branching (PubMed:25390646). Required for cell division
CC (PubMed:25390646). {ECO:0000250|UniProtKB:Q9XF62,
CC ECO:0000269|PubMed:25390646, ECO:0000269|PubMed:34970964}.
CC -!- SUBUNIT: Self-associates to form fibrils (PubMed:22008182,
CC PubMed:34970964). Also forms dimers as well as monomers
CC (PubMed:22008182). Interacts with SPAST (PubMed:15269182,
CC PubMed:25390646). {ECO:0000269|PubMed:15269182,
CC ECO:0000269|PubMed:22008182, ECO:0000269|PubMed:25390646,
CC ECO:0000269|PubMed:34970964}.
CC -!- INTERACTION:
CC O43805; Q16543: CDC37; NbExp=3; IntAct=EBI-2515299, EBI-295634;
CC O43805; Q08426: EHHADH; NbExp=4; IntAct=EBI-2515299, EBI-2339219;
CC O43805; Q9HD26: GOPC; NbExp=3; IntAct=EBI-2515299, EBI-349832;
CC O43805; Q86VQ0: LCA5; NbExp=3; IntAct=EBI-2515299, EBI-6658186;
CC O43805; Q8TBB1: LNX1; NbExp=7; IntAct=EBI-2515299, EBI-739832;
CC O43805; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2515299, EBI-741158;
CC O43805; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2515299, EBI-79165;
CC O43805; P78317: RNF4; NbExp=3; IntAct=EBI-2515299, EBI-2340927;
CC O43805; O00560: SDCBP; NbExp=6; IntAct=EBI-2515299, EBI-727004;
CC O43805; O43805: SSNA1; NbExp=9; IntAct=EBI-2515299, EBI-2515299;
CC O43805; Q9P0N9: TBC1D7; NbExp=7; IntAct=EBI-2515299, EBI-3258000;
CC O43805; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-2515299, EBI-954696;
CC O43805; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2515299, EBI-11955057;
CC O43805; Q99757: TXN2; NbExp=6; IntAct=EBI-2515299, EBI-2932492;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9430706}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:12640030, ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:25390646}.
CC Midbody {ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton,
CC flagellum basal body {ECO:0000269|PubMed:12640030}. Cytoplasm,
CC cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12640030}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q9JJ94}. Note=In sperm,
CC strongly expressed in the basal body region with weaker expression in
CC the axoneme (PubMed:12640030). Localizes to axon branching points in
CC neurons (By similarity). {ECO:0000250|UniProtKB:Q9JJ94,
CC ECO:0000269|PubMed:12640030}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9430706}.
CC -!- SIMILARITY: Belongs to the SSNA1 family. {ECO:0000305}.
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DR EMBL; Z96932; CAB09660.1; -; mRNA.
DR EMBL; BT006766; AAP35412.1; -; mRNA.
DR EMBL; CR542238; CAG47034.1; -; mRNA.
DR EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88362.1; -; Genomic_DNA.
DR EMBL; BC000864; AAH00864.1; -; mRNA.
DR CCDS; CCDS7034.1; -.
DR RefSeq; NP_003722.2; NM_003731.2.
DR AlphaFoldDB; O43805; -.
DR SMR; O43805; -.
DR BioGRID; 114189; 43.
DR IntAct; O43805; 22.
DR MINT; O43805; -.
DR STRING; 9606.ENSP00000313752; -.
DR iPTMnet; O43805; -.
DR PhosphoSitePlus; O43805; -.
DR BioMuta; SSNA1; -.
DR EPD; O43805; -.
DR jPOST; O43805; -.
DR MassIVE; O43805; -.
DR MaxQB; O43805; -.
DR PaxDb; O43805; -.
DR PeptideAtlas; O43805; -.
DR PRIDE; O43805; -.
DR ProteomicsDB; 49174; -.
DR Antibodypedia; 32398; 107 antibodies from 23 providers.
DR DNASU; 8636; -.
DR Ensembl; ENST00000322310.10; ENSP00000313752.5; ENSG00000176101.12.
DR GeneID; 8636; -.
DR KEGG; hsa:8636; -.
DR MANE-Select; ENST00000322310.10; ENSP00000313752.5; NM_003731.3; NP_003722.2.
DR UCSC; uc004cls.3; human.
DR CTD; 8636; -.
DR DisGeNET; 8636; -.
DR GeneCards; SSNA1; -.
DR HGNC; HGNC:11321; SSNA1.
DR HPA; ENSG00000176101; Low tissue specificity.
DR MIM; 610882; gene.
DR neXtProt; NX_O43805; -.
DR OpenTargets; ENSG00000176101; -.
DR PharmGKB; PA36145; -.
DR VEuPathDB; HostDB:ENSG00000176101; -.
DR eggNOG; ENOG502S16M; Eukaryota.
DR GeneTree; ENSGT00390000012318; -.
DR HOGENOM; CLU_153440_0_0_1; -.
DR InParanoid; O43805; -.
DR OMA; SYNNELV; -.
DR OrthoDB; 1513306at2759; -.
DR PhylomeDB; O43805; -.
DR TreeFam; TF328451; -.
DR PathwayCommons; O43805; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O43805; -.
DR BioGRID-ORCS; 8636; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; SSNA1; human.
DR GenomeRNAi; 8636; -.
DR Pharos; O43805; Tbio.
DR PRO; PR:O43805; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O43805; protein.
DR Bgee; ENSG00000176101; Expressed in left testis and 201 other tissues.
DR ExpressionAtlas; O43805; baseline and differential.
DR Genevisible; O43805; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0099512; C:supramolecular fiber; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0140060; P:axon arborization; IMP:UniProtKB.
DR GO; GO:0048675; P:axon extension; IMP:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0060830; P:ciliary receptor clustering involved in smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0042073; P:intraciliary transport; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IDA:UniProtKB.
DR InterPro; IPR033362; SSNA1_fam.
DR PANTHER; PTHR28661; PTHR28661; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cell projection; Cilium;
KW Coiled coil; Cytoplasm; Cytoskeleton; Flagellum; Neurogenesis; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..119
FT /note="Microtubule nucleation factor SSNA1"
FT /id="PRO_0000114483"
FT REGION 2..32
FT /note="Important for localization to the centrosome"
FT /evidence="ECO:0000269|PubMed:25390646"
FT COILED 13..70
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VARIANT 17
FT /note="K -> N (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1289962028)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036343"
FT MUTAGEN 18
FT /note="C->S: Does not affect oligomer formation; when
FT associated with S-23 and S-30."
FT /evidence="ECO:0000269|PubMed:22008182"
FT MUTAGEN 23
FT /note="C->S: Does not affect oligomer formation; when
FT associated with S-18 and S-30."
FT /evidence="ECO:0000269|PubMed:22008182"
FT MUTAGEN 30
FT /note="C->S: Does not affect oligomer formation; when
FT associated with S-18 and S-23."
FT /evidence="ECO:0000269|PubMed:22008182"
FT CONFLICT 57
FT /note="V -> A (in Ref. 3; CAG47034)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> F (in Ref. 1; CAB09660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 119 AA; 13596 MW; 6BB9BB96580DB807 CRC64;
MTQQGAALQN YNNELVKCIE ELCQKREELC RQIQEEEDEK QRLQNEVRQL TEKLARVNEN
LARKIASRNE FDRTIAETEA AYLKILESSQ TLLSVLKREA GNLTKATAPD QKSSGGRDS
