TSACC_HUMAN
ID TSACC_HUMAN Reviewed; 125 AA.
AC Q96A04; D3DVB9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=TSSK6-activating co-chaperone protein;
DE AltName: Full=SSTK-interacting protein {ECO:0000303|PubMed:20829357};
DE Short=SIP {ECO:0000303|PubMed:20829357};
DE Short=SSTK-IP;
GN Name=TSACC; Synonyms=C1orf182;
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], FUNCTION, INTERACTION WITH TSSK6 AND HSP70,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=20829357; DOI=10.1074/jbc.m110.134767;
RA Jha K.N., Wong L., Zerfas P.M., De Silva R.S., Fan Y.X., Spiridonov N.A.,
RA Johnson G.R.;
RT "Identification of a novel HSP70-binding cochaperone critical to HSP90-
RT mediated activation of small serine/threonine kinase.";
RL J. Biol. Chem. 285:35180-35187(2010).
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].
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).
CC -!- FUNCTION: Co-chaperone that facilitates HSP-mediated activation of
CC TSSK6. {ECO:0000269|PubMed:20829357}.
CC -!- SUBUNIT: Interacts with HSP70. Associates with HSP90. Interacts with
CC TSSK6; this interaction is direct and recruits TSACC to HSP90.
CC {ECO:0000269|PubMed:20829357}.
CC -!- INTERACTION:
CC Q96A04; Q86V38: ATN1; NbExp=3; IntAct=EBI-740411, EBI-11954292;
CC Q96A04; P02489: CRYAA; NbExp=3; IntAct=EBI-740411, EBI-6875961;
CC Q96A04; O15409: FOXP2; NbExp=6; IntAct=EBI-740411, EBI-983612;
CC Q96A04; O14901: KLF11; NbExp=3; IntAct=EBI-740411, EBI-948266;
CC Q96A04; Q8N485: LIX1; NbExp=3; IntAct=EBI-740411, EBI-10694501;
CC Q96A04; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-740411, EBI-2811583;
CC Q96A04; Q13153: PAK1; NbExp=3; IntAct=EBI-740411, EBI-1307;
CC -!- TISSUE SPECIFICITY: Expressed in testis but is absent from mature
CC sperm. {ECO:0000269|PubMed:20829357}.
CC -!- SIMILARITY: Belongs to the TSACC family. {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; AY048672; AAL07513.1; -; mRNA.
DR EMBL; AY048673; AAL07514.1; -; mRNA.
DR EMBL; AL589685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52964.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52965.1; -; Genomic_DNA.
DR EMBL; BC014605; AAH14605.1; -; mRNA.
DR CCDS; CCDS1141.1; -.
DR RefSeq; NP_001291746.1; NM_001304817.1.
DR RefSeq; NP_001291747.1; NM_001304818.1.
DR RefSeq; NP_001291748.1; NM_001304819.1.
DR RefSeq; NP_001291749.1; NM_001304820.1.
DR RefSeq; NP_001291750.1; NM_001304821.1.
DR RefSeq; NP_001291751.1; NM_001304822.1.
DR RefSeq; NP_001291752.1; NM_001304823.1.
DR RefSeq; NP_001291753.1; NM_001304824.1.
DR RefSeq; NP_001291754.1; NM_001304825.1.
DR RefSeq; NP_001291755.1; NM_001304826.1.
DR RefSeq; NP_653228.1; NM_144627.4.
DR AlphaFoldDB; Q96A04; -.
DR SMR; Q96A04; -.
DR BioGRID; 126101; 5.
DR IntAct; Q96A04; 9.
DR MINT; Q96A04; -.
DR STRING; 9606.ENSP00000357238; -.
DR iPTMnet; Q96A04; -.
DR PhosphoSitePlus; Q96A04; -.
DR BioMuta; TSACC; -.
DR MassIVE; Q96A04; -.
DR PaxDb; Q96A04; -.
DR PeptideAtlas; Q96A04; -.
DR PRIDE; Q96A04; -.
DR Antibodypedia; 34213; 63 antibodies from 12 providers.
DR DNASU; 128229; -.
DR Ensembl; ENST00000368251.1; ENSP00000357234.1; ENSG00000163467.12.
DR Ensembl; ENST00000368252.5; ENSP00000357235.1; ENSG00000163467.12.
DR Ensembl; ENST00000368253.6; ENSP00000357236.1; ENSG00000163467.12.
DR Ensembl; ENST00000368254.6; ENSP00000357237.1; ENSG00000163467.12.
DR Ensembl; ENST00000368255.7; ENSP00000357238.3; ENSG00000163467.12.
DR GeneID; 128229; -.
DR KEGG; hsa:128229; -.
DR MANE-Select; ENST00000368254.6; ENSP00000357237.1; NM_001304817.2; NP_001291746.1.
DR UCSC; uc001foo.4; human.
DR CTD; 128229; -.
DR DisGeNET; 128229; -.
DR GeneCards; TSACC; -.
DR HGNC; HGNC:30636; TSACC.
DR HPA; ENSG00000163467; Tissue enriched (testis).
DR MIM; 619679; gene.
DR neXtProt; NX_Q96A04; -.
DR OpenTargets; ENSG00000163467; -.
DR PharmGKB; PA142672430; -.
DR VEuPathDB; HostDB:ENSG00000163467; -.
DR eggNOG; ENOG502SWRI; Eukaryota.
DR GeneTree; ENSGT00390000012524; -.
DR HOGENOM; CLU_162380_0_0_1; -.
DR InParanoid; Q96A04; -.
DR OMA; RMYANLQ; -.
DR OrthoDB; 1511256at2759; -.
DR PhylomeDB; Q96A04; -.
DR TreeFam; TF337043; -.
DR PathwayCommons; Q96A04; -.
DR SignaLink; Q96A04; -.
DR BioGRID-ORCS; 128229; 26 hits in 1067 CRISPR screens.
DR ChiTaRS; TSACC; human.
DR GenomeRNAi; 128229; -.
DR Pharos; Q96A04; Tbio.
DR PRO; PR:Q96A04; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96A04; protein.
DR Bgee; ENSG00000163467; Expressed in sperm and 116 other tissues.
DR ExpressionAtlas; Q96A04; baseline and differential.
DR Genevisible; Q96A04; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR InterPro; IPR031679; SSTK-IP.
DR PANTHER; PTHR37368; PTHR37368; 1.
DR Pfam; PF15836; SSTK-IP; 1.
PE 1: Evidence at protein level;
KW Chaperone; Reference proteome.
FT CHAIN 1..125
FT /note="TSSK6-activating co-chaperone protein"
FT /id="PRO_0000271073"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 54
FT /note="S -> L (in dbSNP:rs41265043)"
FT /id="VAR_061567"
SQ SEQUENCE 125 AA; 13670 MW; 40FE1D7B77204DB4 CRC64;
MERHTSHPNR KVPAKEEANA VPLCRAKPSP SYINLQASSP PATFLNIQTT KLPSVDHKPK
ECLGLLECMY ANLQLQTQLA QQQMAVLEHL QASVTQLAPG RGSNNSSLPA LSPNPLLNHL
PQFSK
