SATL1_HUMAN
ID SATL1_HUMAN Reviewed; 695 AA.
AC Q86VE3; A0A2R8Y5C1; A0AVK7; E9PB72; Q5H8V9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 4.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Spermidine/spermine N(1)-acetyltransferase-like protein 1;
DE EC=2.3.1.-;
GN Name=SATL1;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-695 (ISOFORM 2), AND VARIANT
RP ARG-279.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86VE3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86VE3-2; Sequence=VSP_024253, VSP_024254;
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; Z99571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043215; AAH43215.2; -; mRNA.
DR EMBL; BC126401; AAI26402.1; -; mRNA.
DR CCDS; CCDS35343.2; -. [Q86VE3-2]
DR RefSeq; NP_001012998.2; NM_001012980.2. [Q86VE3-2]
DR AlphaFoldDB; Q86VE3; -.
DR SMR; Q86VE3; -.
DR BioGRID; 131076; 1.
DR STRING; 9606.ENSP00000425421; -.
DR iPTMnet; Q86VE3; -.
DR PhosphoSitePlus; Q86VE3; -.
DR BioMuta; SATL1; -.
DR DMDM; 143583359; -.
DR jPOST; Q86VE3; -.
DR MassIVE; Q86VE3; -.
DR PaxDb; Q86VE3; -.
DR PeptideAtlas; Q86VE3; -.
DR PRIDE; Q86VE3; -.
DR Antibodypedia; 54033; 61 antibodies from 14 providers.
DR DNASU; 340562; -.
DR Ensembl; ENST00000509231.1; ENSP00000425421.1; ENSG00000184788.14. [Q86VE3-2]
DR Ensembl; ENST00000644105.2; ENSP00000494345.1; ENSG00000184788.14. [Q86VE3-1]
DR Ensembl; ENST00000646118.1; ENSP00000493598.1; ENSG00000184788.14. [Q86VE3-1]
DR GeneID; 340562; -.
DR KEGG; hsa:340562; -.
DR MANE-Select; ENST00000644105.2; ENSP00000494345.1; NM_001367857.2; NP_001354786.1.
DR UCSC; uc004een.4; human. [Q86VE3-1]
DR CTD; 340562; -.
DR GeneCards; SATL1; -.
DR HGNC; HGNC:27992; SATL1.
DR HPA; ENSG00000184788; Not detected.
DR neXtProt; NX_Q86VE3; -.
DR OpenTargets; ENSG00000184788; -.
DR PharmGKB; PA134969637; -.
DR VEuPathDB; HostDB:ENSG00000184788; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_052128_1_0_1; -.
DR InParanoid; Q86VE3; -.
DR OMA; HPGMWQP; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; Q86VE3; -.
DR TreeFam; TF319736; -.
DR PathwayCommons; Q86VE3; -.
DR BioGRID-ORCS; 340562; 10 hits in 694 CRISPR screens.
DR ChiTaRS; SATL1; human.
DR GenomeRNAi; 340562; -.
DR Pharos; Q86VE3; Tdark.
DR PRO; PR:Q86VE3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q86VE3; protein.
DR Bgee; ENSG00000184788; Expressed in ventricular zone and 34 other tissues.
DR ExpressionAtlas; Q86VE3; baseline and differential.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039533; Satl1.
DR PANTHER; PTHR10545:SF60; PTHR10545:SF60; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Reference proteome; Transferase.
FT CHAIN 1..695
FT /note="Spermidine/spermine N(1)-acetyltransferase-like
FT protein 1"
FT /id="PRO_0000282928"
FT DOMAIN 529..695
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 552..553
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 618..620
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 626..631
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 650..652
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 626..632
FT /note="GLGIGAE -> DSHHNSM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024253"
FT VAR_SEQ 633..695
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024254"
FT VARIANT 279
FT /note="W -> R (in dbSNP:rs10126146)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031438"
FT CONFLICT 176
FT /note="T -> S (in Ref. 1; AAH43215)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="S -> G (in Ref. 1; AAH43215)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="P -> L (in Ref. 2; AAI26402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 75812 MW; 198271758632AEE1 CRC64;
MNQSGTNQSS LSDSNQAGIN QPSTNSLGMN QMDMNQGSAS LYEMNQVDMK QPSMSQAGMR
QSGTNLPDIN QPDMKQPDTW QLGRSQPGML QQELSQLVLS KAGISQPDPS QPGPSQSGPS
QSRMRQIGTN QSGMSQPVMQ QLDSQSGGSQ PSMRQVGTSQ LGTSQIGMSQ PGTWQTGLSQ
PVLRQPNMSP PGMWQPGVQQ PGISQQVPSH PDMSQPGMSQ QVPSQPGIRQ PDTSQSCKNQ
TDMSQPDANQ SSLSDSNQTG IIQPSPSLLG MNQMDMNQWS ASLYEMNQVD MKQPSMSQAG
MRQSGTNLPD INQPGMKQPG TWQLGRSQPG MWPQSLSELV LSEASISQPG PPQRAPSQSG
PRQSSTSQAG TNQSGISQPV MWQLDMRQSG GSQPSMRQVG TSQSGTSQIG MSQPGTWQTG
LSQPVPRQPN KSPPGMWQRG MWQPGMSQQV PSQLGMRQPG TSQSSKNQTG MSHPGRGQPG
IWEPGPSQPG LSQQDLNQLV LSQPGLSQPG RSQPSVSQMG MRQTSMDYFQ IRHAEAGDCP
EILRLIKELA ACENMLDAME LTAADLLRDG FGDNPLFYCL IAEVNDQQKP SGKLTVGFAM
YYFTYDSWTG KVLYLEDFYV TQAYQGLGIG AEMLKRLSQI AITTQCNCMH FLVVIWNQAS
INYYTSRGAL DLSSEEGWHL FRFNREELLD MAWEE
