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SPEE_HUMAN
ID   SPEE_HUMAN              Reviewed;         302 AA.
AC   P19623; B1AKP9; Q15511;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 211.
DE   RecName: Full=Spermidine synthase;
DE            Short=SPDSY;
DE            EC=2.5.1.16;
DE   AltName: Full=Putrescine aminopropyltransferase;
GN   Name=SRM; Synonyms=SPS1, SRML1;
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].
RX   PubMed=2344393; DOI=10.1089/dna.1990.9.103;
RA   Wahlfors J., Alhonen L., Kauppinen L., Hyvoenen T., Jaenne J., Eloranta T.;
RT   "Human spermidine synthase: cloning and primary structure.";
RL   DNA Cell Biol. 9:103-110(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2069720; DOI=10.1089/dna.1991.10.467;
RA   Myoehaenen S., Kauppinen L., Wahlfors J., Alhonen L., Jaenne J.;
RT   "Human spermidine synthase gene: structure and chromosomal localization.";
RL   DNA Cell Biol. 10:467-474(1991).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Skin;
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   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEXES WITH SPERMIDINE;
RP   PUTRESCINE; MTA AND S-ADENOSYLMETHIONINAMINE, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=17585781; DOI=10.1021/bi602498k;
RA   Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E.,
RA   Plotnikov A.N.;
RT   "Structure and mechanism of spermidine synthases.";
RL   Biochemistry 46:8331-8339(2007).
CC   -!- FUNCTION: Catalyzes the production of spermidine from putrescine and
CC       decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference
CC       for putrescine as substrate, and has very low activity towards 1,3-
CC       diaminopropane. Has extremely low activity towards spermidine.
CC       {ECO:0000269|PubMed:17585781}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC         S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC         ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC         Evidence={ECO:0000269|PubMed:17585781};
CC   -!- ACTIVITY REGULATION: The activity is thought to be regulated mainly by
CC       the availability of decarboxylated S-adenosylmethionine.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20 uM for putrescine {ECO:0000269|PubMed:17585781};
CC         KM=0.9 uM for S-adenosylmethioninamine {ECO:0000269|PubMed:17585781};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC       spermidine from putrescine: step 1/1.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:17585781}.
CC   -!- INTERACTION:
CC       P19623; P19623: SRM; NbExp=6; IntAct=EBI-1056183, EBI-1056183;
CC       P19623; P54274: TERF1; NbExp=2; IntAct=EBI-1056183, EBI-710997;
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; M34338; AAA36633.1; -; mRNA.
DR   EMBL; M64231; AAA60574.1; -; Genomic_DNA.
DR   EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71675.1; -; Genomic_DNA.
DR   EMBL; BC000309; AAH00309.1; -; mRNA.
DR   EMBL; BC033106; AAH33106.1; -; mRNA.
DR   CCDS; CCDS125.1; -.
DR   PIR; A32610; A32610.
DR   RefSeq; NP_003123.2; NM_003132.2.
DR   PDB; 2O05; X-ray; 2.00 A; A/B=1-302.
DR   PDB; 2O06; X-ray; 2.00 A; A/B=1-302.
DR   PDB; 2O07; X-ray; 1.89 A; A/B=1-302.
DR   PDB; 2O0L; X-ray; 1.99 A; A/B=1-302.
DR   PDB; 3RW9; X-ray; 2.00 A; A/B=1-302.
DR   PDBsum; 2O05; -.
DR   PDBsum; 2O06; -.
DR   PDBsum; 2O07; -.
DR   PDBsum; 2O0L; -.
DR   PDBsum; 3RW9; -.
DR   AlphaFoldDB; P19623; -.
DR   SMR; P19623; -.
DR   BioGRID; 112601; 49.
DR   IntAct; P19623; 12.
DR   STRING; 9606.ENSP00000366156; -.
DR   BindingDB; P19623; -.
DR   ChEMBL; CHEMBL4232; -.
DR   DrugBank; DB00118; Ademetionine.
DR   GlyGen; P19623; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P19623; -.
DR   MetOSite; P19623; -.
DR   PhosphoSitePlus; P19623; -.
DR   SwissPalm; P19623; -.
DR   BioMuta; SRM; -.
DR   DMDM; 134811; -.
DR   EPD; P19623; -.
DR   jPOST; P19623; -.
DR   MassIVE; P19623; -.
DR   MaxQB; P19623; -.
DR   PaxDb; P19623; -.
DR   PeptideAtlas; P19623; -.
DR   PRIDE; P19623; -.
DR   ProteomicsDB; 53682; -.
DR   Antibodypedia; 13673; 256 antibodies from 28 providers.
DR   DNASU; 6723; -.
DR   Ensembl; ENST00000376957.7; ENSP00000366156.2; ENSG00000116649.10.
DR   GeneID; 6723; -.
DR   KEGG; hsa:6723; -.
DR   MANE-Select; ENST00000376957.7; ENSP00000366156.2; NM_003132.3; NP_003123.2.
DR   UCSC; uc001arz.2; human.
DR   CTD; 6723; -.
DR   DisGeNET; 6723; -.
DR   GeneCards; SRM; -.
DR   HGNC; HGNC:11296; SRM.
DR   HPA; ENSG00000116649; Low tissue specificity.
DR   MIM; 182891; gene.
DR   neXtProt; NX_P19623; -.
DR   OpenTargets; ENSG00000116649; -.
DR   PharmGKB; PA36120; -.
DR   VEuPathDB; HostDB:ENSG00000116649; -.
DR   eggNOG; KOG1562; Eukaryota.
DR   GeneTree; ENSGT00870000136521; -.
DR   HOGENOM; CLU_048199_3_1_1; -.
DR   InParanoid; P19623; -.
DR   OMA; LWPGQSF; -.
DR   OrthoDB; 1059849at2759; -.
DR   PhylomeDB; P19623; -.
DR   TreeFam; TF314466; -.
DR   BioCyc; MetaCyc:HS04027-MON; -.
DR   BRENDA; 2.5.1.16; 2681.
DR   PathwayCommons; P19623; -.
DR   Reactome; R-HSA-351202; Metabolism of polyamines.
DR   SABIO-RK; P19623; -.
DR   SignaLink; P19623; -.
DR   UniPathway; UPA00248; UER00314.
DR   BioGRID-ORCS; 6723; 48 hits in 1083 CRISPR screens.
DR   ChiTaRS; SRM; human.
DR   EvolutionaryTrace; P19623; -.
DR   GenomeRNAi; 6723; -.
DR   Pharos; P19623; Tchem.
DR   PRO; PR:P19623; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P19623; protein.
DR   Bgee; ENSG00000116649; Expressed in body of pancreas and 198 other tissues.
DR   ExpressionAtlas; P19623; baseline and differential.
DR   Genevisible; P19623; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0004766; F:spermidine synthase activity; IDA:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 2.30.140.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR030373; PABS_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001045; Spermi_synthase.
DR   InterPro; IPR030668; Spermi_synthase_euk.
DR   InterPro; IPR035246; Spermidine_synt_N.
DR   InterPro; IPR037163; Spermidine_synt_N_sf.
DR   PANTHER; PTHR11558; PTHR11558; 1.
DR   Pfam; PF17284; Spermine_synt_N; 1.
DR   PIRSF; PIRSF000502; Spermidine_synth; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00417; speE; 1.
DR   PROSITE; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Polyamine biosynthesis; Reference proteome;
KW   Spermidine biosynthesis; Transferase.
FT   CHAIN           1..302
FT                   /note="Spermidine synthase"
FT                   /id="PRO_0000156445"
FT   DOMAIN          18..253
FT                   /note="PABS"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         79
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT   BINDING         80
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         104
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         124
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         155..156
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         173..176
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT   BINDING         173
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         241
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   VARIANT         149
FT                   /note="L -> V (in dbSNP:rs1049932)"
FT                   /id="VAR_011807"
FT   CONFLICT        210
FT                   /note="Q -> E (in Ref. 1; AAA36633)"
FT                   /evidence="ECO:0000305"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          31..45
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          47..59
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   TURN            73..76
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           77..88
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           106..111
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           138..141
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           142..145
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           156..161
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          167..173
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           179..185
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           188..196
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          197..208
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   TURN            210..212
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           214..227
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          229..237
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          245..254
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   STRAND          259..261
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           268..273
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           281..286
FT                   /evidence="ECO:0007829|PDB:2O07"
FT   HELIX           292..299
FT                   /evidence="ECO:0007829|PDB:2O07"
SQ   SEQUENCE   302 AA;  33825 MW;  3EF454D886F6425D CRC64;
     MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG
     NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV
     VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP
     AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT
     YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND
     VS
 
 
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