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P52788

- SPSY_HUMAN

UniProt

P52788 - SPSY_HUMAN

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Protein

Spermine synthase

Gene

SMS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).

Catalytic activityi

S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481S-adenosylmethioninamine
Binding sitei177 – 1771Spermidine
Binding sitei201 – 2011Spermidine
Binding sitei220 – 2201S-adenosylmethioninamine
Active sitei276 – 2761Proton acceptorPROSITE-ProRule annotation
Binding sitei351 – 3511Spermidine
Binding sitei353 – 3531Spermidine

GO - Molecular functioni

  1. spermidine synthase activity Source: ProtInc
  2. spermine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. methionine metabolic process Source: ProtInc
  3. polyamine metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. spermine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Polyamine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS02362-MONOMER.
ReactomeiREACT_14820. Metabolism of polyamines.
SABIO-RKP52788.
UniPathwayiUPA00249; UER00315.

Names & Taxonomyi

Protein namesi
Recommended name:
Spermine synthase (EC:2.5.1.22)
Short name:
SPMSY
Alternative name(s):
Spermidine aminopropyltransferase
Gene namesi
Name:SMS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11123. SMS.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

X-linked syndromic mental retardation Snyder-Robinson type (MRXSSR) [MIM:309583]: Characterized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry. Transmission is X-linked recessive.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011D → A or N: 100,000-fold decrease in catalytic efficiency. 1 Publication
Mutagenesisi276 – 2761D → N: 200,000-fold decrease in catalytic efficiency. 1 Publication
Mutagenesisi353 – 3531E → Q: 800-fold decrease in catalytic efficiency. 1 Publication

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi309583. phenotype.
Orphaneti3063. X-linked intellectual disability, Snyder type.
PharmGKBiPA35972.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 366365Spermine synthasePRO_0000156538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP52788.
PaxDbiP52788.
PRIDEiP52788.

2D gel databases

OGPiP52788.

PTM databases

PhosphoSiteiP52788.

Expressioni

Gene expression databases

BgeeiP52788.
CleanExiHS_SMS.
GenevestigatoriP52788.

Organism-specific databases

HPAiHPA029849.
HPA029852.

Interactioni

Subunit structurei

Homodimer. Dimerization is mediated through the N-terminal domain and seems to be required for activity as deletion of the N-terminal domain causes complete loss of activity.1 Publication

Protein-protein interaction databases

BioGridi112495. 29 interactions.
IntActiP52788. 6 interactions.
MINTiMINT-5002620.
STRINGi9606.ENSP00000385746.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Helixi21 – 3212Combined sources
Beta strandi36 – 427Combined sources
Turni43 – 453Combined sources
Beta strandi46 – 527Combined sources
Beta strandi58 – 636Combined sources
Beta strandi67 – 759Combined sources
Helixi85 – 9814Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi136 – 1449Combined sources
Beta strandi149 – 1557Combined sources
Turni156 – 1583Combined sources
Beta strandi159 – 1646Combined sources
Beta strandi167 – 1715Combined sources
Helixi175 – 1817Combined sources
Turni182 – 1854Combined sources
Beta strandi193 – 1986Combined sources
Helixi203 – 2097Combined sources
Beta strandi214 – 2218Combined sources
Helixi223 – 23210Combined sources
Helixi234 – 2374Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi249 – 2546Combined sources
Helixi256 – 26611Combined sources
Beta strandi270 – 2767Combined sources
Helixi291 – 30414Combined sources
Beta strandi306 – 31813Combined sources
Helixi322 – 33211Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi339 – 3468Combined sources
Helixi349 – 3513Combined sources
Beta strandi355 – 3628Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C6KX-ray1.95A/B/C/D5-366[»]
3C6MX-ray2.45A/B/C/D5-366[»]
ProteinModelPortaliP52788.
SMRiP52788. Positions 3-365.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 362241PABSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni255 – 2562S-adenosylmethioninamine binding

Domaini

Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity.

Sequence similaritiesi

Contains 1 PABS (polyamine biosynthesis) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG259013.
GeneTreeiENSGT00620000088036.
HOGENOMiHOG000007053.
HOVERGENiHBG004512.
InParanoidiP52788.
KOiK00802.
OMAiEGRMFDY.
OrthoDBiEOG7G1V6F.
PhylomeDBiP52788.
TreeFamiTF324508.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases-like.
IPR001045. Spermidine/spermine_synthase.
IPR015576. Spermine_synthase_animal.
[Graphical view]
PANTHERiPTHR11558. PTHR11558. 1 hit.
PTHR11558:SF27. PTHR11558:SF27. 1 hit.
PfamiPF01564. Spermine_synth. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52788-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAARHSTLD FMLGAKADGE TILKGLQSIF QEQGMAESVH TWQDHGYLAT
60 70 80 90 100
YTNKNGSFAN LRIYPHGLVL LDLQSYDGDA QGKEEIDSIL NKVEERMKEL
110 120 130 140 150
SQDSTGRVKR LPPIVRGGAI DRYWPTADGR LVEYDIDEVV YDEDSPYQNI
160 170 180 190 200
KILHSKQFGN ILILSGDVNL AESDLAYTRA IMGSGKEDYT GKDVLILGGG
210 220 230 240 250
DGGILCEIVK LKPKMVTMVE IDQMVIDGCK KYMRKTCGDV LDNLKGDCYQ
260 270 280 290 300
VLIEDCIPVL KRYAKEGREF DYVINDLTAV PISTSPEEDS TWEFLRLILD
310 320 330 340 350
LSMKVLKQDG KYFTQGNCVN LTEALSLYEE QLGRLYCPVE FSKEIVCVPS
360
YLELWVFYTV WKKAKP
Length:366
Mass (Da):41,268
Last modified:May 30, 2000 - v2
Checksum:iD5B23EF61DE66443
GO
Isoform 2 (identifier: P52788-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-109: Missing.

Note: Gene prediction confirmed by EST data.

Show »
Length:313
Mass (Da):35,278
Checksum:i7D237FC4CD55D3E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → MPG in CAA88921. (PubMed:7546290)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601N → S.1 Publication
VAR_071048

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei57 – 10953Missing in isoform 2. CuratedVSP_034406Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49099 mRNA. Translation: CAA88921.1.
AD001528 mRNA. Translation: AAB61308.1.
AK313834 mRNA. Translation: BAG36567.1.
U53331 Genomic DNA. Translation: AAD08634.1.
U73023 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98984.1.
BC009898 mRNA. Translation: AAH09898.1.
BC085621 mRNA. Translation: AAH85621.1.
CCDSiCCDS14203.1. [P52788-1]
CCDS59161.1. [P52788-2]
PIRiS54160.
RefSeqiNP_001245352.1. NM_001258423.1. [P52788-2]
NP_004586.2. NM_004595.4. [P52788-1]
UniGeneiHs.724874.

Genome annotation databases

EnsembliENST00000379404; ENSP00000368714; ENSG00000102172. [P52788-2]
ENST00000404933; ENSP00000385746; ENSG00000102172. [P52788-1]
GeneIDi6611.
KEGGihsa:6611.
UCSCiuc004dag.4. human. [P52788-1]
uc031tgx.1. human. [P52788-2]

Polymorphism databases

DMDMi8247960.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z49099 mRNA. Translation: CAA88921.1 .
AD001528 mRNA. Translation: AAB61308.1 .
AK313834 mRNA. Translation: BAG36567.1 .
U53331 Genomic DNA. Translation: AAD08634.1 .
U73023 Genomic DNA. No translation available.
CH471074 Genomic DNA. Translation: EAW98984.1 .
BC009898 mRNA. Translation: AAH09898.1 .
BC085621 mRNA. Translation: AAH85621.1 .
CCDSi CCDS14203.1. [P52788-1 ]
CCDS59161.1. [P52788-2 ]
PIRi S54160.
RefSeqi NP_001245352.1. NM_001258423.1. [P52788-2 ]
NP_004586.2. NM_004595.4. [P52788-1 ]
UniGenei Hs.724874.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3C6K X-ray 1.95 A/B/C/D 5-366 [» ]
3C6M X-ray 2.45 A/B/C/D 5-366 [» ]
ProteinModelPortali P52788.
SMRi P52788. Positions 3-365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112495. 29 interactions.
IntActi P52788. 6 interactions.
MINTi MINT-5002620.
STRINGi 9606.ENSP00000385746.

Chemistry

BindingDBi P52788.
ChEMBLi CHEMBL4934.
DrugBanki DB00127. Spermine.

PTM databases

PhosphoSitei P52788.

Polymorphism databases

DMDMi 8247960.

2D gel databases

OGPi P52788.

Proteomic databases

MaxQBi P52788.
PaxDbi P52788.
PRIDEi P52788.

Protocols and materials databases

DNASUi 6611.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379404 ; ENSP00000368714 ; ENSG00000102172 . [P52788-2 ]
ENST00000404933 ; ENSP00000385746 ; ENSG00000102172 . [P52788-1 ]
GeneIDi 6611.
KEGGi hsa:6611.
UCSCi uc004dag.4. human. [P52788-1 ]
uc031tgx.1. human. [P52788-2 ]

Organism-specific databases

CTDi 6611.
GeneCardsi GC0XP021958.
GeneReviewsi SMS.
HGNCi HGNC:11123. SMS.
HPAi HPA029849.
HPA029852.
MIMi 300105. gene.
309583. phenotype.
neXtProti NX_P52788.
Orphaneti 3063. X-linked intellectual disability, Snyder type.
PharmGKBi PA35972.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259013.
GeneTreei ENSGT00620000088036.
HOGENOMi HOG000007053.
HOVERGENi HBG004512.
InParanoidi P52788.
KOi K00802.
OMAi EGRMFDY.
OrthoDBi EOG7G1V6F.
PhylomeDBi P52788.
TreeFami TF324508.

Enzyme and pathway databases

UniPathwayi UPA00249 ; UER00315 .
BioCyci MetaCyc:HS02362-MONOMER.
Reactomei REACT_14820. Metabolism of polyamines.
SABIO-RK P52788.

Miscellaneous databases

EvolutionaryTracei P52788.
GeneWikii SMS_(gene).
GenomeRNAii 6611.
NextBioi 25739.
PROi P52788.
SOURCEi Search...

Gene expression databases

Bgeei P52788.
CleanExi HS_SMS.
Genevestigatori P52788.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR029063. SAM-dependent_MTases-like.
IPR001045. Spermidine/spermine_synthase.
IPR015576. Spermine_synthase_animal.
[Graphical view ]
PANTHERi PTHR11558. PTHR11558. 1 hit.
PTHR11558:SF27. PTHR11558:SF27. 1 hit.
Pfami PF01564. Spermine_synth. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Sequence analysis of 139 kb in Xp22.1 containing spermine synthase and the 5' region of PEX."
    Grieff M., Whyte M.P., Thakker R.V., Mazzarella R.
    Genomics 44:227-231(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney and Skin.
  7. Eloranta T., Kajander O., Kauppinen L., Hyvoenen T., Linnala-Kankkunen A., Kalkkinen N., Kulomaa M., Alhonen L., Jaenne J.
    (In) Goldemberg S.H., Algranati I.D. (eds.); Proceedings of the international symposium on the biology and chemistry of polyamines, pp.91-98, ICSU Press, New York (1988)
    Cited for: PARTIAL PROTEIN SEQUENCE.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-107 (ISOFORM 1).
    Tissue: Platelet.
  9. Cited for: INVOLVEMENT IN MRXSSR.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Crystal structure of human spermine synthase: implications of substrate binding and catalytic mechanism."
    Wu H., Min J., Zeng H., McCloskey D.E., Ikeguchi Y., Loppnau P., Michael A.J., Pegg A.E., Plotnikov A.N.
    J. Biol. Chem. 283:16135-16146(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-366 (ISOFORM 1) IN COMPLEX WITH SPERMIDINE AND 5-METHYLTHIOADENOSINE, SUBUNIT, MUTAGENESIS OF ASP-201; ASP-276 AND GLU-353.
  14. "De novo loss-of-function mutations in SETD5, encoding a methyltransferase in a 3p25 microdeletion syndrome critical region, cause intellectual disability."
    UK10K Consortium
    Grozeva D., Carss K., Spasic-Boskovic O., Parker M.J., Archer H., Firth H.V., Park S.M., Canham N., Holder S.E., Wilson M., Hackett A., Field M., Floyd J.A., Hurles M., Raymond F.L.
    Am. J. Hum. Genet. 94:618-624(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-60.

Entry informationi

Entry nameiSPSY_HUMAN
AccessioniPrimary (citable) accession number: P52788
Secondary accession number(s): A6NHA7
, A6NI34, B2R9M0, O00544, Q9UQS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3