Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine hydroxymethyltransferase, cytosolic

Gene

SHMT1

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

Functioni

Interconversion of serine and glycine.

Catalytic activityi

5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.

Cofactori

Pathwayi

GO - Molecular functioni

  1. amino acid binding Source: Ensembl
  2. glycine hydroxymethyltransferase activity Source: UniProtKB
  3. L-allo-threonine aldolase activity Source: Ensembl
  4. protein homodimerization activity Source: UniProtKB
  5. pyridoxal phosphate binding Source: UniProtKB

GO - Biological processi

  1. carnitine biosynthetic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. folic acid metabolic process Source: UniProtKB
  4. glycine biosynthetic process from serine Source: Ensembl
  5. L-serine catabolic process Source: UniProtKB
  6. protein homotetramerization Source: Ensembl
  7. protein tetramerization Source: UniProtKB
  8. purine nucleobase biosynthetic process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
  10. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
  11. vitamin metabolic process Source: Reactome
  12. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS11114-MONOMER.
ReactomeiREACT_11167. Metabolism of folate and pterines.
REACT_2125. Carnitine synthesis.
UniPathwayiUPA00193.

Protein family/group databases

MoonProtiP34896.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine hydroxymethyltransferase, cytosolic (EC:2.1.2.1)
Short name:
SHMT
Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase
Gene namesi
Name:SHMT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:10850. SHMT1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. nucleoplasm Source: HPA
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35753.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 483482Serine hydroxymethyltransferase, cytosolicPRO_0000113504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei257 – 2571N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP34896.
PaxDbiP34896.
PRIDEiP34896.

PTM databases

PhosphoSiteiP34896.

Expressioni

Gene expression databases

BgeeiP34896.
CleanExiHS_SHMT1.
ExpressionAtlasiP34896. baseline and differential.
GenevestigatoriP34896.

Organism-specific databases

HPAiHPA023314.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi112366. 36 interactions.
IntActiP34896. 5 interactions.
STRINGi9606.ENSP00000318868.

Structurei

Secondary structure

1
483
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 219Combined sources
Helixi26 – 294Combined sources
Helixi31 – 4616Combined sources
Beta strandi47 – 493Combined sources
Helixi59 – 657Combined sources
Helixi68 – 703Combined sources
Beta strandi80 – 845Combined sources
Helixi87 – 10317Combined sources
Turni108 – 1103Combined sources
Beta strandi111 – 1144Combined sources
Helixi120 – 13112Combined sources
Beta strandi137 – 1415Combined sources
Helixi143 – 1453Combined sources
Helixi149 – 1513Combined sources
Helixi162 – 1665Combined sources
Beta strandi167 – 1726Combined sources
Turni176 – 1783Combined sources
Helixi183 – 19311Combined sources
Beta strandi196 – 2005Combined sources
Helixi211 – 22010Combined sources
Beta strandi224 – 2285Combined sources
Helixi230 – 2323Combined sources
Helixi233 – 2375Combined sources
Helixi244 – 2463Combined sources
Beta strandi249 – 2568Combined sources
Helixi257 – 2593Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi272 – 2765Combined sources
Turni278 – 2803Combined sources
Beta strandi283 – 2853Combined sources
Helixi288 – 2969Combined sources
Turni297 – 3004Combined sources
Helixi306 – 31813Combined sources
Helixi322 – 34423Combined sources
Beta strandi355 – 3628Combined sources
Helixi363 – 3664Combined sources
Helixi370 – 37910Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi400 – 4045Combined sources
Helixi406 – 4105Combined sources
Helixi415 – 43824Combined sources
Helixi445 – 4528Combined sources
Beta strandi453 – 4553Combined sources
Helixi458 – 47215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJ4X-ray2.65A11-480[»]
ProteinModelPortaliP34896.
SMRiP34896. Positions 11-480.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34896.

Family & Domainsi

Sequence similaritiesi

Belongs to the SHMT family.Curated

Phylogenomic databases

eggNOGiCOG0112.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP34896.
KOiK00600.
OMAiQAMTLEF.
OrthoDBiEOG7327NN.
PhylomeDBiP34896.
TreeFamiTF314667.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERiPTHR11680. PTHR11680. 1 hit.
PfamiPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000412. SHMT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00096. SHMT. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P34896-1) [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
MTMPVNGAHK DADLWSSHDK MLAQPLKDSD VEVYNIIKKE SNRQRVGLEL
60 70 80 90 100
IASENFASRA VLEALGSCLN NKYSEGYPGQ RYYGGTEFID ELETLCQKRA
110 120 130 140 150
LQAYKLDPQC WGVNVQPYSG SPANFAVYTA LVEPHGRIMG LDLPDGGHLT
160 170 180 190 200
HGFMTDKKKI SATSIFFESM PYKVNPDTGY INYDQLEENA RLFHPKLIIA
210 220 230 240 250
GTSCYSRNLE YARLRKIADE NGAYLMADMA HISGLVAAGV VPSPFEHCHV
260 270 280 290 300
VTTTTHKTLR GCRAGMIFYR KGVKSVDPKT GKEILYNLES LINSAVFPGL
310 320 330 340 350
QGGPHNHAIA GVAVALKQAM TLEFKVYQHQ VVANCRALSE ALTELGYKIV
360 370 380 390 400
TGGSDNHLIL VDLRSKGTDG GRAEKVLEAC SIACNKNTCP GDRSALRPSG
410 420 430 440 450
LRLGTPALTS RGLLEKDFQK VAHFIHRGIE LTLQIQSDTG VRATLKEFKE
460 470 480
RLAGDKYQAA VQALREEVES FASLFPLPGL PDF
Length:483
Mass (Da):53,083
Last modified:February 1, 1994 - v1
Checksum:i6CDD6CA06D017C19
GO
Isoform 2 (identifier: P34896-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     274-312: Missing.

Note: Contains a N6-acetyllysine at position 271.

Show »
Length:444
Mass (Da):49,028
Checksum:i92091DCEB64B65D1
GO
Isoform 3 (identifier: P34896-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     273-352: Missing.

Show »
Length:403
Mass (Da):44,552
Checksum:i9CE930DFA6FC1FF7
GO
Isoform 4 (identifier: P34896-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.

Note: No experimental confirmation available.

Show »
Length:345
Mass (Da):37,672
Checksum:iDD683D88B3A1D1FA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti340 – 3401E → Q.
Corresponds to variant rs7215148 [ dbSNP | Ensembl ].
VAR_059795
Natural varianti474 – 4741L → F.2 Publications
Corresponds to variant rs1979277 [ dbSNP | Ensembl ].
VAR_022010

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 138138Missing in isoform 4. 1 PublicationVSP_054610Add
BLAST
Alternative sequencei273 – 35280Missing in isoform 3. CuratedVSP_006096Add
BLAST
Alternative sequencei274 – 31239Missing in isoform 2. 1 PublicationVSP_006095Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11931 mRNA. Translation: AAA63257.1.
L23928 mRNA. Translation: AAA36020.1.
L23928 mRNA. Translation: AAA36019.1.
L23928 mRNA. Translation: AAA36018.1.
Y14485 mRNA. Translation: CAB54838.1.
Y14486 mRNA. Translation: CAB54839.1.
Y14487 mRNA. Translation: CAB54840.1.
AK298415 mRNA. Translation: BAG60641.1.
AC127537 Genomic DNA. No translation available.
AL353997 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55637.1.
CH471196 Genomic DNA. Translation: EAW55640.1.
CH471196 Genomic DNA. Translation: EAW55641.1.
BC007979 mRNA. Translation: AAH07979.1.
BC022874 mRNA. Translation: AAH22874.1.
BC038598 mRNA. Translation: AAH38598.1.
CCDSiCCDS11196.1. [P34896-1]
CCDS11197.1. [P34896-2]
CCDS62112.1. [P34896-4]
PIRiA46746.
RefSeqiNP_001268715.1. NM_001281786.1. [P34896-4]
NP_004160.3. NM_004169.4. [P34896-1]
NP_683718.1. NM_148918.2. [P34896-2]
XP_005256824.1. XM_005256767.1. [P34896-1]
UniGeneiHs.513987.
Hs.592944.
Hs.636044.

Genome annotation databases

EnsembliENST00000316694; ENSP00000318868; ENSG00000176974. [P34896-1]
ENST00000352886; ENSP00000345881; ENSG00000176974. [P34896-4]
ENST00000354098; ENSP00000318805; ENSG00000176974. [P34896-2]
GeneIDi6470.
KEGGihsa:6470.
UCSCiuc002gsz.3. human. [P34896-1]
uc002gtb.3. human. [P34896-2]

Polymorphism databases

DMDMi462184.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11931 mRNA. Translation: AAA63257.1.
L23928 mRNA. Translation: AAA36020.1.
L23928 mRNA. Translation: AAA36019.1.
L23928 mRNA. Translation: AAA36018.1.
Y14485 mRNA. Translation: CAB54838.1.
Y14486 mRNA. Translation: CAB54839.1.
Y14487 mRNA. Translation: CAB54840.1.
AK298415 mRNA. Translation: BAG60641.1.
AC127537 Genomic DNA. No translation available.
AL353997 Genomic DNA. No translation available.
CH471196 Genomic DNA. Translation: EAW55637.1.
CH471196 Genomic DNA. Translation: EAW55640.1.
CH471196 Genomic DNA. Translation: EAW55641.1.
BC007979 mRNA. Translation: AAH07979.1.
BC022874 mRNA. Translation: AAH22874.1.
BC038598 mRNA. Translation: AAH38598.1.
CCDSiCCDS11196.1. [P34896-1]
CCDS11197.1. [P34896-2]
CCDS62112.1. [P34896-4]
PIRiA46746.
RefSeqiNP_001268715.1. NM_001281786.1. [P34896-4]
NP_004160.3. NM_004169.4. [P34896-1]
NP_683718.1. NM_148918.2. [P34896-2]
XP_005256824.1. XM_005256767.1. [P34896-1]
UniGeneiHs.513987.
Hs.592944.
Hs.636044.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJ4X-ray2.65A11-480[»]
ProteinModelPortaliP34896.
SMRiP34896. Positions 11-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112366. 36 interactions.
IntActiP34896. 5 interactions.
STRINGi9606.ENSP00000318868.

Chemistry

BindingDBiP34896.
ChEMBLiCHEMBL1772927.
DrugBankiDB00145. Glycine.
DB01055. Mimosine.
DB00116. Tetrahydrofolic acid.

Protein family/group databases

MoonProtiP34896.

PTM databases

PhosphoSiteiP34896.

Polymorphism databases

DMDMi462184.

Proteomic databases

MaxQBiP34896.
PaxDbiP34896.
PRIDEiP34896.

Protocols and materials databases

DNASUi6470.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316694; ENSP00000318868; ENSG00000176974. [P34896-1]
ENST00000352886; ENSP00000345881; ENSG00000176974. [P34896-4]
ENST00000354098; ENSP00000318805; ENSG00000176974. [P34896-2]
GeneIDi6470.
KEGGihsa:6470.
UCSCiuc002gsz.3. human. [P34896-1]
uc002gtb.3. human. [P34896-2]

Organism-specific databases

CTDi6470.
GeneCardsiGC17M018231.
HGNCiHGNC:10850. SHMT1.
HPAiHPA023314.
MIMi182144. gene.
neXtProtiNX_P34896.
PharmGKBiPA35753.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0112.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP34896.
KOiK00600.
OMAiQAMTLEF.
OrthoDBiEOG7327NN.
PhylomeDBiP34896.
TreeFamiTF314667.

Enzyme and pathway databases

UniPathwayiUPA00193.
BioCyciMetaCyc:HS11114-MONOMER.
ReactomeiREACT_11167. Metabolism of folate and pterines.
REACT_2125. Carnitine synthesis.

Miscellaneous databases

ChiTaRSiSHMT1. human.
EvolutionaryTraceiP34896.
GenomeRNAii6470.
NextBioi25133.
PROiP34896.
SOURCEiSearch...

Gene expression databases

BgeeiP34896.
CleanExiHS_SHMT1.
ExpressionAtlasiP34896. baseline and differential.
GenevestigatoriP34896.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00051. SHMT.
InterProiIPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR001085. Ser_HO-MeTrfase.
IPR019798. Ser_HO-MeTrfase_PLP_BS.
[Graphical view]
PANTHERiPTHR11680. PTHR11680. 1 hit.
PfamiPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000412. SHMT. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization."
    Garrow T.A., Brenner A.A., Whitehead M.V., Chen X.-N., Duncan R.G., Korenberg J.R., Shane B.
    J. Biol. Chem. 268:11910-11916(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Xu L., Mangum J.H., Robertson D.L.
    Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Isolation and characterisation of human genomic sequences encoding cytosolic serine hydroxymethyltransferase."
    Chave K.J., Snell K., Sanders P.G.
    Biochem. Soc. Trans. 25:53-53(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary gland.
  4. "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 4).
    Tissue: Liver.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-474.
  7. "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] (ISOFORMS 1 AND 2), VARIANT PHE-474.
    Tissue: Bone marrow, Lymph and Testis.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-271 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy."
    Renwick S.B., Snell K., Baumann U.
    Structure 6:1105-1116(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 11-480.

Entry informationi

Entry nameiGLYC_HUMAN
AccessioniPrimary (citable) accession number: P34896
Secondary accession number(s): B4DPM9
, D3DXD0, Q96HY0, Q9UMD1, Q9UMD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 4, 2015
This is version 157 of the entry and version 1 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

Miscellaneous

In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.