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P34897

- GLYM_HUMAN

UniProt

P34897 - GLYM_HUMAN

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Protein

Serine hydroxymethyltransferase, mitochondrial

Gene

SHMT2

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

Functioni

Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA.1 Publication

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. glycine biosynthetic process from serine Source: Ensembl
  2. L-serine biosynthetic process Source: Ensembl
  3. one-carbon metabolic process Source: UniProtKB
  4. positive regulation of cell proliferation Source: Ensembl
  5. protein homotetramerization Source: Ensembl
  6. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS00049-MONOMER.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine hydroxymethyltransferase, mitochondrial (EC:2.1.2.1)
Short name:
SHMT
Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase
Gene namesi
Name:SHMT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:10852. SHMT2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. microtubule cytoskeleton Source: HPA
  3. mitochondrial inner membrane Source: UniProtKB
  4. mitochondrial intermembrane space Source: Ensembl
  5. mitochondrial matrix Source: UniProtKB
  6. mitochondrial nucleoid Source: BHF-UCL
  7. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion nucleoid

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionAdd
BLAST
Chaini30 – 504475Serine hydroxymethyltransferase, mitochondrialPRO_0000032562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031N6-acetyllysine1 Publication
Modified residuei181 – 1811N6-acetyllysine1 Publication
Modified residuei196 – 1961N6-acetyllysine1 Publication
Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei297 – 2971N6-acetyllysine1 Publication
Modified residuei356 – 3561N6-acetyllysine1 Publication
Modified residuei464 – 4641N6-acetyllysine1 Publication
Modified residuei469 – 4691N6-acetyllysine1 Publication
Modified residuei474 – 4741N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP34897.
PaxDbiP34897.
PRIDEiP34897.

PTM databases

PhosphoSiteiP34897.

Expressioni

Gene expression databases

BgeeiP34897.
CleanExiHS_SHMT2.
ExpressionAtlasiP34897. baseline and differential.
GenevestigatoriP34897.

Organism-specific databases

HPAiHPA020543.
HPA020549.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi112368. 44 interactions.
IntActiP34897. 18 interactions.
MINTiMINT-3013548.
STRINGi9606.ENSP00000333667.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi49 – 524
Helixi54 – 6916
Beta strandi70 – 723
Helixi82 – 887
Helixi91 – 933
Helixi111 – 12616
Turni131 – 1333
Beta strandi134 – 1374
Helixi143 – 15412
Turni199 – 2013
Helixi206 – 21611
Beta strandi219 – 2235
Helixi234 – 24411
Beta strandi247 – 2515
Helixi253 – 2553
Helixi256 – 2605
Helixi267 – 2693
Beta strandi272 – 2809
Beta strandi288 – 2936
Beta strandi295 – 2995
Beta strandi306 – 3083
Helixi312 – 3198
Turni320 – 3234
Helixi329 – 34315
Helixi345 – 36723
Helixi373 – 3753
Beta strandi378 – 3858
Helixi387 – 3893
Helixi393 – 40210
Beta strandi408 – 4103
Beta strandi418 – 4203
Beta strandi422 – 4287
Helixi429 – 4335
Helixi438 – 46023
Helixi465 – 47410
Helixi476 – 49318

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OU5X-ray2.04A17-504[»]
ProteinModelPortaliP34897.
SMRiP34897. Positions 42-504.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34897.

Family & Domainsi

Sequence similaritiesi

Belongs to the SHMT family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0112.
GeneTreeiENSGT00390000002762.
HOGENOMiHOG000239405.
HOVERGENiHBG002807.
InParanoidiP34897.
KOiK00600.
OMAiPMFREYA.
OrthoDBiEOG7327NN.
PhylomeDBiP34897.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P34897-1) [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
MLYFSLFWAA RPLQRCGQLV RMAIRAQHSN AAQTQTGEAN RGWTGQESLS
60 70 80 90 100
DSDPEMWELL QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY
110 120 130 140 150
PGKRYYGGAE VVDEIELLCQ RRALEAFDLD PAQWGVNVQP YSGSPANLAV
160 170 180 190 200
YTALLQPHDR IMGLDLPDGG HLTHGYMSDV KRISATSIFF ESMPYKLNPK
210 220 230 240 250
TGLIDYNQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV CDEVKAHLLA
260 270 280 290 300
DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD
310 320 330 340 350
PKTGREIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY
360 370 380 390 400
SLQVLKNARA MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL
410 420 430 440 450
ELVSITANKN TCPGDRSAIT PGGLRLGAPA LTSRQFREDD FRRVVDFIDE
460 470 480 490 500
GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ RLANLRQRVE QFARAFPMPG

FDEH
Length:504
Mass (Da):55,993
Last modified:May 30, 2000 - v3
Checksum:i7A13AF741C68FFD6
GO
Isoform 2 (identifier: P34897-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     199-208: Missing.

Note: No experimental confirmation available.

Show »
Length:494
Mass (Da):54,863
Checksum:iA304DE25F96E942E
GO
Isoform 3 (identifier: P34897-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Show »
Length:483
Mass (Da):53,455
Checksum:i9F8925E18D758E65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081P → L in AAA63258. (PubMed:8505317)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 3. 1 PublicationVSP_043844Add
BLAST
Alternative sequencei199 – 20810Missing in isoform 2. 1 PublicationVSP_043088

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK315916 mRNA. Translation: BAH14287.1.
BT006866 mRNA. Translation: AAP35512.1.
AC137834 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96994.1.
CH471054 Genomic DNA. Translation: EAW96998.1.
BC011911 mRNA. Translation: AAH11911.1.
BC013677 mRNA. Translation: AAH13677.1.
BC032584 mRNA. Translation: AAH32584.1.
BC044211 mRNA. Translation: AAH44211.1.
Y12331 Genomic DNA. Translation: CAA72999.1.
U23143 Genomic DNA. Translation: AAA64572.1.
L11932 mRNA. Translation: AAA63258.1.
CCDSiCCDS53805.1. [P34897-3]
CCDS55837.1. [P34897-2]
CCDS8934.1. [P34897-1]
PIRiB46746.
RefSeqiNP_001159828.1. NM_001166356.1. [P34897-2]
NP_001159829.1. NM_001166357.1. [P34897-3]
NP_001159830.1. NM_001166358.1. [P34897-3]
NP_001159831.1. NM_001166359.1. [P34897-3]
NP_005403.2. NM_005412.5. [P34897-1]
UniGeneiHs.741179.

Genome annotation databases

EnsembliENST00000328923; ENSP00000333667; ENSG00000182199. [P34897-1]
ENST00000414700; ENSP00000406881; ENSG00000182199. [P34897-3]
ENST00000449049; ENSP00000413770; ENSG00000182199. [P34897-3]
ENST00000553474; ENSP00000452419; ENSG00000182199. [P34897-3]
ENST00000557487; ENSP00000452315; ENSG00000182199. [P34897-2]
GeneIDi6472.
KEGGihsa:6472.
UCSCiuc001snf.2. human. [P34897-1]
uc009zpk.2. human. [P34897-2]

Polymorphism databases

DMDMi6226865.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK315916 mRNA. Translation: BAH14287.1 .
BT006866 mRNA. Translation: AAP35512.1 .
AC137834 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96994.1 .
CH471054 Genomic DNA. Translation: EAW96998.1 .
BC011911 mRNA. Translation: AAH11911.1 .
BC013677 mRNA. Translation: AAH13677.1 .
BC032584 mRNA. Translation: AAH32584.1 .
BC044211 mRNA. Translation: AAH44211.1 .
Y12331 Genomic DNA. Translation: CAA72999.1 .
U23143 Genomic DNA. Translation: AAA64572.1 .
L11932 mRNA. Translation: AAA63258.1 .
CCDSi CCDS53805.1. [P34897-3 ]
CCDS55837.1. [P34897-2 ]
CCDS8934.1. [P34897-1 ]
PIRi B46746.
RefSeqi NP_001159828.1. NM_001166356.1. [P34897-2 ]
NP_001159829.1. NM_001166357.1. [P34897-3 ]
NP_001159830.1. NM_001166358.1. [P34897-3 ]
NP_001159831.1. NM_001166359.1. [P34897-3 ]
NP_005403.2. NM_005412.5. [P34897-1 ]
UniGenei Hs.741179.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OU5 X-ray 2.04 A 17-504 [» ]
ProteinModelPortali P34897.
SMRi P34897. Positions 42-504.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112368. 44 interactions.
IntActi P34897. 18 interactions.
MINTi MINT-3013548.
STRINGi 9606.ENSP00000333667.

Chemistry

DrugBanki DB00145. Glycine.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSitei P34897.

Polymorphism databases

DMDMi 6226865.

Proteomic databases

MaxQBi P34897.
PaxDbi P34897.
PRIDEi P34897.

Protocols and materials databases

DNASUi 6472.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328923 ; ENSP00000333667 ; ENSG00000182199 . [P34897-1 ]
ENST00000414700 ; ENSP00000406881 ; ENSG00000182199 . [P34897-3 ]
ENST00000449049 ; ENSP00000413770 ; ENSG00000182199 . [P34897-3 ]
ENST00000553474 ; ENSP00000452419 ; ENSG00000182199 . [P34897-3 ]
ENST00000557487 ; ENSP00000452315 ; ENSG00000182199 . [P34897-2 ]
GeneIDi 6472.
KEGGi hsa:6472.
UCSCi uc001snf.2. human. [P34897-1 ]
uc009zpk.2. human. [P34897-2 ]

Organism-specific databases

CTDi 6472.
GeneCardsi GC12P057623.
HGNCi HGNC:10852. SHMT2.
HPAi HPA020543.
HPA020549.
MIMi 138450. gene.
neXtProti NX_P34897.
PharmGKBi PA35755.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0112.
GeneTreei ENSGT00390000002762.
HOGENOMi HOG000239405.
HOVERGENi HBG002807.
InParanoidi P34897.
KOi K00600.
OMAi PMFREYA.
OrthoDBi EOG7327NN.
PhylomeDBi P34897.
TreeFami TF314667.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BioCyci MetaCyc:HS00049-MONOMER.

Miscellaneous databases

ChiTaRSi SHMT2. human.
EvolutionaryTracei P34897.
GenomeRNAii 6472.
NextBioi 25141.
PROi P34897.
SOURCEi Search...

Gene expression databases

Bgeei P34897.
CleanExi HS_SHMT2.
ExpressionAtlasi P34897. baseline and differential.
Genevestigatori P34897.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_00051. SHMT.
InterProi IPR015424. 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 ]
PANTHERi PTHR11680. PTHR11680. 1 hit.
Pfami PF00464. SHMT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000412. SHMT. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00096. SHMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 3).
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Lymph, Muscle, Ovary and Uterus.
  6. "The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase."
    Snell K., Baumann U., Byrne P.C., Chave K.J., Renwick S.B., Sanders P.G., Whitehouse S.K.
    Adv. Enzyme Regul. 40:353-403(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
  7. "Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene."
    Stover P.J., Chen L.H., Suh J.R., Stover D.M., Keyomarsi K., Shane B.
    J. Biol. Chem. 272:1842-1848(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-504.
  8. "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] OF 31-504 (ISOFORM 1).
  9. "The layered structure of human mitochondrial DNA nucleoids."
    Bogenhagen D.F., Rousseau D., Burke S.
    J. Biol. Chem. 283:3665-3675(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH MITOCHONDRIAL DNA, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "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-103; LYS-181; LYS-196; LYS-297; LYS-356; LYS-464; LYS-469 AND LYS-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria."
    Anderson D.D., Quintero C.M., Stover P.J.
    Proc. Natl. Acad. Sci. U.S.A. 108:15163-15168(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Crystal structure of human mitochondrial serine hydroxymethyltransferase 2."
    Structural genomics consortium (SGC)
    Submitted (OCT-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 17-504.

Entry informationi

Entry nameiGLYM_HUMAN
AccessioniPrimary (citable) accession number: P34897
Secondary accession number(s): B7Z9F1
, E7EQ19, E7EU43, O00740, Q8N1A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 155 of the entry and version 3 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3