P34897 (GLYM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine hydroxymethyltransferase, mitochondrial
Short name=SHMT
EC=2.1.2.1

Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase

Gene names

Name:

SHMT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.12
Catalytic activity	5,10-methylenetetrahydrofolate + glycine + H2O = tetrahydrofolate + L-serine.
Cofactor	Pyridoxal phosphate.
Pathway	One-carbon metabolism; tetrahydrofolate interconversion.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion. Mitochondrion matrix › mitochondrion nucleoid. Mitochondrion inner membrane Ref.9 Ref.12.
Miscellaneous	In eukaryotes there are two forms of the enzymes: a cytosolic one and a mitochondrial one.
Sequence similarities	Belongs to the SHMT family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane Mitochondrion nucleoid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Methyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-serine biosynthetic process Inferred from electronic annotation. Source: Compara glycine biosynthetic process from serine Inferred from electronic annotation. Source: Compara one-carbon metabolic process Inferred from direct assay PubMed 11516159. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara tetrahydrofolate interconversion Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	microtubule cytoskeleton Inferred from direct assay. Source: HPA mitochondrial inner membrane Inferred from direct assay Ref.12. Source: UniProtKB mitochondrial intermembrane space Inferred from electronic annotation. Source: Compara mitochondrial nucleoid Inferred from direct assay Ref.9. Source: BHF-UCL
Molecular_function	L-allo-threonine aldolase activity Inferred from electronic annotation. Source: Compara amino acid binding Inferred from electronic annotation. Source: Compara chromatin binding Inferred from direct assay Ref.9. Source: UniProtKB glycine hydroxymethyltransferase activity Inferred from direct assay PubMed 17482557Ref.8. Source: UniProtKB methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P34897-1)

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.

Isoform 2 (identifier: P34897-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P34897-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

29

Mitochondrion

Chain

30 – 504

475

Serine hydroxymethyltransferase, mitochondrial

PRO_0000032562

Amino acid modifications

Modified residue

103

1

N6-acetyllysine Ref.10

Modified residue

181

1

N6-acetyllysine Ref.10

Modified residue

196

1

N6-acetyllysine Ref.10

Modified residue

280

1

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

297

1

N6-acetyllysine Ref.10

Modified residue

356

1

N6-acetyllysine Ref.10

Modified residue

464

1

N6-acetyllysine Ref.10

Modified residue

469

1

N6-acetyllysine Ref.10

Modified residue

474

1

N6-acetyllysine Ref.10

Natural variations

Alternative sequence

1 – 21

21

Missing in isoform 3.

VSP_043844

Alternative sequence

199 – 208

10

Missing in isoform 2.

VSP_043088

Experimental info

Sequence conflict

308

1

P → L in AAA63258. Ref.8

Secondary structure

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504

Helix Strand Turn

Details...

Helix

49 – 52

4

Helix

54 – 69

16

Beta strand

70 – 72

3

Helix

82 – 88

7

Helix

91 – 93

3

Helix

111 – 126

16

Turn

131 – 133

3

Beta strand

134 – 137

4

Helix

143 – 154

12

Turn

199 – 201

3

Helix

206 – 216

11

Beta strand

219 – 223

5

Helix

234 – 244

11

Beta strand

247 – 251

5

Helix

253 – 255

3

Helix

256 – 260

5

Helix

267 – 269

3

Beta strand

272 – 280

9

Beta strand

288 – 293

6

Beta strand

295 – 299

5

Beta strand

306 – 308

3

Helix

312 – 319

8

Turn

320 – 323

4

Helix

329 – 343

15

Helix

345 – 367

23

Helix

373 – 375

3

Beta strand

378 – 385

8

Helix

387 – 389

3

Helix

393 – 402

10

Beta strand

408 – 410

3

Beta strand

418 – 420

3

Beta strand

422 – 428

7

Helix

429 – 433

5

Helix

438 – 460

23

Helix

465 – 474

10

Helix

476 – 493

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2000. Version 3. Checksum: 7A13AF741C68FFD6	FASTA	504	55,993
	10 20 30 40 50 60 MLYFSLFWAA RPLQRCGQLV RMAIRAQHSN AAQTQTGEAN RGWTGQESLS DSDPEMWELL 70 80 90 100 110 120 QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ 130 140 150 160 170 180 RRALEAFDLD PAQWGVNVQP YSGSPANLAV YTALLQPHDR IMGLDLPDGG HLTHGYMSDV 190 200 210 220 230 240 KRISATSIFF ESMPYKLNPK TGLIDYNQLA LTARLFRPRL IIAGTSAYAR LIDYARMREV 250 260 270 280 290 300 CDEVKAHLLA DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD 310 320 330 340 350 360 PKTGREIPYT FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLKNARA 370 380 390 400 410 420 MADALLERGY SLVSGGTDNH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT 430 440 450 460 470 480 PGGLRLGAPA LTSRQFREDD FRRVVDFIDE GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ 490 500 RLANLRQRVE QFARAFPMPG FDEH
	Isoform 2 [UniParc]. Checksum: A304DE25F96E942E	FASTA	494	54,863
	10 20 30 40 50 60 MLYFSLFWAA RPLQRCGQLV RMAIRAQHSN AAQTQTGEAN RGWTGQESLS DSDPEMWELL 70 80 90 100 110 120 QREKDRQCRG LELIASENFC SRAALEALGS CLNNKYSEGY PGKRYYGGAE VVDEIELLCQ 130 140 150 160 170 180 RRALEAFDLD PAQWGVNVQP YSGSPANLAV YTALLQPHDR IMGLDLPDGG HLTHGYMSDV 190 200 210 220 230 240 KRISATSIFF ESMPYKLNLA LTARLFRPRL IIAGTSAYAR LIDYARMREV CDEVKAHLLA 250 260 270 280 290 300 DMAHISGLVA AKVIPSPFKH ADIVTTTTHK TLRGARSGLI FYRKGVKAVD PKTGREIPYT 310 320 330 340 350 360 FEDRINFAVF PSLQGGPHNH AIAAVAVALK QACTPMFREY SLQVLKNARA MADALLERGY 370 380 390 400 410 420 SLVSGGTDNH LVLVDLRPKG LDGARAERVL ELVSITANKN TCPGDRSAIT PGGLRLGAPA 430 440 450 460 470 480 LTSRQFREDD FRRVVDFIDE GVNIGLEVKS KTAKLQDFKS FLLKDSETSQ RLANLRQRVE 490 QFARAFPMPG FDEH
	Isoform 3 [UniParc]. Checksum: 9F8925E18D758E65	FASTA	483	53,455
	10 20 30 40 50 60 MAIRAQHSNA AQTQTGEANR GWTGQESLSD SDPEMWELLQ REKDRQCRGL ELIASENFCS 70 80 90 100 110 120 RAALEALGSC LNNKYSEGYP GKRYYGGAEV VDEIELLCQR RALEAFDLDP AQWGVNVQPY 130 140 150 160 170 180 SGSPANLAVY TALLQPHDRI MGLDLPDGGH LTHGYMSDVK RISATSIFFE SMPYKLNPKT 190 200 210 220 230 240 GLIDYNQLAL TARLFRPRLI IAGTSAYARL IDYARMREVC DEVKAHLLAD MAHISGLVAA 250 260 270 280 290 300 KVIPSPFKHA DIVTTTTHKT LRGARSGLIF YRKGVKAVDP KTGREIPYTF EDRINFAVFP 310 320 330 340 350 360 SLQGGPHNHA IAAVAVALKQ ACTPMFREYS LQVLKNARAM ADALLERGYS LVSGGTDNHL 370 380 390 400 410 420 VLVDLRPKGL DGARAERVLE LVSITANKNT CPGDRSAITP GGLRLGAPAL TSRQFREDDF 430 440 450 460 470 480 RRVVDFIDEG VNIGLEVKSK TAKLQDFKSF LLKDSETSQR LANLRQRVEQ FARAFPMPGF DEH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00002520.
IPI00795816.

PIR

B46746.

RefSeq

NP_001159828.1. NM_001166356.1.
NP_001159829.1. NM_001166357.1.
NP_001159830.1. NM_001166358.1.
NP_001159831.1. NM_001166359.1.
NP_005403.2. NM_005412.5.

UniGene

Hs.741179.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OU5	X-ray	2.04	A	17-504	[»]

ProteinModelPortal

P34897.

ModBase

Search...

Protein-protein interaction databases

IntAct

P34897. 15 interactions.

STRING

9606.ENSP00000333667.

PTM databases

PhosphoSite

P34897.

Polymorphism databases

DMDM

6226865.

Proteomic databases

PaxDb

P34897.

PRIDE

P34897.

Protocols and materials databases

DNASU

6472.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000328923; ENSP00000333667; ENSG00000182199.
ENST00000414700; ENSP00000406881; ENSG00000182199.
ENST00000449049; ENSP00000413770; ENSG00000182199.
ENST00000553474; ENSP00000452419; ENSG00000182199.
ENST00000557487; ENSP00000452315; ENSG00000182199.

GeneID

6472.

KEGG

hsa:6472.

UCSC

uc001snf.2. human.

Organism-specific databases

CTD

6472.

GeneCards

GC12P057623.

HGNC

HGNC:10852. SHMT2.

HPA

HPA020543.
HPA020549.

MIM

138450. gene.

neXtProt

NX_P34897.

PharmGKB

PA35755.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0112.

HOGENOM

HOG000239405.

HOVERGEN

HBG002807.

InParanoid

P34897.

KO

K00600.

OMA

GKIDYED.

PhylomeDB

P34897.

Enzyme and pathway databases

BioCyc

MetaCyc:HS00049-MONOMER.

UniPathway

UPA00193.

Gene expression databases

ArrayExpress

P34897.

Bgee

P34897.

CleanEx

HS_SHMT2.

Genevestigator

P34897.

GermOnline

ENSG00000182199. Homo sapiens.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

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]

PANTHER

PTHR11680. PTHR11680. 1 hit.

Pfam

PF00464. SHMT. 1 hit.
[Graphical view]

PIRSF

PIRSF000412. SHMT. 1 hit.

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00096. SHMT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SHMT2. human.

DrugBank

DB00145. Glycine.
DB00114. Pyridoxal Phosphate.
DB00116. Tetrahydrofolic acid.

EvolutionaryTrace

P34897.

GenomeRNAi

6472.

NextBio

25141.

SOURCE

Search...

Entry information

Entry name

GLYM_HUMAN

Accession

Primary (citable) accession number: P34897
Secondary accession number(s): B7Z9F1 , E7EQ19, E7EU43, O00740, Q8N1A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.