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P34897 (GLYM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine hydroxymethyltransferase, mitochondrial

Short name=SHMT
EC=2.1.2.1
Alternative name(s):
Glycine hydroxymethyltransferase
Serine methylase
Gene names
Name:SHMT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. HAMAP-Rule MF_00051

Cofactor

Pyridoxal phosphate.

Pathway

One-carbon metabolism; tetrahydrofolate interconversion. HAMAP-Rule MF_00051

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion. Mitochondrion matrixmitochondrion 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 processOne-carbon metabolism
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
Mitochondrion nucleoid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionTransferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-serine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

glycine biosynthetic process from serine

Inferred from electronic annotation. Source: Ensembl

one-carbon metabolic process

Inferred from direct assay PubMed 11516159. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

tetrahydrofolate interconversion

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

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: Ensembl

mitochondrial matrix

Inferred from direct assay PubMed 11516159Ref.12. Source: UniProtKB

mitochondrial nucleoid

Inferred from direct assay Ref.9. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 17482557. Source: UniProtKB

   Molecular_functionL-allo-threonine aldolase activity

Inferred from electronic annotation. Source: Ensembl

amino acid binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay Ref.9. Source: UniProtKB

glycine hydroxymethyltransferase activity

Inferred from direct assay PubMed 17482557Ref.8. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion HAMAP-Rule MF_00051
Chain30 – 504475Serine hydroxymethyltransferase, mitochondrial HAMAP-Rule MF_00051
PRO_0000032562

Amino acid modifications

Modified residue1031N6-acetyllysine Ref.10
Modified residue1811N6-acetyllysine Ref.10
Modified residue1961N6-acetyllysine Ref.10
Modified residue2801N6-(pyridoxal phosphate)lysine By similarity
Modified residue2971N6-acetyllysine Ref.10
Modified residue3561N6-acetyllysine Ref.10
Modified residue4641N6-acetyllysine Ref.10
Modified residue4691N6-acetyllysine Ref.10
Modified residue4741N6-acetyllysine Ref.10

Natural variations

Alternative sequence1 – 2121Missing in isoform 3.
VSP_043844
Alternative sequence199 – 20810Missing in isoform 2.
VSP_043088

Experimental info

Sequence conflict3081P → L in AAA63258. Ref.8

Secondary structure

.................................................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 30, 2000. Version 3.
Checksum: 7A13AF741C68FFD6

FASTA50455,993
        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 

« Hide

Isoform 2 [UniParc].

Checksum: A304DE25F96E942E
Show »

FASTA49454,863
Isoform 3 [UniParc].

Checksum: 9F8925E18D758E65
Show »

FASTA48353,455

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
CCDSCCDS53805.1. [P34897-3]
CCDS55837.1. [P34897-2]
CCDS8934.1. [P34897-1]
PIRB46746.
RefSeqNP_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]
UniGeneHs.741179.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OU5X-ray2.04A17-504[»]
ProteinModelPortalP34897.
SMRP34897. Positions 42-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112368. 43 interactions.
IntActP34897. 18 interactions.
MINTMINT-3013548.
STRING9606.ENSP00000333667.

Chemistry

DrugBankDB00145. Glycine.
DB00114. Pyridoxal Phosphate.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSiteP34897.

Polymorphism databases

DMDM6226865.

Proteomic databases

MaxQBP34897.
PaxDbP34897.
PRIDEP34897.

Protocols and materials databases

DNASU6472.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328923; ENSP00000333667; ENSG00000182199. [P34897-1]
ENST00000414700; ENSP00000406881; ENSG00000182199. [P34897-3]
ENST00000449049; ENSP00000413770; ENSG00000182199. [P34897-3]
ENST00000553474; ENSP00000452419; ENSG00000182199. [P34897-3]
ENST00000557487; ENSP00000452315; ENSG00000182199. [P34897-2]
GeneID6472.
KEGGhsa:6472.
UCSCuc001snf.2. human. [P34897-1]
uc009zpk.2. human. [P34897-2]

Organism-specific databases

CTD6472.
GeneCardsGC12P057623.
HGNCHGNC:10852. SHMT2.
HPAHPA020543.
HPA020549.
MIM138450. gene.
neXtProtNX_P34897.
PharmGKBPA35755.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0112.
HOGENOMHOG000239405.
HOVERGENHBG002807.
InParanoidP34897.
KOK00600.
OMAPMFREYA.
OrthoDBEOG7327NN.
PhylomeDBP34897.
TreeFamTF314667.

Enzyme and pathway databases

BioCycMetaCyc:HS00049-MONOMER.
UniPathwayUPA00193.

Gene expression databases

ArrayExpressP34897.
BgeeP34897.
CleanExHS_SHMT2.
GenevestigatorP34897.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00051. SHMT.
InterProIPR015424. 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]
PANTHERPTHR11680. PTHR11680. 1 hit.
PfamPF00464. SHMT. 1 hit.
[Graphical view]
PIRSFPIRSF000412. SHMT. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00096. SHMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSHMT2. human.
EvolutionaryTraceP34897.
GenomeRNAi6472.
NextBio25141.
PROP34897.
SOURCESearch...

Entry information

Entry nameGLYM_HUMAN
AccessionPrimary (citable) accession number: P34897
Secondary accession number(s): B7Z9F1 expand/collapse secondary AC list , E7EQ19, E7EU43, O00740, Q8N1A5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM