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Protein

S-adenosylmethionine synthase isoform type-2

Gene

MAT2A

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

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP.

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K(+)By similarityNote: Binds 1 potassium ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311MagnesiumBy similarity
Metal bindingi57 – 571PotassiumBy similarity
Binding sitei159 – 1591ATPSequence Analysis
Metal bindingi283 – 2831PotassiumBy similarity
Metal bindingi291 – 2911MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1366ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methionine adenosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. methylation Source: Reactome
  2. one-carbon metabolic process Source: UniProtKB-KW
  3. S-adenosylmethionine biosynthetic process Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
  5. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDAi2.5.1.6. 2681.
ReactomeiREACT_6946. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.6)
Short name:
AdoMet synthase 2
Alternative name(s):
Methionine adenosyltransferase 2
Short name:
MAT 2
Methionine adenosyltransferase II
Short name:
MAT-II
Gene namesi
Name:MAT2A
Synonyms:AMS2, MATA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6904. MAT2A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. methionine adenosyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30647.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395S-adenosylmethionine synthase isoform type-2PRO_0000174435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811N6-acetyllysine1 Publication
Modified residuei114 – 1141Phosphoserine1 Publication

Post-translational modificationi

The alpha' subunit is a post-translationally modified version of MAT2A.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP31153.
PaxDbiP31153.
PeptideAtlasiP31153.
PRIDEiP31153.

2D gel databases

REPRODUCTION-2DPAGEIPI00010157.

PTM databases

PhosphoSiteiP31153.

Expressioni

Gene expression databases

BgeeiP31153.
CleanExiHS_MAT2A.
ExpressionAtlasiP31153. baseline and differential.
GenevestigatoriP31153.

Organism-specific databases

HPAiCAB009968.
HPA043028.

Interactioni

Subunit structurei

Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).1 Publication

Protein-protein interaction databases

BioGridi110314. 26 interactions.
IntActiP31153. 17 interactions.
STRINGi9606.ENSP00000303147.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 259Combined sources
Helixi30 – 4819Combined sources
Beta strandi53 – 619Combined sources
Beta strandi64 – 729Combined sources
Helixi79 – 9012Combined sources
Helixi95 – 973Combined sources
Turni101 – 1033Combined sources
Beta strandi104 – 1118Combined sources
Helixi115 – 1217Combined sources
Turni122 – 1243Combined sources
Helixi127 – 1293Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi136 – 1438Combined sources
Helixi152 – 16918Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi176 – 19116Combined sources
Beta strandi194 – 20916Combined sources
Beta strandi211 – 2133Combined sources
Helixi215 – 22410Combined sources
Helixi227 – 2304Combined sources
Helixi233 – 2353Combined sources
Beta strandi241 – 2455Combined sources
Helixi254 – 2563Combined sources
Turni266 – 2738Combined sources
Helixi290 – 30718Combined sources
Beta strandi312 – 3209Combined sources
Beta strandi328 – 3336Combined sources
Helixi342 – 35211Combined sources
Helixi357 – 3648Combined sources
Turni365 – 3673Combined sources
Helixi371 – 3744Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi379 – 3824Combined sources
Helixi386 – 3883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P02X-ray1.21A1-395[»]
4KTTX-ray2.59A/B/C/D1-395[»]
4KTVX-ray3.30A/B/C/D1-395[»]
4NDNX-ray2.34A/B/C/D1-395[»]
ProteinModelPortaliP31153.
SMRiP31153. Positions 16-395.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31153.

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiCOG0192.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiP31153.
KOiK00789.
OMAiGQMNGFH.
OrthoDBiEOG7TF79H.
PhylomeDBiP31153.
TreeFamiTF300511.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P31153-1) [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
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP
60 70 80 90 100
DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD
110 120 130 140 150
YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM
160 170 180 190 200
PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV
210 220 230 240 250
HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF
260 270 280 290 300
VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
310 320 330 340 350
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK
360 370 380 390
KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY
Length:395
Mass (Da):43,661
Last modified:June 30, 1993 - v1
Checksum:i2E7D1B91CC4F7BDD
GO
Isoform 2 (identifier: P31153-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: Missing.
     363-395: Missing.

Note: No experimental confirmation available.

Show »
Length:299
Mass (Da):32,965
Checksum:i3E3903C0EFD85F00
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6363Missing in isoform 2. 1 PublicationVSP_056186Add
BLAST
Alternative sequencei363 – 39533Missing in isoform 2. 1 PublicationVSP_056187Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68836 mRNA. Translation: CAA48726.1.
DQ083239 mRNA. Translation: AAY85355.1.
AK291126 mRNA. Translation: BAF83815.1.
AK297758 mRNA. Translation: BAG60107.1.
AK316411 mRNA. Translation: BAH14782.1.
AC016753 Genomic DNA. Translation: AAY24339.1.
CH471053 Genomic DNA. Translation: EAW99511.1.
CH471053 Genomic DNA. Translation: EAW99513.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.
CCDSiCCDS1977.1. [P31153-1]
PIRiS27257.
RefSeqiNP_005902.1. NM_005911.5. [P31153-1]
UniGeneiHs.516157.

Genome annotation databases

EnsembliENST00000306434; ENSP00000303147; ENSG00000168906. [P31153-1]
ENST00000409017; ENSP00000386353; ENSG00000168906. [P31153-2]
GeneIDi4144.
KEGGihsa:4144.
UCSCiuc002spr.3. human. [P31153-1]

Polymorphism databases

DMDMi400245.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68836 mRNA. Translation: CAA48726.1.
DQ083239 mRNA. Translation: AAY85355.1.
AK291126 mRNA. Translation: BAF83815.1.
AK297758 mRNA. Translation: BAG60107.1.
AK316411 mRNA. Translation: BAH14782.1.
AC016753 Genomic DNA. Translation: AAY24339.1.
CH471053 Genomic DNA. Translation: EAW99511.1.
CH471053 Genomic DNA. Translation: EAW99513.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.
CCDSiCCDS1977.1. [P31153-1]
PIRiS27257.
RefSeqiNP_005902.1. NM_005911.5. [P31153-1]
UniGeneiHs.516157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P02X-ray1.21A1-395[»]
4KTTX-ray2.59A/B/C/D1-395[»]
4KTVX-ray3.30A/B/C/D1-395[»]
4NDNX-ray2.34A/B/C/D1-395[»]
ProteinModelPortaliP31153.
SMRiP31153. Positions 16-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110314. 26 interactions.
IntActiP31153. 17 interactions.
STRINGi9606.ENSP00000303147.

Chemistry

DrugBankiDB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

PTM databases

PhosphoSiteiP31153.

Polymorphism databases

DMDMi400245.

2D gel databases

REPRODUCTION-2DPAGEIPI00010157.

Proteomic databases

MaxQBiP31153.
PaxDbiP31153.
PeptideAtlasiP31153.
PRIDEiP31153.

Protocols and materials databases

DNASUi4144.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306434; ENSP00000303147; ENSG00000168906. [P31153-1]
ENST00000409017; ENSP00000386353; ENSG00000168906. [P31153-2]
GeneIDi4144.
KEGGihsa:4144.
UCSCiuc002spr.3. human. [P31153-1]

Organism-specific databases

CTDi4144.
GeneCardsiGC02P085766.
H-InvDBHIX0117562.
HGNCiHGNC:6904. MAT2A.
HPAiCAB009968.
HPA043028.
MIMi601468. gene.
neXtProtiNX_P31153.
PharmGKBiPA30647.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0192.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiP31153.
KOiK00789.
OMAiGQMNGFH.
OrthoDBiEOG7TF79H.
PhylomeDBiP31153.
TreeFamiTF300511.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BRENDAi2.5.1.6. 2681.
ReactomeiREACT_6946. Methylation.

Miscellaneous databases

ChiTaRSiMAT2A. human.
EvolutionaryTraceiP31153.
GenomeRNAii4144.
NextBioi16276.
PROiP31153.
SOURCEiSearch...

Gene expression databases

BgeeiP31153.
CleanExiHS_MAT2A.
ExpressionAtlasiP31153. baseline and differential.
GenevestigatoriP31153.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase."
    Horikawa S., Tsukada K.
    FEBS Lett. 312:37-41(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  2. "Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia."
    Panayiotidis M.I., Stabler S.P., Ahmad A., Pappa A., Legros L.H. Jr., Hernandez-Saavedra D., Schneider B.K., Allen R.H., Vasiliou V., McCord J.M., Kotb M., White C.W.
    Free Radic. Biol. Med. 40:348-358(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  7. "Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II)."
    LeGros H.L., Halim A.-B., Geller A.M., Kotb M.
    J. Biol. Chem. 275:2359-2366(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMETK2_HUMAN
AccessioniPrimary (citable) accession number: P31153
Secondary accession number(s): A8K511
, B4DN45, D6W5L1, Q53SP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1993
Last sequence update: June 30, 1993
Last modified: March 31, 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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.