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Q02252

- MMSA_HUMAN

UniProt

Q02252 - MMSA_HUMAN

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Protein

Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial

Gene

ALDH6A1

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

Functioni

Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.

Catalytic activityi

2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH.
3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei317 – 3171NucleophilePROSITE-ProRule annotation
Binding sitei417 – 4171NADSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi209 – 2135NADSequence Analysis
Nucleotide bindingi261 – 2666NADSequence Analysis

GO - Molecular functioni

  1. fatty-acyl-CoA binding Source: UniProtKB
  2. malonate-semialdehyde dehydrogenase (acetylating) activity Source: UniProtKB
  3. methylmalonate-semialdehyde dehydrogenase (acylating) activity Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: Reactome
  2. brown fat cell differentiation Source: Ensembl
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. thymine catabolic process Source: BHF-UCL
  6. thymine metabolic process Source: UniProtKB
  7. valine catabolic process Source: BHF-UCL
  8. valine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_197. Branched-chain amino acid catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (EC:1.2.1.18, EC:1.2.1.27)
Short name:
MMSDH
Short name:
Malonate-semialdehyde dehydrogenase [acylating]
Alternative name(s):
Aldehyde dehydrogenase family 6 member A1
Gene namesi
Name:ALDH6A1
Synonyms:MMSDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:7179. ALDH6A1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Methylmalonate semialdehyde dehydrogenase deficiency (MMSDHD) [MIM:614105]: A metabolic disorder characterized by elevated beta-alanine, 3-hydroxypropionic acid, and both isomers of 3-amino and 3-hydroxyisobutyric acids in urine organic acids.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti446 – 4461G → R in MMSDHD. 1 Publication
VAR_010244

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614105. phenotype.
Orphaneti289307. Developmental delay due to methylmalonate semialdehyde dehydrogenase deficiency.
PharmGKBiPA24703.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 535502Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrialPRO_0000007189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471N6-acetyllysine; alternateBy similarity
Modified residuei47 – 471N6-succinyllysine; alternateBy similarity
Modified residuei52 – 521N6-acetyllysine; alternateBy similarity
Modified residuei52 – 521N6-succinyllysine; alternateBy similarity
Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
Modified residuei87 – 871N6-acetyllysineBy similarity
Modified residuei117 – 1171N6-acetyllysine; alternateBy similarity
Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei298 – 2981N6-acetyllysineBy similarity
Modified residuei330 – 3301N6-acetyllysineBy similarity
Modified residuei331 – 3311N6-acetyllysineBy similarity
Modified residuei364 – 3641N6-acetyllysine; alternateBy similarity
Modified residuei364 – 3641N6-succinyllysine; alternateBy similarity
Modified residuei376 – 3761N6-acetyllysine; alternateBy similarity
Modified residuei376 – 3761N6-succinyllysine; alternateBy similarity
Modified residuei391 – 3911N6-succinyllysineBy similarity
Modified residuei500 – 5001N6-acetyllysineBy similarity
Modified residuei517 – 5171N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ02252.
PaxDbiQ02252.
PeptideAtlasiQ02252.
PRIDEiQ02252.

2D gel databases

REPRODUCTION-2DPAGEIPI00024990.
UCD-2DPAGEQ02252.

PTM databases

PhosphoSiteiQ02252.

Expressioni

Gene expression databases

BgeeiQ02252.
CleanExiHS_ALDH6A1.
ExpressionAtlasiQ02252. baseline and differential.
GenevestigatoriQ02252.

Organism-specific databases

HPAiHPA029072.
HPA029073.
HPA029074.
HPA029075.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi110472. 4 interactions.
IntActiQ02252. 2 interactions.
STRINGi9606.ENSP00000342564.

Structurei

3D structure databases

ProteinModelPortaliQ02252.
SMRiQ02252. Positions 40-516.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00770000120629.
HOGENOMiHOG000271507.
HOVERGENiHBG105023.
InParanoidiQ02252.
KOiK00140.
OMAiQVVEHCC.
OrthoDBiEOG7J70F8.
PhylomeDBiQ02252.
TreeFamiTF105651.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010061. MeMal-semiAld_DH.
[Graphical view]
PANTHERiPTHR11699:SF27. PTHR11699:SF27. 1 hit.
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01722. MMSDH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q02252-1) [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
MAALLAAAAV RARILQVSSK VKSSPTWYSA SSFSSSVPTV KLFIGGKFVE
60 70 80 90 100
SKSDKWIDIH NPATNEVIGR VPQATKAEMD AAIASCKRAF PAWADTSVLS
110 120 130 140 150
RQQVLLRYQQ LIKENLKEIA KLITLEQGKT LADAEGDVFR GLQVVEHACS
160 170 180 190 200
VTSLMMGETM PSITKDMDLY SYRLPLGVCA GIAPFNFPAM IPLWMFPMAM
210 220 230 240 250
VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG QHEAVNFICD
260 270 280 290 300
HPDIKAISFV GSNKAGEYIF ERGSRHGKRV QANMGAKNHG VVMPDANKEN
310 320 330 340 350
TLNQLVGAAF GAAGQRCMAL STAVLVGEAK KWLPELVEHA KNLRVNAGDQ
360 370 380 390 400
PGADLGPLIT PQAKERVCNL IDSGTKEGAS ILLDGRKIKV KGYENGNFVG
410 420 430 440 450
PTIISNVKPN MTCYKEEIFG PVLVVLETET LDEAIQIVNN NPYGNGTAIF
460 470 480 490 500
TTNGATARKY AHLVDVGQVG VNVPIPVPLP MFSFTGSRSS FRGDTNFYGK
510 520 530
QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR
Length:535
Mass (Da):57,840
Last modified:January 24, 2001 - v2
Checksum:i0786AF63897E7962
GO
Isoform 2 (identifier: Q02252-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-116: Missing.

Show »
Length:522
Mass (Da):56,228
Checksum:iFBAB6B1DA77B3ADB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011R → C in BAG57539. (PubMed:14702039)Curated
Sequence conflicti212 – 2121E → K in BAG57539. (PubMed:14702039)Curated
Sequence conflicti460 – 4601Y → H in BAG57539. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti446 – 4461G → R in MMSDHD. 1 Publication
VAR_010244

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei104 – 11613Missing in isoform 2. 1 PublicationVSP_055067Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249994 mRNA. Translation: CAB76468.1.
AF159889 mRNA. Translation: AAF80380.1.
AF148505 mRNA. Translation: AAF04489.1.
AF148855 Genomic DNA. Translation: AAG29581.1.
AK312389 mRNA. Translation: BAG35306.1.
AK294243 mRNA. Translation: BAG57539.1.
AC005484 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81159.1.
BC004909 mRNA. Translation: AAH04909.1.
BC032371 mRNA. Translation: AAH32371.1.
M93405 mRNA. Translation: AAA36328.1.
CCDSiCCDS61501.1. [Q02252-2]
CCDS9826.1. [Q02252-1]
RefSeqiNP_001265522.1. NM_001278593.1. [Q02252-2]
NP_005580.1. NM_005589.3. [Q02252-1]
UniGeneiHs.293970.
Hs.744472.

Genome annotation databases

EnsembliENST00000350259; ENSP00000342564; ENSG00000119711. [Q02252-2]
ENST00000553458; ENSP00000450436; ENSG00000119711. [Q02252-1]
GeneIDi4329.
KEGGihsa:4329.
UCSCiuc001xpo.3. human. [Q02252-1]

Polymorphism databases

DMDMi12643424.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ249994 mRNA. Translation: CAB76468.1 .
AF159889 mRNA. Translation: AAF80380.1 .
AF148505 mRNA. Translation: AAF04489.1 .
AF148855 Genomic DNA. Translation: AAG29581.1 .
AK312389 mRNA. Translation: BAG35306.1 .
AK294243 mRNA. Translation: BAG57539.1 .
AC005484 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81159.1 .
BC004909 mRNA. Translation: AAH04909.1 .
BC032371 mRNA. Translation: AAH32371.1 .
M93405 mRNA. Translation: AAA36328.1 .
CCDSi CCDS61501.1. [Q02252-2 ]
CCDS9826.1. [Q02252-1 ]
RefSeqi NP_001265522.1. NM_001278593.1. [Q02252-2 ]
NP_005580.1. NM_005589.3. [Q02252-1 ]
UniGenei Hs.293970.
Hs.744472.

3D structure databases

ProteinModelPortali Q02252.
SMRi Q02252. Positions 40-516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110472. 4 interactions.
IntActi Q02252. 2 interactions.
STRINGi 9606.ENSP00000342564.

PTM databases

PhosphoSitei Q02252.

Polymorphism databases

DMDMi 12643424.

2D gel databases

REPRODUCTION-2DPAGE IPI00024990.
UCD-2DPAGE Q02252.

Proteomic databases

MaxQBi Q02252.
PaxDbi Q02252.
PeptideAtlasi Q02252.
PRIDEi Q02252.

Protocols and materials databases

DNASUi 4329.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000350259 ; ENSP00000342564 ; ENSG00000119711 . [Q02252-2 ]
ENST00000553458 ; ENSP00000450436 ; ENSG00000119711 . [Q02252-1 ]
GeneIDi 4329.
KEGGi hsa:4329.
UCSCi uc001xpo.3. human. [Q02252-1 ]

Organism-specific databases

CTDi 4329.
GeneCardsi GC14M074527.
HGNCi HGNC:7179. ALDH6A1.
HPAi HPA029072.
HPA029073.
HPA029074.
HPA029075.
MIMi 603178. gene.
614105. phenotype.
neXtProti NX_Q02252.
Orphaneti 289307. Developmental delay due to methylmalonate semialdehyde dehydrogenase deficiency.
PharmGKBi PA24703.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00770000120629.
HOGENOMi HOG000271507.
HOVERGENi HBG105023.
InParanoidi Q02252.
KOi K00140.
OMAi QVVEHCC.
OrthoDBi EOG7J70F8.
PhylomeDBi Q02252.
TreeFami TF105651.

Enzyme and pathway databases

Reactomei REACT_197. Branched-chain amino acid catabolism.

Miscellaneous databases

GeneWikii Aldehyde_dehydrogenase_6_family,_member_A1.
GenomeRNAii 4329.
NextBioi 17035.
PROi Q02252.
SOURCEi Search...

Gene expression databases

Bgeei Q02252.
CleanExi HS_ALDH6A1.
ExpressionAtlasi Q02252. baseline and differential.
Genevestigatori Q02252.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010061. MeMal-semiAld_DH.
[Graphical view ]
PANTHERi PTHR11699:SF27. PTHR11699:SF27. 1 hit.
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01722. MMSDH. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency."
    Chambliss K.L., Gray R.G.F., Rylance G., Pollitt R.J., Gibson K.M.
    J. Inherit. Metab. Dis. 23:497-504(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MMSDHD ARG-446.
    Tissue: Liver and Lymphocyte.
  2. "Molecular basis of human MMSDH deficiency: gene organization and mutation analysis."
    Ding J.H., Yang B.Z., Wilkinson J., Roe C.R.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skin.
  3. "The structure and organization of the methylmalonic semialdehyde dehydrogenase (MMSDH) gene."
    Ding J.H., Yang B.Z., Wilkinson J.K., Roe C.R.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Amygdala.
  5. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Brain and Muscle.
  8. "CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution."
    Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A.
    J. Biol. Chem. 267:19724-19729(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-535 (ISOFORM 1).
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMMSA_HUMAN
AccessioniPrimary (citable) accession number: Q02252
Secondary accession number(s): B2R609
, B4DFS8, J3KNU8, Q9UKM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 24, 2001
Last modified: November 26, 2014
This is version 154 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3