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Q9Y600

- CSAD_HUMAN

UniProt

Q9Y600 - CSAD_HUMAN

Protein

Cysteine sulfinic acid decarboxylase

Gene

CSAD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    3-sulfino-L-alanine = hypotaurine + CO2.

    Cofactori

    Pyridoxal phosphate.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. pyridoxal phosphate binding Source: InterPro
    2. sulfinoalanine decarboxylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. small molecule metabolic process Source: Reactome
    3. sulfur amino acid catabolic process Source: Reactome
    4. sulfur amino acid metabolic process Source: Reactome
    5. taurine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06642-MONOMER.
    ReactomeiREACT_115654. Degradation of cysteine and homocysteine.
    UniPathwayiUPA00012; UER00538.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine sulfinic acid decarboxylase (EC:4.1.1.29)
    Alternative name(s):
    Cysteine-sulfinate decarboxylase
    Sulfinoalanine decarboxylase
    Gene namesi
    Name:CSAD
    Synonyms:CSD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:18966. CSAD.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38771.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 493493Cysteine sulfinic acid decarboxylasePRO_0000147006Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei305 – 3051N6-(pyridoxal phosphate)lysine

    Proteomic databases

    MaxQBiQ9Y600.
    PaxDbiQ9Y600.
    PRIDEiQ9Y600.

    PTM databases

    PhosphoSiteiQ9Y600.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y600.
    BgeeiQ9Y600.
    CleanExiHS_CSAD.
    GenevestigatoriQ9Y600.

    Organism-specific databases

    HPAiHPA039487.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi119512. 11 interactions.
    IntActiQ9Y600. 10 interactions.
    MINTiMINT-4832217.
    STRINGi9606.ENSP00000267085.

    Structurei

    Secondary structure

    1
    493
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 3118
    Turni32 – 343
    Helixi35 – 373
    Helixi49 – 568
    Helixi67 – 8014
    Beta strandi89 – 935
    Helixi99 – 11113
    Turni118 – 1203
    Helixi122 – 13918
    Beta strandi145 – 1517
    Helixi152 – 16716
    Helixi171 – 1744
    Helixi176 – 1783
    Beta strandi182 – 1876
    Helixi193 – 2008
    Helixi205 – 2073
    Beta strandi208 – 2114
    Helixi221 – 23313
    Beta strandi237 – 24610
    Turni248 – 2503
    Helixi256 – 26611
    Beta strandi269 – 2746
    Helixi277 – 2826
    Turni284 – 2863
    Helixi287 – 2904
    Helixi293 – 2953
    Beta strandi297 – 3015
    Beta strandi314 – 3196
    Helixi324 – 3296
    Helixi345 – 3473
    Helixi350 – 3523
    Helixi362 – 39635
    Beta strandi401 – 4055
    Beta strandi408 – 4169
    Helixi419 – 4213
    Helixi430 – 4356
    Helixi437 – 44812
    Beta strandi452 – 4587
    Beta strandi461 – 4688
    Helixi476 – 49015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JISX-ray1.60A/B1-493[»]
    ProteinModelPortaliQ9Y600.
    SMRiQ9Y600. Positions 7-493.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y600.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the group II decarboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0076.
    HOGENOMiHOG000005382.
    HOVERGENiHBG004980.
    InParanoidiQ9Y600.
    KOiK01594.
    OMAiLQDTSNL.
    OrthoDBiEOG7H1JM3.
    PhylomeDBiQ9Y600.
    TreeFamiTF314688.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00282. Pyridoxal_deC. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y600-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MADSEALPSL AGDPVAVEAL LRAVFGVVVD EAIQKGTSVS QKVCEWKEPE    50
    ELKQLLDLEL RSQGESQKQI LERCRAVIRY SVKTGHPRFF NQLFSGLDPH 100
    ALAGRIITES LNTSQYTYEI APVFVLMEEE VLRKLRALVG WSSGDGIFCP 150
    GGSISNMYAV NLARYQRYPD CKQRGLRTLP PLALFTSKEC HYSIQKGAAF 200
    LGLGTDSVRV VKADERGKMV PEDLERQIGM AEAEGAVPFL VSATSGTTVL 250
    GAFDPLEAIA DVCQRHGLWL HVDAAWGGSV LLSQTHRHLL DGIQRADSVA 300
    WNPHKLLAAG LQCSALLLQD TSNLLKRCHG SQASYLFQQD KFYDVALDTG 350
    DKVVQCGRRV DCLKLWLMWK AQGDQGLERR IDQAFVLARY LVEEMKKREG 400
    FELVMEPEFV NVCFWFVPPS LRGKQESPDY HERLSKVAPV LKERMVKEGS 450
    MMIGYQPHGT RGNFFRVVVA NSALTCADMD FLLNELERLG QDL 493
    Length:493
    Mass (Da):55,023
    Last modified:October 17, 2006 - v2
    Checksum:i09BA2028D942016E
    GO
    Isoform 2 (identifier: Q9Y600-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         43-189: Missing.

    Show »
    Length:346
    Mass (Da):38,232
    Checksum:iE214BE34AFA35101
    GO
    Isoform 3 (identifier: Q9Y600-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MSIPLKSSFLLSYLCTLPPALLSREILM

    Note: No experimental confirmation available.Curated

    Show »
    Length:520
    Mass (Da):58,012
    Checksum:i5EE3EF5294A87E27
    GO

    Sequence cautioni

    The sequence AAD32546.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH98278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH98342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH99717.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAI05919.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2571E → G in AAD32545. 1 PublicationCurated
    Sequence conflicti377 – 3771L → P in AAD32546. 1 PublicationCurated
    Sequence conflicti433 – 4331R → G in AAD32544. 1 PublicationCurated
    Isoform 3 (identifier: Q9Y600-3)
    Sequence conflicti9 – 91F → S in AAH98342. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MSIPLKSSFLLSYLCTLPPA LLSREILM in isoform 3. 2 PublicationsVSP_039002
    Alternative sequencei43 – 189147Missing in isoform 2. 2 PublicationsVSP_001307Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF116546 mRNA. Translation: AAD32544.1.
    AF116547 mRNA. Translation: AAD32545.1.
    AF116548 mRNA. Translation: AAD32546.1. Different initiation.
    AK289659 mRNA. Translation: BAF82348.1.
    CH471054 Genomic DNA. Translation: EAW96670.1.
    BC098278 mRNA. Translation: AAH98278.1. Different initiation.
    BC098342 mRNA. Translation: AAH98342.1. Different initiation.
    BC099717 mRNA. Translation: AAH99717.1. Different initiation.
    BC105918 mRNA. Translation: AAI05919.1. Different initiation.
    CCDSiCCDS58235.1. [Q9Y600-1]
    CCDS8848.2. [Q9Y600-3]
    RefSeqiNP_001231634.1. NM_001244705.1. [Q9Y600-1]
    NP_057073.4. NM_015989.4. [Q9Y600-3]
    XP_006719510.1. XM_006719447.1. [Q9Y600-3]
    UniGeneiHs.279815.

    Genome annotation databases

    EnsembliENST00000267085; ENSP00000267085; ENSG00000139631. [Q9Y600-3]
    ENST00000379843; ENSP00000369172; ENSG00000139631. [Q9Y600-2]
    ENST00000379846; ENSP00000369175; ENSG00000139631. [Q9Y600-2]
    ENST00000444623; ENSP00000415485; ENSG00000139631. [Q9Y600-1]
    ENST00000453446; ENSP00000410648; ENSG00000139631. [Q9Y600-1]
    GeneIDi51380.
    KEGGihsa:51380.
    UCSCiuc001sbw.3. human. [Q9Y600-2]
    uc001sby.3. human. [Q9Y600-1]
    uc010snx.2. human. [Q9Y600-3]

    Polymorphism databases

    DMDMi116241317.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF116546 mRNA. Translation: AAD32544.1 .
    AF116547 mRNA. Translation: AAD32545.1 .
    AF116548 mRNA. Translation: AAD32546.1 . Different initiation.
    AK289659 mRNA. Translation: BAF82348.1 .
    CH471054 Genomic DNA. Translation: EAW96670.1 .
    BC098278 mRNA. Translation: AAH98278.1 . Different initiation.
    BC098342 mRNA. Translation: AAH98342.1 . Different initiation.
    BC099717 mRNA. Translation: AAH99717.1 . Different initiation.
    BC105918 mRNA. Translation: AAI05919.1 . Different initiation.
    CCDSi CCDS58235.1. [Q9Y600-1 ]
    CCDS8848.2. [Q9Y600-3 ]
    RefSeqi NP_001231634.1. NM_001244705.1. [Q9Y600-1 ]
    NP_057073.4. NM_015989.4. [Q9Y600-3 ]
    XP_006719510.1. XM_006719447.1. [Q9Y600-3 ]
    UniGenei Hs.279815.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JIS X-ray 1.60 A/B 1-493 [» ]
    ProteinModelPortali Q9Y600.
    SMRi Q9Y600. Positions 7-493.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119512. 11 interactions.
    IntActi Q9Y600. 10 interactions.
    MINTi MINT-4832217.
    STRINGi 9606.ENSP00000267085.

    Chemistry

    DrugBanki DB00151. L-Cysteine.
    DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei Q9Y600.

    Polymorphism databases

    DMDMi 116241317.

    Proteomic databases

    MaxQBi Q9Y600.
    PaxDbi Q9Y600.
    PRIDEi Q9Y600.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267085 ; ENSP00000267085 ; ENSG00000139631 . [Q9Y600-3 ]
    ENST00000379843 ; ENSP00000369172 ; ENSG00000139631 . [Q9Y600-2 ]
    ENST00000379846 ; ENSP00000369175 ; ENSG00000139631 . [Q9Y600-2 ]
    ENST00000444623 ; ENSP00000415485 ; ENSG00000139631 . [Q9Y600-1 ]
    ENST00000453446 ; ENSP00000410648 ; ENSG00000139631 . [Q9Y600-1 ]
    GeneIDi 51380.
    KEGGi hsa:51380.
    UCSCi uc001sbw.3. human. [Q9Y600-2 ]
    uc001sby.3. human. [Q9Y600-1 ]
    uc010snx.2. human. [Q9Y600-3 ]

    Organism-specific databases

    CTDi 51380.
    GeneCardsi GC12M053551.
    HGNCi HGNC:18966. CSAD.
    HPAi HPA039487.
    neXtProti NX_Q9Y600.
    PharmGKBi PA38771.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0076.
    HOGENOMi HOG000005382.
    HOVERGENi HBG004980.
    InParanoidi Q9Y600.
    KOi K01594.
    OMAi LQDTSNL.
    OrthoDBi EOG7H1JM3.
    PhylomeDBi Q9Y600.
    TreeFami TF314688.

    Enzyme and pathway databases

    UniPathwayi UPA00012 ; UER00538 .
    BioCyci MetaCyc:HS06642-MONOMER.
    Reactomei REACT_115654. Degradation of cysteine and homocysteine.

    Miscellaneous databases

    ChiTaRSi CSAD. human.
    EvolutionaryTracei Q9Y600.
    GenomeRNAii 51380.
    NextBioi 54887.
    PROi Q9Y600.

    Gene expression databases

    ArrayExpressi Q9Y600.
    Bgeei Q9Y600.
    CleanExi HS_CSAD.
    Genevestigatori Q9Y600.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR002129. PyrdxlP-dep_de-COase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF00282. Pyridoxal_deC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Pritchard J.E., Ramsden D.B.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Brain.
    2. "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 2).
      Tissue: Amygdala.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 3).
    5. "The crystal structure of human cysteine sulfinic acid decarboxylase (CSAD)."
      Structural genomics consortium (SGC)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR.

    Entry informationi

    Entry nameiCSAD_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y600
    Secondary accession number(s): A8K0U4
    , Q4QQH9, Q9UNJ5, Q9Y601
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 125 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3