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Protein

Cysteine sulfinic acid decarboxylase

Gene

CSAD

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

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 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
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS06642-MONOMER.
BRENDAi4.1.1.29. 2681.
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 Componenti: 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

BgeeiQ9Y600.
CleanExiHS_CSAD.
ExpressionAtlasiQ9Y600. baseline and differential.
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 – 3118Combined sources
Turni32 – 343Combined sources
Helixi35 – 373Combined sources
Helixi49 – 568Combined sources
Helixi67 – 8014Combined sources
Beta strandi89 – 935Combined sources
Helixi99 – 11113Combined sources
Turni118 – 1203Combined sources
Helixi122 – 13918Combined sources
Beta strandi145 – 1517Combined sources
Helixi152 – 16716Combined sources
Helixi171 – 1744Combined sources
Helixi176 – 1783Combined sources
Beta strandi182 – 1876Combined sources
Helixi193 – 2008Combined sources
Helixi205 – 2073Combined sources
Beta strandi208 – 2114Combined sources
Helixi221 – 23313Combined sources
Beta strandi237 – 24610Combined sources
Turni248 – 2503Combined sources
Helixi256 – 26611Combined sources
Beta strandi269 – 2746Combined sources
Helixi277 – 2826Combined sources
Turni284 – 2863Combined sources
Helixi287 – 2904Combined sources
Helixi293 – 2953Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi314 – 3196Combined sources
Helixi324 – 3296Combined sources
Helixi345 – 3473Combined sources
Helixi350 – 3523Combined sources
Helixi362 – 39635Combined sources
Beta strandi401 – 4055Combined sources
Beta strandi408 – 4169Combined sources
Helixi419 – 4213Combined sources
Helixi430 – 4356Combined sources
Helixi437 – 44812Combined sources
Beta strandi452 – 4587Combined sources
Beta strandi461 – 4688Combined sources
Helixi476 – 49015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119205.
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. AlignAdd to basket

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

        10         20         30         40         50
MADSEALPSL AGDPVAVEAL LRAVFGVVVD EAIQKGTSVS QKVCEWKEPE
60 70 80 90 100
ELKQLLDLEL RSQGESQKQI LERCRAVIRY SVKTGHPRFF NQLFSGLDPH
110 120 130 140 150
ALAGRIITES LNTSQYTYEI APVFVLMEEE VLRKLRALVG WSSGDGIFCP
160 170 180 190 200
GGSISNMYAV NLARYQRYPD CKQRGLRTLP PLALFTSKEC HYSIQKGAAF
210 220 230 240 250
LGLGTDSVRV VKADERGKMV PEDLERQIGM AEAEGAVPFL VSATSGTTVL
260 270 280 290 300
GAFDPLEAIA DVCQRHGLWL HVDAAWGGSV LLSQTHRHLL DGIQRADSVA
310 320 330 340 350
WNPHKLLAAG LQCSALLLQD TSNLLKRCHG SQASYLFQQD KFYDVALDTG
360 370 380 390 400
DKVVQCGRRV DCLKLWLMWK AQGDQGLERR IDQAFVLARY LVEEMKKREG
410 420 430 440 450
FELVMEPEFV NVCFWFVPPS LRGKQESPDY HERLSKVAPV LKERMVKEGS
460 470 480 490
MMIGYQPHGT RGNFFRVVVA NSALTCADMD FLLNELERLG QDL
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.Curated
The sequence AAH98278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH98342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH99717.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI05919.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571E → G in AAD32545 (Ref. 1) Curated
Sequence conflicti377 – 3771L → P in AAD32546 (Ref. 1) Curated
Sequence conflicti433 – 4331R → G in AAD32544 (Ref. 1) Curated
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:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

DrugBankiDB00151. L-Cysteine.

PTM databases

PhosphoSiteiQ9Y600.

Polymorphism databases

DMDMi116241317.

Proteomic databases

MaxQBiQ9Y600.
PaxDbiQ9Y600.
PRIDEiQ9Y600.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267085; ENSP00000267085; ENSG00000139631. [Q9Y600-3]
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]

Organism-specific databases

CTDi51380.
GeneCardsiGC12M053551.
HGNCiHGNC:18966. CSAD.
HPAiHPA039487.
neXtProtiNX_Q9Y600.
PharmGKBiPA38771.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0076.
GeneTreeiENSGT00760000119205.
HOGENOMiHOG000005382.
HOVERGENiHBG004980.
InParanoidiQ9Y600.
KOiK01594.
OMAiLQDTSNL.
OrthoDBiEOG7H1JM3.
PhylomeDBiQ9Y600.
TreeFamiTF314688.

Enzyme and pathway databases

UniPathwayiUPA00012; UER00538.
BioCyciMetaCyc:HS06642-MONOMER.
BRENDAi4.1.1.29. 2681.
ReactomeiREACT_115654. Degradation of cysteine and homocysteine.

Miscellaneous databases

ChiTaRSiCSAD. human.
EvolutionaryTraceiQ9Y600.
GenomeRNAii51380.
NextBioi54887.
PROiQ9Y600.

Gene expression databases

BgeeiQ9Y600.
CleanExiHS_CSAD.
ExpressionAtlasiQ9Y600. baseline and differential.
GenevestigatoriQ9Y600.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Pritchard J.E., Ramsden D.B.
    Submitted (NOV-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(2003) [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(2003) [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 (JUL-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: April 1, 2015
This is version 130 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

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.