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Q9GZT4

- SRR_HUMAN

UniProt

Q9GZT4 - SRR_HUMAN

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Protein

Serine racemase

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

Functioni

Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.2 Publications

Catalytic activityi

L-serine = D-serine.1 Publication
L-serine = pyruvate + NH3.1 Publication
D-serine = pyruvate + NH3.1 Publication

Cofactori

Pyridoxal phosphate.1 Publication

Enzyme regulationi

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP. Competitively inhibited by malonate.

Kineticsi

  1. KM=6.5 mM for L-serine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATP By similarity
Active sitei56 – 561Proton acceptor By similarity
Active sitei84 – 841Proton acceptor By similarity
Binding sitei121 – 1211ATP By similarity
Binding sitei135 – 1351Substrate Inferred
Metal bindingi210 – 2101Magnesium
Metal bindingi214 – 2141Magnesium; via carbonyl oxygen
Metal bindingi216 – 2161Magnesium

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  3. D-serine ammonia-lyase activity Source: UniProtKB-EC
  4. glycine binding Source: UniProtKB
  5. L-serine ammonia-lyase activity Source: UniProtKB
  6. magnesium ion binding Source: UniProtKB
  7. PDZ domain binding Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. pyridoxal phosphate binding Source: UniProtKB
  10. serine racemase activity Source: UniProtKB
  11. threonine racemase activity Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. brain development Source: Ensembl
  3. D-serine biosynthetic process Source: UniProtKB
  4. D-serine metabolic process Source: UniProtKB
  5. L-serine metabolic process Source: UniProtKB
  6. protein homotetramerization Source: UniProtKB
  7. pyruvate biosynthetic process Source: UniProtKB
  8. response to drug Source: Ensembl
  9. response to lipopolysaccharide Source: UniProtKB
  10. response to morphine Source: Ensembl
  11. serine family amino acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS09614-MONOMER.
BRENDAi5.1.1.18. 2681.
SignaLinkiQ9GZT4.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine racemase (EC:4.3.1.17, EC:4.3.1.18, EC:5.1.1.18)
Alternative name(s):
D-serine ammonia-lyase
D-serine dehydratase
L-serine ammonia-lyase
L-serine dehydratase
Gene namesi
Name:SRR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:14398. SRR.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. neuronal cell body Source: UniProtKB
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37877.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Serine racemasePRO_0000185650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-(pyridoxal phosphate)lysine
Modified residuei113 – 1131S-nitrosocysteine By similarity

Post-translational modificationi

S-nitrosylated, leading to decrease the enzyme activity By similarity.

Keywords - PTMi

S-nitrosylation

Proteomic databases

MaxQBiQ9GZT4.
PaxDbiQ9GZT4.
PRIDEiQ9GZT4.

PTM databases

PhosphoSiteiQ9GZT4.

Expressioni

Tissue specificityi

Brain: expressed at high levels in hippocampus and corpus callosum, intermediate levels in substantia nigra and caudate, and low levels in amygdala, thalamus, and subthalamic nuclei. Expressed in heart, skeletal muscle, kidney and liver.1 Publication

Gene expression databases

ArrayExpressiQ9GZT4.
BgeeiQ9GZT4.
CleanExiHS_SRR.
GenevestigatoriQ9GZT4.

Organism-specific databases

HPAiCAB015343.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi121963. 7 interactions.
STRINGi9606.ENSP00000339435.

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911
Helixi20 – 223
Helixi32 – 387
Beta strandi40 – 467
Helixi47 – 493
Helixi51 – 533
Helixi56 – 6510
Beta strandi79 – 824
Helixi86 – 9712
Beta strandi102 – 1076
Helixi112 – 1209
Beta strandi124 – 1285
Helixi132 – 14615
Beta strandi153 – 1553
Helixi157 – 17317
Beta strandi179 – 1835
Beta strandi185 – 1873
Helixi188 – 20013
Beta strandi204 – 2118
Helixi212 – 2143
Helixi216 – 2238
Helixi238 – 2403
Helixi248 – 2558
Beta strandi258 – 2625
Helixi264 – 27815
Helixi284 – 29411
Helixi296 – 3005
Beta strandi307 – 3126
Helixi321 – 3233

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L6BX-ray1.50A1-340[»]
3L6RX-ray1.70A1-340[»]
ProteinModelPortaliQ9GZT4.
SMRiQ9GZT4. Positions 3-329.

Miscellaneous databases

EvolutionaryTraceiQ9GZT4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2392Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1171.
HOGENOMiHOG000046974.
HOVERGENiHBG023167.
InParanoidiQ9GZT4.
KOiK12235.
OMAiVEHYEAP.
OrthoDBiEOG7HB5B2.
PhylomeDBiQ9GZT4.
TreeFamiTF313346.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9GZT4-1 [UniParc]FASTAAdd to Basket

« Hide

MCAQYCISFA DVEKAHINIR DSIHLTPVLT SSILNQLTGR NLFFKCELFQ    50
KTGSFKIRGA LNAVRSLVPD ALERKPKAVV THSSGNHGQA LTYAAKLEGI 100
PAYIVVPQTA PDCKKLAIQA YGASIVYCEP SDESRENVAK RVTEETEGIM 150
VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGML AGIAITVKAL 200
KPSVKVYAAE PSNADDCYQS KLKGKLMPNL YPPETIADGV KSSIGLNTWP 250
IIRDLVDDIF TVTEDEIKCA TQLVWERMKL LIEPTAGVGV AAVLSQHFQT 300
VSPEVKNICI VLSGGNVDLT SSITWVKQAE RPASYQSVSV 340
Length:340
Mass (Da):36,566
Last modified:March 1, 2001 - v1
Checksum:i873342C62D5D7B9D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF169974 mRNA. Translation: AAG27081.1.
AY034081 mRNA. Translation: AAK58495.1.
AK023169 mRNA. Translation: BAB14442.1.
CR457300 mRNA. Translation: CAG33581.1.
CH471108 Genomic DNA. Translation: EAW90553.1.
CH471108 Genomic DNA. Translation: EAW90554.1.
CH471108 Genomic DNA. Translation: EAW90555.1.
BC074728 mRNA. Translation: AAH74728.1.
CCDSiCCDS11017.1.
RefSeqiNP_068766.1. NM_021947.1.
XP_006721628.1. XM_006721565.1.
XP_006721629.1. XM_006721566.1.
UniGeneiHs.461954.

Genome annotation databases

EnsembliENST00000344595; ENSP00000339435; ENSG00000167720.
GeneIDi63826.
KEGGihsa:63826.
UCSCiuc002fue.1. human.

Polymorphism databases

DMDMi20139924.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF169974 mRNA. Translation: AAG27081.1 .
AY034081 mRNA. Translation: AAK58495.1 .
AK023169 mRNA. Translation: BAB14442.1 .
CR457300 mRNA. Translation: CAG33581.1 .
CH471108 Genomic DNA. Translation: EAW90553.1 .
CH471108 Genomic DNA. Translation: EAW90554.1 .
CH471108 Genomic DNA. Translation: EAW90555.1 .
BC074728 mRNA. Translation: AAH74728.1 .
CCDSi CCDS11017.1.
RefSeqi NP_068766.1. NM_021947.1.
XP_006721628.1. XM_006721565.1.
XP_006721629.1. XM_006721566.1.
UniGenei Hs.461954.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3L6B X-ray 1.50 A 1-340 [» ]
3L6R X-ray 1.70 A 1-340 [» ]
ProteinModelPortali Q9GZT4.
SMRi Q9GZT4. Positions 3-329.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121963. 7 interactions.
STRINGi 9606.ENSP00000339435.

Chemistry

BindingDBi Q9GZT4.
ChEMBLi CHEMBL4460.
DrugBanki DB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSitei Q9GZT4.

Polymorphism databases

DMDMi 20139924.

Proteomic databases

MaxQBi Q9GZT4.
PaxDbi Q9GZT4.
PRIDEi Q9GZT4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344595 ; ENSP00000339435 ; ENSG00000167720 .
GeneIDi 63826.
KEGGi hsa:63826.
UCSCi uc002fue.1. human.

Organism-specific databases

CTDi 63826.
GeneCardsi GC17P002212.
HGNCi HGNC:14398. SRR.
HPAi CAB015343.
MIMi 606477. gene.
neXtProti NX_Q9GZT4.
PharmGKBi PA37877.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1171.
HOGENOMi HOG000046974.
HOVERGENi HBG023167.
InParanoidi Q9GZT4.
KOi K12235.
OMAi VEHYEAP.
OrthoDBi EOG7HB5B2.
PhylomeDBi Q9GZT4.
TreeFami TF313346.

Enzyme and pathway databases

BioCyci MetaCyc:HS09614-MONOMER.
BRENDAi 5.1.1.18. 2681.
SignaLinki Q9GZT4.

Miscellaneous databases

ChiTaRSi SRR. human.
EvolutionaryTracei Q9GZT4.
GeneWikii Serine_racemase.
GenomeRNAii 63826.
NextBioi 65538.
PROi Q9GZT4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9GZT4.
Bgeei Q9GZT4.
CleanExi HS_SRR.
Genevestigatori Q9GZT4.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human serine racemase: molecular cloning, genomic organization and functional expression."
    De Miranda J., Santoro A., Engelender S., Wolosker H.
    Gene 256:183-188(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 97-114; 116-135; 206-221 AND 226-241, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  8. "The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding."
    Smith M.A., Mack V., Ebneth A., Moraes I., Felicetti B., Wood M., Schonfeld D., Mather O., Cesura A., Barker J.
    J. Biol. Chem. 285:12873-12881(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 3-340 IN COMPLEX WITH MANGANESE IONS; MALONATE AND PYRIDOXAL PHOSPHATE, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Entry informationi

Entry nameiSRR_HUMAN
AccessioniPrimary (citable) accession number: Q9GZT4
Secondary accession number(s): D3DTI5, Q6IA55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 108 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, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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