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Protein

Ketimine reductase mu-crystallin

Gene

CRYM

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

Functioni

Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors.1 Publication

Catalytic activityi

Thiomorpholine 3-carboxylate + NAD(P)+ = 3,4-dehydro-thiomorpholine-3-carboxylate + NAD(P)H.1 Publication

Cofactori

NAD+2 Publications, NADP+2 Publications

Kineticsi

  1. KM=47 µM for 3,4-dehydro-thiomorpholine-3-carboxylate (at pH 5.0 and 37 degrees Celsius)1 Publication
  2. KM=3.6 µM for NADH (at pH 5.0 and 37 degrees Celsius)1 Publication
  1. Vmax=9.6 µmol/min/mg enzyme with 3,4-dehydro-thiomorpholine-3-carboxylate as substrate (at pH 5.0 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 4.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei168NADP1 Publication1
Binding sitei169NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi143 – 148NADP1 Publication6

GO - Molecular functioni

  • NADP binding Source: UniProtKB
  • oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: GO_Central
  • protein homodimerization activity Source: UniProtKB
  • thiomorpholine-carboxylate dehydrogenase activity Source: Reactome
  • thyroid hormone binding Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB

GO - Biological processi

  • lysine catabolic process Source: Reactome
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • sensory perception of sound Source: UniProtKB
  • thyroid hormone metabolic process Source: GO_Central
  • thyroid hormone transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000103316-MONOMER.
ZFISH:ENSG00000103316-MONOMER.
ReactomeiR-HSA-71064. Lysine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Ketimine reductase mu-crystallin (EC:1.5.1.25)
Alternative name(s):
NADP-regulated thyroid-hormone-binding protein
Gene namesi
Name:CRYM
Synonyms:THBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2418. CRYM.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: Ensembl
  • peroxisomal matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal dominant, 40 (DFNA40)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
See also OMIM:616357
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073780314K → KYNKGY in DFNA40. 1 Publication1
Natural variantiVAR_073781314K → T in DFNA40. 1 PublicationCorresponds to variant rs104894512dbSNPEnsembl.1

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

DisGeNETi1428.
MalaCardsiCRYM.
MIMi616357. phenotype.
OpenTargetsiENSG00000103316.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA26924.

Polymorphism and mutation databases

BioMutaiCRYM.
DMDMi2498259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002006781 – 314Ketimine reductase mu-crystallinAdd BLAST314

Proteomic databases

EPDiQ14894.
PaxDbiQ14894.
PeptideAtlasiQ14894.
PRIDEiQ14894.

PTM databases

iPTMnetiQ14894.
PhosphoSitePlusiQ14894.

Expressioni

Tissue specificityi

Expressed in neural tissue, muscle and kidney.

Gene expression databases

BgeeiENSG00000103316.
CleanExiHS_CRYM.
ExpressionAtlasiQ14894. baseline and differential.
GenevisibleiQ14894. HS.

Organism-specific databases

HPAiHPA019086.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF1P542742EBI-7107048,EBI-710997

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi107815. 4 interactors.
IntActiQ14894. 3 interactors.
MINTiMINT-4532969.
STRINGi9606.ENSP00000219599.

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi10 – 16Combined sources7
Helixi20 – 23Combined sources4
Helixi24 – 35Combined sources12
Helixi37 – 40Combined sources4
Beta strandi48 – 52Combined sources5
Helixi53 – 55Combined sources3
Beta strandi57 – 66Combined sources10
Turni67 – 70Combined sources4
Beta strandi71 – 80Combined sources10
Beta strandi84 – 87Combined sources4
Beta strandi89 – 99Combined sources11
Turni101 – 103Combined sources3
Beta strandi106 – 111Combined sources6
Helixi113 – 131Combined sources19
Beta strandi138 – 142Combined sources5
Helixi146 – 158Combined sources13
Beta strandi162 – 167Combined sources6
Helixi171 – 180Combined sources10
Beta strandi181 – 183Combined sources3
Helixi191 – 195Combined sources5
Beta strandi199 – 203Combined sources5
Helixi214 – 216Combined sources3
Beta strandi222 – 225Combined sources4
Helixi238 – 243Combined sources6
Beta strandi244 – 249Combined sources6
Helixi251 – 257Combined sources7
Helixi259 – 262Combined sources4
Turni263 – 265Combined sources3
Helixi272 – 277Combined sources6
Beta strandi288 – 291Combined sources4
Helixi296 – 310Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I99X-ray2.60A/B2-313[»]
ProteinModelPortaliQ14894.
SMRiQ14894.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14894.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3007. Eukaryota.
COG2423. LUCA.
GeneTreeiENSGT00390000000237.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiQ14894.
KOiK18258.
OMAiQRNLVNM.
OrthoDBiEOG091G0NR8.
PhylomeDBiQ14894.
TreeFamiTF105309.

Family and domain databases

Gene3Di3.30.1780.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR023401. ODC_N.
[Graphical view]
PfamiPF02423. OCD_Mu_crystall. 1 hit.
[Graphical view]
PIRSFiPIRSF001439. CryM. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q14894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV
60 70 80 90 100
PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE
110 120 130 140 150
PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS
160 170 180 190 200
HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV
210 220 230 240 250
IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS
260 270 280 290 300
QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT
310
VAAKLIYDSW SSGK
Length:314
Mass (Da):33,776
Last modified:November 1, 1997 - v1
Checksum:iA49D316B41CE6648
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073780314K → KYNKGY in DFNA40. 1 Publication1
Natural variantiVAR_073781314K → T in DFNA40. 1 PublicationCorresponds to variant rs104894512dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02950 mRNA. Translation: AAC16914.1.
U85772 mRNA. Translation: AAB81564.1.
AF039397
, AF039392, AF039393, AF039394, AF039395, AF039396 Genomic DNA. Translation: AAB94938.1.
AK290852 mRNA. Translation: BAF83541.1.
BX648477 mRNA. Translation: CAI46030.1.
AF001550 Genomic DNA. Translation: AAB67600.1.
CH471228 Genomic DNA. Translation: EAW66863.1.
BC018061 mRNA. Translation: AAH18061.1.
CCDSiCCDS10597.1.
PIRiB46290.
RefSeqiNP_001879.1. NM_001888.4.
UniGeneiHs.924.

Genome annotation databases

EnsembliENST00000219599; ENSP00000219599; ENSG00000103316.
ENST00000543948; ENSP00000440227; ENSG00000103316.
GeneIDi1428.
KEGGihsa:1428.
UCSCiuc002dim.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02950 mRNA. Translation: AAC16914.1.
U85772 mRNA. Translation: AAB81564.1.
AF039397
, AF039392, AF039393, AF039394, AF039395, AF039396 Genomic DNA. Translation: AAB94938.1.
AK290852 mRNA. Translation: BAF83541.1.
BX648477 mRNA. Translation: CAI46030.1.
AF001550 Genomic DNA. Translation: AAB67600.1.
CH471228 Genomic DNA. Translation: EAW66863.1.
BC018061 mRNA. Translation: AAH18061.1.
CCDSiCCDS10597.1.
PIRiB46290.
RefSeqiNP_001879.1. NM_001888.4.
UniGeneiHs.924.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I99X-ray2.60A/B2-313[»]
ProteinModelPortaliQ14894.
SMRiQ14894.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107815. 4 interactors.
IntActiQ14894. 3 interactors.
MINTiMINT-4532969.
STRINGi9606.ENSP00000219599.

PTM databases

iPTMnetiQ14894.
PhosphoSitePlusiQ14894.

Polymorphism and mutation databases

BioMutaiCRYM.
DMDMi2498259.

Proteomic databases

EPDiQ14894.
PaxDbiQ14894.
PeptideAtlasiQ14894.
PRIDEiQ14894.

Protocols and materials databases

DNASUi1428.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219599; ENSP00000219599; ENSG00000103316.
ENST00000543948; ENSP00000440227; ENSG00000103316.
GeneIDi1428.
KEGGihsa:1428.
UCSCiuc002dim.4. human.

Organism-specific databases

CTDi1428.
DisGeNETi1428.
GeneCardsiCRYM.
HGNCiHGNC:2418. CRYM.
HPAiHPA019086.
MalaCardsiCRYM.
MIMi123740. gene.
616357. phenotype.
neXtProtiNX_Q14894.
OpenTargetsiENSG00000103316.
Orphaneti90635. Autosomal dominant non-syndromic sensorineural deafness type DFNA.
PharmGKBiPA26924.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3007. Eukaryota.
COG2423. LUCA.
GeneTreeiENSGT00390000000237.
HOGENOMiHOG000137263.
HOVERGENiHBG005408.
InParanoidiQ14894.
KOiK18258.
OMAiQRNLVNM.
OrthoDBiEOG091G0NR8.
PhylomeDBiQ14894.
TreeFamiTF105309.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000103316-MONOMER.
ZFISH:ENSG00000103316-MONOMER.
ReactomeiR-HSA-71064. Lysine catabolism.

Miscellaneous databases

ChiTaRSiCRYM. human.
EvolutionaryTraceiQ14894.
GeneWikiiCRYM.
GenomeRNAii1428.
PROiQ14894.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103316.
CleanExiHS_CRYM.
ExpressionAtlasiQ14894. baseline and differential.
GenevisibleiQ14894. HS.

Family and domain databases

Gene3Di3.30.1780.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR003462. ODC_Mu_crystall.
IPR023401. ODC_N.
[Graphical view]
PfamiPF02423. OCD_Mu_crystall. 1 hit.
[Graphical view]
PIRSFiPIRSF001439. CryM. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCRYM_HUMAN
AccessioniPrimary (citable) accession number: Q14894
Secondary accession number(s): D5MNX0, Q5HYB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 153 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.