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Protein

Gephyrin

Gene

GPHN

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

Functioni

Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.By similarity

Catalytic activityi

ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by copper and tungsten.By similarity

Pathway: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Molybdenum, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000171723-MONOMER.
ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.
UniPathwayiUPA00344.

Protein family/group databases

MoonProtiQ9NQX3.

Names & Taxonomyi

Protein namesi
Recommended name:
Gephyrin
Including the following 2 domains:
Molybdopterin adenylyltransferase (EC:2.7.7.75)
Short name:
MPT adenylyltransferase
Alternative name(s):
Domain G
Molybdopterin molybdenumtransferase (EC:2.10.1.1)
Short name:
MPT Mo-transferase
Alternative name(s):
Domain E
Gene namesi
Name:GPHN
Synonyms:GPH, KIAA1385
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:15465. GPHN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

Molybdenum cofactor deficiency, complementation group C (MOCODC)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of molybdenum cofactor deficiency, an autosomal recessive metabolic disorder leading to the pleiotropic loss of molybdoenzyme activities. It is clinically characterized by onset in infancy of poor feeding, intractable seizures, severe psychomotor retardation, and death in early childhood in most patients.

See also OMIM:615501
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti580 – 5801D → A in MOCODC. 1 Publication
VAR_070275

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615501. phenotype.
Orphaneti3197. Hereditary hyperekplexia.
308400. Sulfite oxidase deficiency due to molybdenum cofactor deficiency type C.
PharmGKBiPA28840.

Polymorphism and mutation databases

BioMutaiGPHN.
DMDMi13431554.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 736736GephyrinPRO_0000170964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881Phosphoserine3 Publications
Modified residuei194 – 1941Phosphoserine3 Publications
Modified residuei198 – 1981Phosphothreonine1 Publication
Modified residuei266 – 2661Phosphothreonine1 Publication
Modified residuei305 – 3051Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NQX3.
PaxDbiQ9NQX3.
PRIDEiQ9NQX3.

PTM databases

PhosphoSiteiQ9NQX3.

Expressioni

Gene expression databases

BgeeiQ9NQX3.
CleanExiHS_GPHN.
ExpressionAtlasiQ9NQX3. baseline and differential.
GenevisibleiQ9NQX3. HS.

Organism-specific databases

HPAiCAB004419.
HPA003116.
HPA024694.

Interactioni

Subunit structurei

Homotrimer. Interacts with GABARAP (By similarity). Interacts with SRGAP2 (via SH3 domain) (By similarity).By similarity

Protein-protein interaction databases

BioGridi115537. 24 interactions.
IntActiQ9NQX3. 8 interactions.
MINTiMINT-139581.
STRINGi9606.ENSP00000417901.

Structurei

Secondary structure

1
736
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 227Combined sources
Helixi24 – 274Combined sources
Helixi34 – 4411Combined sources
Turni46 – 494Combined sources
Beta strandi52 – 598Combined sources
Helixi63 – 7513Combined sources
Beta strandi80 – 867Combined sources
Beta strandi89 – 913Combined sources
Helixi96 – 1038Combined sources
Beta strandi105 – 1073Combined sources
Helixi109 – 12214Combined sources
Helixi124 – 1285Combined sources
Beta strandi133 – 1364Combined sources
Beta strandi139 – 1446Combined sources
Helixi148 – 15811Combined sources
Helixi159 – 1613Combined sources
Helixi162 – 1698Combined sources
Helixi175 – 1784Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JLJX-ray1.60A/B/C1-181[»]
ProteinModelPortaliQ9NQX3.
SMRiQ9NQX3. Positions 13-181, 319-736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQX3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 166153MPT Mo-transferaseAdd
BLAST
Regioni140 – 316177Interaction with GABARAPBy similarityAdd
BLAST
Regioni326 – 736411MPT adenylyltransferaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the MoaB/Mog family.Curated
In the C-terminal section; belongs to the MoeA family.Curated

Phylogenomic databases

eggNOGiCOG0303.
GeneTreeiENSGT00390000016577.
HOGENOMiHOG000280651.
HOVERGENiHBG005828.
InParanoidiQ9NQX3.
KOiK15376.
OrthoDBiEOG70087N.
PhylomeDBiQ9NQX3.
TreeFamiTF300902.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NQX3-1) [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
MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG
60 70 80 90 100
GTISAYKIVP DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT
110 120 130 140 150
KEVIEREAPG MALAMLMGSL NVTPLGMLSR PVCGIRGKTL IINLPGSKKG
160 170 180 190 200
SQECFQFILP ALPHAIDLLR DAIVKVKEVH DELEDLPSPP PPLSPPPTTS
210 220 230 240 250
PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAI AAKIPDSIIS
260 270 280 290 300
RGVQVLPRDT ASLSTTPSES PRAQATSRLS TASCPTPKVQ SRCSSKENIL
310 320 330 340 350
RASHSAVDIT KVARRHRMSP FPLTSMDKAF ITVLEMTPVL GTEIINYRDG
360 370 380 390 400
MGRVLAQDVY AKDNLPPFPA SVKDGYAVRA ADGPGDRFII GESQAGEQPT
410 420 430 440 450
QTVMPGQVMR VTTGAPIPCG ADAVVQVEDT ELIRESDDGT EELEVRILVQ
460 470 480 490 500
ARPGQDIRPI GHDIKRGECV LAKGTHMGPS EIGLLATVGV TEVEVNKFPV
510 520 530 540 550
VAVMSTGNEL LNPEDDLLPG KIRDSNRSTL LATIQEHGYP TINLGIVGDN
560 570 580 590 600
PDDLLNALNE GISRADVIIT SGGVSMGEKD YLKQVLDIDL HAQIHFGRVF
610 620 630 640 650
MKPGLPTTFA TLDIDGVRKI IFALPGNPVS AVVTCNLFVV PALRKMQGIL
660 670 680 690 700
DPRPTIIKAR LSCDVKLDPR PEYHRCILTW HHQEPLPWAQ STGNQMSSRL
710 720 730
MSMRSANGLL MLPPKTEQYV ELHKGEVVDV MVIGRL
Length:736
Mass (Da):79,748
Last modified:October 1, 2000 - v1
Checksum:iE2BDA3AD3AB962C0
GO
Isoform 2 (identifier: Q9NQX3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     243-243: K → KKHPFYTSPAVVMAHGEQPIPGLINYSHHSTDER

Show »
Length:769
Mass (Da):83,448
Checksum:i552D5B7BD9AD7452
GO

Sequence cautioni

The sequence BAA92623.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101N → Y Found in a patient with hyperekplexia; unknown pathological significance; does not affect the structural lattices formed by gephyrin. 1 Publication
Corresponds to variant rs121908539 [ dbSNP | Ensembl ].
VAR_044162
Natural varianti580 – 5801D → A in MOCODC. 1 Publication
VAR_070275

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei243 – 2431K → KKHPFYTSPAVVMAHGEQPI PGLINYSHHSTDER in isoform 2. 2 PublicationsVSP_021769

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272663 mRNA. Translation: AAF81785.1.
AJ272343 mRNA. Translation: CAC10537.1.
AB037806 mRNA. Translation: BAA92623.1. Different initiation.
BC030016 mRNA. Translation: AAH30016.1.
CCDSiCCDS32103.1. [Q9NQX3-1]
CCDS9777.1. [Q9NQX3-2]
RefSeqiNP_001019389.1. NM_001024218.1. [Q9NQX3-1]
NP_065857.1. NM_020806.4. [Q9NQX3-2]
UniGeneiHs.208765.

Genome annotation databases

EnsembliENST00000315266; ENSP00000312771; ENSG00000171723. [Q9NQX3-1]
ENST00000478722; ENSP00000417901; ENSG00000171723. [Q9NQX3-2]
GeneIDi10243.
KEGGihsa:10243.
UCSCiuc001xix.3. human. [Q9NQX3-2]
uc001xiy.3. human. [Q9NQX3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272663 mRNA. Translation: AAF81785.1.
AJ272343 mRNA. Translation: CAC10537.1.
AB037806 mRNA. Translation: BAA92623.1. Different initiation.
BC030016 mRNA. Translation: AAH30016.1.
CCDSiCCDS32103.1. [Q9NQX3-1]
CCDS9777.1. [Q9NQX3-2]
RefSeqiNP_001019389.1. NM_001024218.1. [Q9NQX3-1]
NP_065857.1. NM_020806.4. [Q9NQX3-2]
UniGeneiHs.208765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JLJX-ray1.60A/B/C1-181[»]
ProteinModelPortaliQ9NQX3.
SMRiQ9NQX3. Positions 13-181, 319-736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115537. 24 interactions.
IntActiQ9NQX3. 8 interactions.
MINTiMINT-139581.
STRINGi9606.ENSP00000417901.

Protein family/group databases

MoonProtiQ9NQX3.

PTM databases

PhosphoSiteiQ9NQX3.

Polymorphism and mutation databases

BioMutaiGPHN.
DMDMi13431554.

Proteomic databases

MaxQBiQ9NQX3.
PaxDbiQ9NQX3.
PRIDEiQ9NQX3.

Protocols and materials databases

DNASUi10243.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315266; ENSP00000312771; ENSG00000171723. [Q9NQX3-1]
ENST00000478722; ENSP00000417901; ENSG00000171723. [Q9NQX3-2]
GeneIDi10243.
KEGGihsa:10243.
UCSCiuc001xix.3. human. [Q9NQX3-2]
uc001xiy.3. human. [Q9NQX3-1]

Organism-specific databases

CTDi10243.
GeneCardsiGC14P066974.
GeneReviewsiGPHN.
HGNCiHGNC:15465. GPHN.
HPAiCAB004419.
HPA003116.
HPA024694.
MIMi603930. gene.
615501. phenotype.
neXtProtiNX_Q9NQX3.
Orphaneti3197. Hereditary hyperekplexia.
308400. Sulfite oxidase deficiency due to molybdenum cofactor deficiency type C.
PharmGKBiPA28840.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0303.
GeneTreeiENSGT00390000016577.
HOGENOMiHOG000280651.
HOVERGENiHBG005828.
InParanoidiQ9NQX3.
KOiK15376.
OrthoDBiEOG70087N.
PhylomeDBiQ9NQX3.
TreeFamiTF300902.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciMetaCyc:ENSG00000171723-MONOMER.
ReactomeiREACT_25073. Molybdenum cofactor biosynthesis.

Miscellaneous databases

ChiTaRSiGPHN. human.
EvolutionaryTraceiQ9NQX3.
GeneWikiiGPHN.
GenomeRNAii10243.
NextBioi38806.
PROiQ9NQX3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQX3.
CleanExiHS_GPHN.
ExpressionAtlasiQ9NQX3. baseline and differential.
GenevisibleiQ9NQX3. HS.

Family and domain databases

Gene3Di2.40.340.10. 1 hit.
3.40.980.10. 2 hits.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
IPR005111. MoeA_C_domain_IV.
IPR005110. MoeA_linker/N.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 2 hits.
PF03454. MoeA_C. 1 hit.
PF03453. MoeA_N. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 2 hits.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 2 hits.
SSF63867. SSF63867. 1 hit.
SSF63882. SSF63882. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 2 hits.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
PS01079. MOCF_BIOSYNTHESIS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mutation in the gene for the neurotransmitter receptor-clustering protein gephyrin causes a novel form of molybdenum cofactor deficiency."
    Reiss J., Gross-Hardt S., Christensen E., Schmidt P., Mendel R.R., Schwarz G.
    Am. J. Hum. Genet. 68:208-213(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN MOCODC.
  2. "The human gephyrin (GPHN) gene: structure, chromosome localization and expression in non-neuronal cells."
    David-Watine B.
    Gene 271:239-245(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Kidney.
  3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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 2).
    Tissue: Testis.
  5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-194; THR-198 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structures of human gephyrin and plant Cnx1 G domains: comparative analysis and functional implications."
    Schwarz G., Schrader N., Mendel R.R., Hecht H.-J., Schindelin H.
    J. Mol. Biol. 312:405-418(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-181, SUBUNIT.
  13. "Isoform heterogeneity of the human gephyrin gene (GPHN), binding domains to the glycine receptor, and mutation analysis in hyperekplexia."
    Rees M.I., Harvey K., Ward H., White J.H., Evans L., Duguid I.C., Hsu C.-C., Coleman S.L., Miller J., Baer K., Waldvogel H.J., Gibbon F., Smart T.G., Owen M.J., Harvey R.J., Snell R.G.
    J. Biol. Chem. 278:24688-24696(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TYR-10, CHARACTERIZATION OF VARIANT TYR-10.
  14. Cited for: VARIANT MOCODC ALA-580.

Entry informationi

Entry nameiGEPH_HUMAN
AccessioniPrimary (citable) accession number: Q9NQX3
Secondary accession number(s): Q9H4E9, Q9P2G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 144 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, Multifunctional enzyme, 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.