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Protein

14-3-3 protein theta

Gene

YWHAQ

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

Functioni

Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Interaction with phosphoserine on interacting protein
Sitei127 – 1271Interaction with phosphoserine on interacting protein

GO - Molecular functioni

  1. protein N-terminus binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: Reactome
  2. intrinsic apoptotic signaling pathway Source: Reactome
  3. membrane organization Source: Reactome
  4. negative regulation of transcription, DNA-templated Source: BHF-UCL
  5. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  6. protein targeting Source: Ensembl
  7. small GTPase mediated signal transduction Source: Ensembl
  8. substantia nigra development Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_549. Activation of BAD and translocation to mitochondria.
SignaLinkiP27348.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein theta
Alternative name(s):
14-3-3 protein T-cell
14-3-3 protein tau
Protein HS1
Gene namesi
Name:YWHAQ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12854. YWHAQ.

Subcellular locationi

Cytoplasm
Note: In neurons, axonally transported to the nerve terminals.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoplasmic vesicle membrane Source: Reactome
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24524514-3-3 protein thetaPRO_0000058636Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei49 – 491N6-acetyllysine1 Publication
Modified residuei68 – 681N6-acetyllysine1 Publication
Modified residuei82 – 821Nitrated tyrosineBy similarity
Modified residuei104 – 1041Nitrated tyrosineBy similarity
Modified residuei115 – 1151N6-acetyllysine1 Publication
Modified residuei232 – 2321Phosphoserine2 Publications

Post-translational modificationi

Ser-232 is probably phosphorylated by CK1.1 Publication

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP27348.
PaxDbiP27348.
PeptideAtlasiP27348.
PRIDEiP27348.

2D gel databases

OGPiP27348.
REPRODUCTION-2DPAGEIPI00018146.

PTM databases

PhosphoSiteiP27348.

Miscellaneous databases

PMAP-CutDBP27348.

Expressioni

Tissue specificityi

Abundantly expressed in brain, heart and pancreas, and at lower levels in kidney and placenta. Up-regulated in the lumbar spinal cord from patients with sporadic amyotrophic lateral sclerosis (ALS) compared with controls, with highest levels of expression in individuals with predominant lower motor neuron involvement.1 Publication

Gene expression databases

BgeeiP27348.
CleanExiHS_YWHAQ.
ExpressionAtlasiP27348. baseline and differential.
GenevestigatoriP27348.

Organism-specific databases

HPAiCAB010286.
HPA007925.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK16 (By similarity). Interacts with SSH1. Interacts with CDKN1B ('Thr-198' phosphorylated form); the interaction translocates CDKN1B to the cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241' phosphorylated form of PDPK1.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ADAM22Q9P0K1-32EBI-359854,EBI-1567267
ARRB1P494073EBI-359854,EBI-743313
ARRB2P321213EBI-359854,EBI-714559
CBLP226816EBI-359854,EBI-518228
CDK14O949213EBI-359854,EBI-1043945
CDKN1BP465274EBI-359854,EBI-519280
CSNK1A1P678282EBI-359854,EBI-7540603From a different organism.
EGFRP005336EBI-359854,EBI-297353
FSHRP239454EBI-359854,EBI-848239
KANK1Q146782EBI-359854,EBI-2556221
KANK1Q14678-23EBI-359854,EBI-6173812
LRRK2Q5S0078EBI-359854,EBI-5323863
Rnd3P615882EBI-359854,EBI-6930266From a different organism.
SSH1Q8WYL52EBI-359854,EBI-1222387

Protein-protein interaction databases

BioGridi116168. 392 interactions.
DIPiDIP-27584N.
IntActiP27348. 83 interactions.
MINTiMINT-121282.
STRINGi9606.ENSP00000238081.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513Combined sources
Helixi19 – 3113Combined sources
Helixi38 – 6831Combined sources
Helixi75 – 10329Combined sources
Turni104 – 1085Combined sources
Helixi112 – 13221Combined sources
Helixi135 – 15925Combined sources
Helixi165 – 18016Combined sources
Helixi185 – 20117Combined sources
Turni202 – 2054Combined sources
Helixi208 – 22720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTPX-ray2.80A/B1-234[»]
ProteinModelPortaliP27348.
SMRiP27348. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27348.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP27348.
KOiK16197.
OMAiSGDDRKQ.
OrthoDBiEOG7HHWT3.
PhylomeDBiP27348.
TreeFamiTF102002.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27348-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN
60 70 80 90 100
VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL
110 120 130 140 150
LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ
160 170 180 190 200
EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI
210 220 230 240
AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN
Length:245
Mass (Da):27,764
Last modified:July 31, 1992 - v1
Checksum:i175534325E9E37C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361D → N in AAV38817 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56468 mRNA. Translation: CAA39840.1.
X57347 mRNA. Translation: CAA40622.1.
BT020014 mRNA. Translation: AAV38817.1.
CH471053 Genomic DNA. Translation: EAX00977.1.
CH471053 Genomic DNA. Translation: EAX00979.1.
BC050601 mRNA. Translation: AAH50601.1.
BC056867 mRNA. Translation: AAH56867.1.
BC093019 mRNA. Translation: AAH93019.1.
AF070556 mRNA. Translation: AAC28640.1.
CCDSiCCDS1666.1.
PIRiS15076.
RefSeqiNP_006817.1. NM_006826.3.
UniGeneiHs.74405.

Genome annotation databases

EnsembliENST00000238081; ENSP00000238081; ENSG00000134308.
ENST00000381844; ENSP00000371267; ENSG00000134308.
GeneIDi10971.
KEGGihsa:10971.
UCSCiuc002qzx.3. human.

Polymorphism databases

DMDMi112690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56468 mRNA. Translation: CAA39840.1.
X57347 mRNA. Translation: CAA40622.1.
BT020014 mRNA. Translation: AAV38817.1.
CH471053 Genomic DNA. Translation: EAX00977.1.
CH471053 Genomic DNA. Translation: EAX00979.1.
BC050601 mRNA. Translation: AAH50601.1.
BC056867 mRNA. Translation: AAH56867.1.
BC093019 mRNA. Translation: AAH93019.1.
AF070556 mRNA. Translation: AAC28640.1.
CCDSiCCDS1666.1.
PIRiS15076.
RefSeqiNP_006817.1. NM_006826.3.
UniGeneiHs.74405.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTPX-ray2.80A/B1-234[»]
ProteinModelPortaliP27348.
SMRiP27348. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116168. 392 interactions.
DIPiDIP-27584N.
IntActiP27348. 83 interactions.
MINTiMINT-121282.
STRINGi9606.ENSP00000238081.

PTM databases

PhosphoSiteiP27348.

Polymorphism databases

DMDMi112690.

2D gel databases

OGPiP27348.
REPRODUCTION-2DPAGEIPI00018146.

Proteomic databases

MaxQBiP27348.
PaxDbiP27348.
PeptideAtlasiP27348.
PRIDEiP27348.

Protocols and materials databases

DNASUi10971.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238081; ENSP00000238081; ENSG00000134308.
ENST00000381844; ENSP00000371267; ENSG00000134308.
GeneIDi10971.
KEGGihsa:10971.
UCSCiuc002qzx.3. human.

Organism-specific databases

CTDi10971.
GeneCardsiGC02M009724.
H-InvDBHIX0077146.
HGNCiHGNC:12854. YWHAQ.
HPAiCAB010286.
HPA007925.
MIMi609009. gene.
neXtProtiNX_P27348.
PharmGKBiPA37443.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5040.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP27348.
KOiK16197.
OMAiSGDDRKQ.
OrthoDBiEOG7HHWT3.
PhylomeDBiP27348.
TreeFamiTF102002.

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_549. Activation of BAD and translocation to mitochondria.
SignaLinkiP27348.

Miscellaneous databases

ChiTaRSiYWHAQ. human.
EvolutionaryTraceiP27348.
GeneWikiiYWHAQ.
GenomeRNAii10971.
NextBioi41686.
PMAP-CutDBP27348.
PROiP27348.
SOURCEiSearch...

Gene expression databases

BgeeiP27348.
CleanExiHS_YWHAQ.
ExpressionAtlasiP27348. baseline and differential.
GenevestigatoriP27348.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of a human protein kinase regulator protein."
    Nielsen P.J.
    Biochim. Biophys. Acta 1088:425-428(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: T-cell.
  2. "Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway."
    Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., Walbum E., Vandekerckhove J., Celis J.E.
    J. Mol. Biol. 231:982-998(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Keratinocyte.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Placenta, Skin and Uterus.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18.
    Tissue: Platelet.
  7. Bienvenut W.V., Dhillon A.S., Kolch W.
    Submitted (JAN-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and Hepatoma.
  8. Yu W., Gibbs R.A.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245.
    Tissue: Brain.
  9. "14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction."
    Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., Morrice N., Moelling K., Aitken A.
    J. Biol. Chem. 272:28882-28888(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal cord."
    Malaspina A., Kaushik N., de Belleroche J.
    J. Neurochem. 75:2511-2520(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization."
    Fujita N., Sato S., Katayama K., Tsuruo T.
    J. Biol. Chem. 277:28706-28713(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDKN1B.
  12. "Regulation of kinase activity of 3-phosphoinositide-dependent protein kinase-1 by binding to 14-3-3."
    Sato S., Fujita N., Tsuruo T.
    J. Biol. Chem. 277:39360-39367(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PDPK1.
  13. "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia."
    Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.
    J. Cell Biol. 165:465-471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSH1.
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
    Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
    EMBO J. 27:2305-2316(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAB2.
  16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND LYS-115, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways."
    Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., Gamblin S.J.
    Nature 376:188-191(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  25. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.

Entry informationi

Entry namei1433T_HUMAN
AccessioniPrimary (citable) accession number: P27348
Secondary accession number(s): D6W4Z5
, Q567U5, Q5TZU8, Q9UP48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: July 31, 1992
Last modified: March 31, 2015
This is version 166 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 2
    Human chromosome 2: 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

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.