FRMPD4

Functionⁱ

Positive regulator of dendritic spine morphogenesis and density. Required for the maintenance of excitatory synaptic transmission. Binds phosphatidylinositol 4,5-bisphosphate.1 Publication

GO - Molecular functionⁱ

phosphatidylinositol-4,5-bisphosphate binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19118189

Complete GO annotation...

GO - Biological processⁱ

positive regulation of synapse structural plasticity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19118189

Complete GO annotation...

Keywordsⁱ

Ligand	Lipid-binding

Ligand

Lipid-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: FERM and PDZ domain-containing protein 4 Alternative name(s): PDZ domain-containing protein 10 PSD-95-interacting regulator of spine morphogenesis Short name: Preso
Gene namesⁱ	Name:FRMPD4 Synonyms:KIAA0316, PDZD10, PDZK10
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome X

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:29007. FRMPD4.

HGNCⁱ

HGNC:29007. FRMPD4.

Subcellular locationⁱ

Cell projection › dendritic spine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that regulates dendritic spine morphogenesis."
  Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B., Eom S.H., Kim H., Kim E.
  J. Neurosci. 28:14546-14556(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH DLG1; DLG2; DLG3; DLG4; ARHGEF7 AND PHOSPHATIDYLINOSITOL-4,5-BIPHOSPHATE, DOMAIN FERM, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-102; 1319-GLU--VAL-1322 AND THR-1320.

GO - Cellular componentⁱ

cytoskeleton Source: InterPro
dendritic spine
Source: UniProtKB
Inferred from direct assayⁱ
- 19118189

Complete GO annotation...

Keywords - Cellular componentⁱ

Cell projection

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Mental retardation, X-linked 104 (MRX104)1 Publication

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

Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	102	R → A: Abolishes the interaction with ARHGEF7. Mutant overexpression in cultured neurons does not induce a significant increase in spine density contrary to wild type. 1 Publication	1
Mutagenesisⁱ	990	L → A: Nearly abolishes interaction with GPSM2; when associated with 1010-A-A-1011. 1 Publication	1
Mutagenesisⁱ	1010 – 1011	YF → AA: Nearly abolishes interaction with GPSM2; when associated with A-990. 1 Publication	2
Mutagenesisⁱ	1319 – 1322	Missing : Abolishes the interaction with DLG1, DLG2, DLG3 and DLG4/PSD95. Reduces protein localization to dendritic spines. 1 Publication	4
Mutagenesisⁱ	1320	T → D: Abolishes the interaction with DLG4/PSD95. Reduces protein localization to dendritic spines. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	9758.
MIMⁱ	300983. phenotype.
Open Targets More...OpenTargetsⁱ	ENSG00000169933.
PharmGKBⁱ	PA134977575.

Polymorphism and mutation databases

BioMutaⁱ	FRMPD4.
DMDMⁱ	121948742.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000307132	1 – 1322	FERM and PDZ domain-containing protein 4Add BLAST		1322

Proteomic databases

EPDⁱ	Q14CM0.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q14CM0.
PaxDbⁱ	Q14CM0.
PeptideAtlas More...PeptideAtlasⁱ	Q14CM0.
PRIDEⁱ	Q14CM0.

PTM databases

iPTMnetⁱ	Q14CM0.
PhosphoSitePlusⁱ	Q14CM0.
SwissPalmⁱ	Q14CM0.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000169933.
CleanExⁱ	HS_FRMPD4.
ExpressionAtlasⁱ	Q14CM0. baseline and differential.
Genevisibleⁱ	Q14CM0. HS.

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA035580.

HPAⁱ

HPA035580.

Interactionⁱ

Subunit structureⁱ

Interacts (via C-terminus) with DLG1, DLG2, DLG3 and DLG4/PSD95. Interacts (via N-terminus) with ARHGEF7; the interaction is mediated by the PDZ domain (PubMed:19118189). Interacts with GPSM2 (via TPR repeat region) (PubMed:25664792).2 Publications

Protein-protein interaction databases

BioGridⁱ	115105. 2 interactors.
IntActⁱ	Q14CM0. 6 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-2795491.
STRINGⁱ	9606.ENSP00000370057.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Helixⁱ	1007 – 1009	Combined sources		3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4WND	X-ray	1.50	B	978-1025	[»]
	4WNE	X-ray	2.00	B	987-1011	[»]
	4WNF	X-ray	2.90	B	978-1025	[»]
	4WNG	X-ray	2.11	B	978-1025	[»]
ProteinModelPortalⁱ	Q14CM0.
SMRⁱ	Q14CM0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	33 – 66	WWPROSITE-ProRule annotationAdd BLAST	34
Domainⁱ	78 – 155	PDZPROSITE-ProRule annotationAdd BLAST	78
Domainⁱ	204 – 519	FERMPROSITE-ProRule annotationAdd BLAST	316

Domainⁱ

The FERM domain mediates the interaction with phosphatidylinositol 4,5-bisphosphate.1 Publication

Phylogenomic databases

eggNOGⁱ	KOG3552. Eukaryota. ENOG410YV8Z. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063201.
HOGENOMⁱ	HOG000090222.
HOVERGENⁱ	HBG106593.
InParanoidⁱ	Q14CM0.
OMAⁱ	KDHRHLY.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G00W9.
PhylomeDBⁱ	Q14CM0.
TreeFamⁱ	TF316497.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd14473. FERM_B-lobe. 1 hit.
Gene3Dⁱ	1.20.80.10. 1 hit.
InterProⁱ	View protein in InterPro IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR000299. FERM_domain. IPR001478. PDZ. IPR011993. PH_dom-like. IPR029071. Ubiquitin-rel_dom. IPR001202. WW_dom.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00373. FERM_M. 1 hit. PF00595. PDZ. 1 hit.
SMARTⁱ	View protein in SMART SM00295. B41. 1 hit. SM00228. PDZ. 1 hit.
SUPFAMⁱ	SSF47031. SSF47031. 1 hit. SSF50156. SSF50156. 1 hit. SSF50729. SSF50729. 1 hit. SSF54236. SSF54236. 1 hit.
PROSITEⁱ	View protein in PROSITE PS50057. FERM_3. 1 hit. PS50106. PDZ. 1 hit. PS50020. WW_DOMAIN_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q14CM0-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MDVFSFVKIA KLSSHRTKSS GWPPPSGTWG LSQVPPYGWE MTANRDGRDY 
        60         70         80         90        100
FINHMTQAIP FDDPRLESCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV 
       110        120        130        140        150
VRSVTPGGPS EGKLIPGDQI VMINDEPVSA APRERVIDLV RSCKESILLT 
       160        170        180        190        200
VIQPYPSPKS AFISAAKKAR LKSNPVKVRF SEEVIINGQV SETVKDNSLL 
       210        220        230        240        250
FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK GIEHFSLMLE 
       260        270        280        290        300
QRTEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR 
       310        320        330        340        350
DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK 
       360        370        380        390        400
ISLKYIEKEW GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL 
       410        420        430        440        450
SALQAKVHYL KFLSDLRLYG GRVFKATLVQ AEKRSEVTLL VGPRYGISHV 
       460        470        480        490        500
INTKTNLVAL LADFSHVNRI EMFSEEESLV RVELHVLDVK PITLLMESSD 
       510        520        530        540        550
AMNLACLTAG YYRLLVDSRR SIFNMANKKN TATQETGPEN KGKHNLLGPD 
       560        570        580        590        600
WNCIPQMTTF IGEGEQEAQI TYIDSKQKTV EITDSTMCPK EHRHLYIDNA 
       610        620        630        640        650
YSSDGLNQQL SQPGEAPCEA DYRSLAQRSL LTLSGPETLK KAQESPRGAK 
       660        670        680        690        700
VSFIFGDFAL DDGISPPTLG YETLLDEGPE MLEKQRNLYI GSANDMKGLD 
       710        720        730        740        750
LTPEAEGIQF VENSVYANIG DVKSFQAAEG IEEPLLHDIC YAENTDDAED 
       760        770        780        790        800
EDEVSCEEDL VVGEMNQPAI LNLSGSSDDI IDLTSLPPPE GDDNEDDFLL 
       810        820        830        840        850
RSLNMAIAAP PPGFRDSSDE EDSQSQAASF PEDKEKGSSL QNDEIPVSLI 
       860        870        880        890        900
DAVPTSAEGK CEKGLDNAVV STLGALEALS VSEEQQTSDN SGVAILRAYS 
       910        920        930        940        950
PESSSDSGNE TNSSEMTESS ELATAQKQSE NLSRMFLATH EGYHPLAEEQ 
       960        970        980        990       1000
TEFPASKTPA GGLPPKSSHA LAARPATDLP PKVVPSKQLL HSDHMEMEPE 
      1010       1020       1030       1040       1050
TMETKSVTDY FSKLHMGSVA YSCTSKRKSK LADGEGKAPP NGNTTGKKQQ 
      1060       1070       1080       1090       1100
GTKTAEMEEE ASGKFGTVSS RDSQHLSTFN LERTAFRKDS QRWYVATEGG 
      1110       1120       1130       1140       1150
MAEKSGLEAA TGKTFPRASG LGAREAEGKE EGAPDGETSD GSGLGQGDRF 
      1160       1170       1180       1190       1200
LTDVTCASSA KDLDNPEDAD SSTCDHPSKL PEADESVARL CDYHLAKRMS 
      1210       1220       1230       1240       1250
SLQSEGHFSL QSSQGSSVDA GCGTGSSGSA CATPVESPLC PSLGKHLIPD 
      1260       1270       1280       1290       1300
ASGKGVNYIP SEERAPGLPN HGATFKELHP QTEGMCPRMT VPALHTAINT 
      1310       1320 
EPLFGTLRDG CHRLPKIKET TV

Length:1,322

Mass (Da):144,379

Last modified:August 22, 2006 - v1

Checksum:ⁱ79B73E41B89E2D08

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	130	A → T in BAA20774 (PubMed:9205841).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_077481	553	C → R in MRX104. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB002314 mRNA. Translation: BAA20774.3. AK289694 mRNA. Translation: BAF82383.1. BC113700 mRNA. Translation: AAI13701.1. BC113702 mRNA. Translation: AAI13703.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS35201.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_055543.2. NM_014728.3.
UniGeneⁱ	Hs.657507.

Genome annotation databases

Ensemblⁱ	ENST00000380682; ENSP00000370057; ENSG00000169933.
GeneIDⁱ	9758.
KEGGⁱ	hsa:9758.
UCSC genome browser More...UCSCⁱ	uc004cuz.2. human.

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.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB002314 mRNA. Translation: BAA20774.3. AK289694 mRNA. Translation: BAF82383.1. BC113700 mRNA. Translation: AAI13701.1. BC113702 mRNA. Translation: AAI13703.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS35201.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_055543.2. NM_014728.3.
UniGeneⁱ	Hs.657507.

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4WND	X-ray	1.50	B	978-1025	[»]
	4WNE	X-ray	2.00	B	987-1011	[»]
	4WNF	X-ray	2.90	B	978-1025	[»]
	4WNG	X-ray	2.11	B	978-1025	[»]
ProteinModelPortalⁱ	Q14CM0.
SMRⁱ	Q14CM0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115105. 2 interactors.
IntActⁱ	Q14CM0. 6 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-2795491.
STRINGⁱ	9606.ENSP00000370057.

PTM databases

iPTMnetⁱ	Q14CM0.
PhosphoSitePlusⁱ	Q14CM0.
SwissPalmⁱ	Q14CM0.

Polymorphism and mutation databases

BioMutaⁱ	FRMPD4.
DMDMⁱ	121948742.

Proteomic databases

EPDⁱ	Q14CM0.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q14CM0.
PaxDbⁱ	Q14CM0.
PeptideAtlas More...PeptideAtlasⁱ	Q14CM0.
PRIDEⁱ	Q14CM0.

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	9758.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000380682; ENSP00000370057; ENSG00000169933.
GeneIDⁱ	9758.
KEGGⁱ	hsa:9758.
UCSC genome browser More...UCSCⁱ	uc004cuz.2. human.

Organism-specific databases

CTDⁱ	9758.
DisGeNET More...DisGeNETⁱ	9758.
GeneCardsⁱ	FRMPD4.
H-InvDBⁱ	HIX0016653.
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:29007. FRMPD4.
Human Protein Atlas More...HPAⁱ	HPA035580.
MIMⁱ	300838. gene. 300983. phenotype.
neXtProtⁱ	NX_Q14CM0.
Open Targets More...OpenTargetsⁱ	ENSG00000169933.
PharmGKBⁱ	PA134977575.
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3552. Eukaryota. ENOG410YV8Z. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063201.
HOGENOMⁱ	HOG000090222.
HOVERGENⁱ	HBG106593.
InParanoidⁱ	Q14CM0.
OMAⁱ	KDHRHLY.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G00W9.
PhylomeDBⁱ	Q14CM0.
TreeFamⁱ	TF316497.

Miscellaneous databases

ChiTaRSⁱ	FRMPD4. human.
GenomeRNAiⁱ	9758.
Protein Ontology More...PROⁱ	PR:Q14CM0.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000169933.
CleanExⁱ	HS_FRMPD4.
ExpressionAtlasⁱ	Q14CM0. baseline and differential.
Genevisibleⁱ	Q14CM0. HS.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd14473. FERM_B-lobe. 1 hit.
Gene3Dⁱ	1.20.80.10. 1 hit.
InterProⁱ	View protein in InterPro IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR000299. FERM_domain. IPR001478. PDZ. IPR011993. PH_dom-like. IPR029071. Ubiquitin-rel_dom. IPR001202. WW_dom.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00373. FERM_M. 1 hit. PF00595. PDZ. 1 hit.
SMARTⁱ	View protein in SMART SM00295. B41. 1 hit. SM00228. PDZ. 1 hit.
SUPFAMⁱ	SSF47031. SSF47031. 1 hit. SSF50156. SSF50156. 1 hit. SSF50729. SSF50729. 1 hit. SSF54236. SSF54236. 1 hit.
PROSITEⁱ	View protein in PROSITE PS50057. FERM_3. 1 hit. PS50106. PDZ. 1 hit. PS50020. WW_DOMAIN_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FRPD4_HUMAN
Accessionⁱ	Q14CM0Primary (citable) accession number: Q14CM0 Secondary accession number(s): A8K0X9, O15032
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
	Last sequence update:	August 22, 2006
	Last modified:	June 7, 2017
	This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Human chromosome X
Human chromosome X: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

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UniRef

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Supporting data

UniProtKB - Q14CM0 (FRPD4_HUMAN)

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FERM and PDZ domain-containing protein 4

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ