Homer1

Functionⁱ

Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Differentially regulates the functions of the calcium activated channel ryanodine receptors RYR1 and RYR2. Isoform 1 decreases the activity of RYR2, and increases the activity of RYR1, whereas isoform 3 counteracts the effects by competing for binding sites. Isoform 1 regulates the trafficking and surface expression of GRM5. Isoform 3 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1, and isoform 2 to regulate synaptic metabotropic glutamate function. Isoform 3, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development.1 Publication

GO - Molecular functionⁱ

G-protein coupled glutamate receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15758184
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 19345194
protein complex scaffold
Source: BHF-UCL
Inferred from physical interactionⁱ
- 10433269
protein heterodimerization activity
Source: RGD
Inferred from physical interactionⁱ
- 9727012
receptor binding
Source: RGD
Inferred from direct assayⁱ
- 9069287
scaffold protein binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 10433269
type 5 metabotropic glutamate receptor binding
Source: RGD
Inferred from physical interactionⁱ
- 16554037

GO - Biological processⁱ

circadian rhythm
Source: RGD
Inferred from expression patternⁱ
- 15308308
G-protein coupled glutamate receptor signaling pathway
Source: RGD
Inferred from direct assayⁱ
- 9069287
protein localization to synapse
Source: BHF-UCL
Inferred from direct assayⁱ
- 12867517
response to cocaine
Source: RGD
Inferred from expression patternⁱ
- 18932227
response to nicotine
Source: RGD
Inferred from expression patternⁱ
- 15813924

Complete GO annotation...

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Homer protein homolog 1 Alternative name(s): PSD-Zip45 VASP/Ena-related gene up-regulated during seizure and LTP 1 Short name: Vesl-1
Gene namesⁱ	Name:Homer1 Synonyms:Homer, Vesl
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [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 › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 2

Organism-specific databases

RGDⁱ	628725. Homer1.

Subcellular locationⁱ

Cytoplasm By similarity
Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity
Cell junction › synapse
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins."
  Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P., Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.
  Neuron 23:583-592(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: INTERACTION WITH SHANK1 AND SHANK3, SUBCELLULAR LOCATION.

Note:

Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum.By similarity

GO - Cellular componentⁱ

cell junction Source: UniProtKB-KW
cytoplasm Source: UniProtKB-SubCell
dendrite
Source: RGD
Inferred from direct assayⁱ
- 16554037
dendritic shaft
Source: RGD
Inferred from direct assayⁱ
- 9069287
neuronal cell body
Source: RGD
Inferred from direct assayⁱ
- 16554037
- 9069287
neuron projection
Source: RGD
Inferred from direct assayⁱ
- 19105975
postsynaptic density
Source: BHF-UCL
Inferred from direct assayⁱ
- 10433269
postsynaptic membrane Source: UniProtKB-KW
synapse
Source: RGD
Inferred from direct assayⁱ
- 19547699

Complete GO annotation...

Keywords - Cellular componentⁱ

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

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description
Mutagenesisⁱ	24 – 24	1	W → A: Disrupts binding to both GRM1 and SHANK3. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	24 – 24	1	W → Y: Disrupts binding to GRM1. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	70 – 70	1	T → A: Normal binding. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	70 – 70	1	T → E: Disrupts binding to SHANK3. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	74 – 74	1	F → A: Eliminates binding to both GRM1 and SHANK3. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	76 – 76	1	Q → A: Normal binding. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	76 – 76	1	Q → R: Normal binding. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	85 – 85	1	V → A: Diminishes binding to GRM1. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	89 – 89	1	G → A: Eliminates binding to both GRM1 and SHANK3. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.
Mutagenesisⁱ	89 – 89	1	G → N: Eliminates binding to both GRM1 and SHANK3. 1 Publication Manual assertion based on experiment inⁱ Ref.14 "Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition." Beneken J., Tu J.C., Xiao B., Nuriya M., Yuan J.P., Worley P.F., Leahy D.J. Neuron 26:143-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-111 IN COMPLEX WITH GRM5, MUTAGENESIS OF TRP-24; THR-70; PHE-74; GLN-76; VAL-85 AND GLY-89.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 366	366	Homer protein homolog 1		PRO_0000191007	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Modified residueⁱ	318 – 318	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9Z2Y3 (HOME1_MOUSE)

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

PaxDbⁱ	Q9Z214.
PRIDEⁱ	Q9Z214.

PTM databases

iPTMnetⁱ	Q9Z214.
PhosphoSiteⁱ	Q9Z214.

Expressionⁱ

Tissue specificityⁱ

Highly expressed in cortex, Purkinje cells of the cerebellum, hippocampus, striatum and olfactory bulb. Isoform 1 and isoform 3 are expressed in skeletal and cardiac muscle.1 Publication

Developmental stageⁱ

In the developing hippocampus, the expression of isoform 1 is high at P8, then decreased with progression of hippocampal development. Isoform 3 expression was constitutively low, and not regulated during hippocampal development.

Inductionⁱ

Isoform 3 is induced in the hippocampus, by seizure and synaptic mechanisms in association with long-term potentiation (LTP). It is also induced in the striatum by drugs that alter dopamine signaling.

Gene expression databases

Bgeeⁱ	ENSRNOG00000047014.
ExpressionAtlasⁱ	Q9Z214. baseline and differential.
Genevisibleⁱ	Q9Z214. RN.

Interactionⁱ

Subunit structureⁱ

Interacts with GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. Interacts with IFT57 and OPHN1. Isoform 1 and isoform 2 encode coiled-coil structures that mediate homo- and heteromultimerization.10 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Agap2	Q8CGU4	4	EBI-4410552,EBI-4409108
Grm5	Q3UVX5	3	EBI-4410552,EBI-8795045	From a different organism.
Shank1	Q9WV48	4	EBI-2338999,EBI-80909

With

Entry

#Exp.

IntAct

Notes

Agap2

Q8CGU4

4

EBI-4410552,EBI-4409108

Grm5

Q3UVX5

3

EBI-4410552,EBI-8795045

From a different organism.

Shank1

Q9WV48

4

EBI-2338999,EBI-80909

GO - Molecular functionⁱ

G-protein coupled glutamate receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15758184
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 19345194
protein complex scaffold
Source: BHF-UCL
Inferred from physical interactionⁱ
- 10433269
protein heterodimerization activity
Source: RGD
Inferred from physical interactionⁱ
- 9727012
receptor binding
Source: RGD
Inferred from direct assayⁱ
- 9069287
scaffold protein binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 10433269
type 5 metabotropic glutamate receptor binding
Source: RGD
Inferred from physical interactionⁱ
- 16554037

Protein-protein interaction databases

BioGridⁱ	248180. 11 interactions.
IntActⁱ	Q9Z214. 9 interactions.
MINTⁱ	MINT-1891037.
STRINGⁱ	10116.ENSRNOP00000065989.

Structureⁱ

Secondary structure

1

366

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Beta strandⁱ	3 – 16	14	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Turnⁱ	18 – 20	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Beta strandⁱ	23 – 27	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Beta strandⁱ	32 – 39	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Turnⁱ	40 – 43	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Beta strandⁱ	44 – 51	8	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Beta strandⁱ	54 – 60	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Beta strandⁱ	71 – 79	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Turnⁱ	80 – 83	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Beta strandⁱ	84 – 89	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Helixⁱ	93 – 110	18	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:1DDW
Helixⁱ	302 – 362	61	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:3CVE

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DDV	X-ray	1.90	A	1-111	[»]
1DDW	X-ray	1.70	A	1-120	[»]
1I2H	X-ray	1.80	A	1-163	[»]
3CVE	X-ray	1.75	A/B/C/D	302-366	[»]

ProteinModelPortalⁱ

Q9Z214.

SMRⁱ

Q9Z214. Positions 1-143.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q9Z214.

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Domainⁱ	1 – 110	110	WH1PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00410			Add BLAST

Coiled coil

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Coiled coilⁱ	193 – 364	172	Sequence analysis			Add BLAST

Domainⁱ

The WH1 domain interacts with the PPXXF motif in GRM1, GRM5, RYR1, RYR2, ITPR1, SHANK 1 and SHANK3.

Sequence similaritiesⁱ

Belongs to the Homer family.Curated

Contains 1 WH1 domain.PROSITE-ProRule annotation

Keywords - Domainⁱ

Coiled coil

Phylogenomic databases

eggNOGⁱ	ENOG410IGRQ. Eukaryota. ENOG410XQWT. LUCA.
GeneTreeⁱ	ENSGT00390000017850.
HOVERGENⁱ	HBG051918.
InParanoidⁱ	Q9Z214.
KOⁱ	K15010.
OrthoDBⁱ	EOG091G0CQ0.
PhylomeDBⁱ	Q9Z214.

Family and domain databases

Gene3Dⁱ	2.30.29.30. 1 hit.
InterProⁱ	IPR011993. PH_dom-like. IPR000697. WH1/EVH1_dom. [Graphical view]
Pfamⁱ	PF00568. WH1. 1 hit. [Graphical view]
SMARTⁱ	SM00461. WH1. 1 hit. [Graphical view]
SUPFAMⁱ	SSF50729. SSF50729. 1 hit.
PROSITEⁱ	PS50229. WH1. 1 hit. [Graphical view]

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q9Z214-1) [UniParc]FASTA Add to basket

Also known as: 1c, Vesl-1L

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
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL 
        60         70         80         90        100
DGSKAIINST ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA 
       110        120        130        140        150
EKFQEFKEAA RLAKEKSQEK MELTSTPSQE SAGGDLQSPL TPESINGTDD 
       160        170        180        190        200
ERTPDVTQNS EPRAEPAQNA LPFSHSAGDR TQGLSHASSA ISKHWEAELA 
       210        220        230        240        250
TLKGNNAKLT AALLESTANV KQWKQQLAAY QEEAERLHKR VTELECVSSQ 
       260        270        280        290        300
ANAVHSHKTE LSQTVQELEE TLKVKEEEIE RLKQEIDNAR ELQEQRDSLT 
       310        320        330        340        350
QKLQEVEIRN KDLEGQLSEL EQRLEKSQSE QDAFRSNLKT LLEILDGKIF 
       360 
ELTELRDNLA KLLECS

Length:366

Mass (Da):41,305

Last modified:November 28, 2003 - v2

Checksum:ⁱA6A21CB14207A384

GO

Isoform 2 (identifier: Q9Z214-2) [UniParc]FASTA Add to basket

Also known as: 1b

The sequence of this isoform differs from the canonical sequence as follows:
176-187: Missing.

« Hide

        10         20         30         40         50
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL 
        60         70         80         90        100
DGSKAIINST ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA 
       110        120        130        140        150
EKFQEFKEAA RLAKEKSQEK MELTSTPSQE SAGGDLQSPL TPESINGTDD 
       160        170        180        190        200
ERTPDVTQNS EPRAEPAQNA LPFSHSSAIS KHWEAELATL KGNNAKLTAA 
       210        220        230        240        250
LLESTANVKQ WKQQLAAYQE EAERLHKRVT ELECVSSQAN AVHSHKTELS 
       260        270        280        290        300
QTVQELEETL KVKEEEIERL KQEIDNAREL QEQRDSLTQK LQEVEIRNKD 
       310        320        330        340        350
LEGQLSELEQ RLEKSQSEQD AFRSNLKTLL EILDGKIFEL TELRDNLAKL 

LECS

Show »

Length:354

Mass (Da):40,124

Checksum:ⁱC8F4579BFE3E69BF

GO

Isoform 3 (identifier: Q9Z214-3) [UniParc]FASTA Add to basket

Also known as: 1a, Vesl

The sequence of this isoform differs from the canonical sequence as follows:
176-186: SAGDRTQGLSH → RYTFNSAIMIK
187-366: Missing.

« Hide

        10         20         30         40         50
MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL 
        60         70         80         90        100
DGSKAIINST ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA 
       110        120        130        140        150
EKFQEFKEAA RLAKEKSQEK MELTSTPSQE SAGGDLQSPL TPESINGTDD 
       160        170        180 
ERTPDVTQNS EPRAEPAQNA LPFSHRYTFN SAIMIK

Show »

Length:186

Mass (Da):20,872

Checksum:ⁱ9845DA6E2574BF83

GO

Sequence cautionⁱ

The sequence AAC53113 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Sequence conflictⁱ	268 – 268	1	L → R in BAA32477 (PubMed:9727012).Curated

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	176 – 187	12	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.3 "Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins." Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D., Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F. Neuron 21:707-716(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), CHARACTERIZATION, INTERACTION WITH GRM1 AND GRM5.	VSP_009066	Add BLAST
Alternative sequenceⁱ	176 – 186	11	SAGDRTQGLSH → RYTFNSAIMIK in isoform 3. 5 Publications Manual assertion based on opinion inⁱ Ref.1 "Homer: a protein that selectively binds metabotropic glutamate receptors." Brakeman P.R., Lanahan A.A., O'Brien R., Roche K., Barnes C.A., Huganir R.L., Worley P.F. Nature 386:284-288(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH GRM1 AND GRM5. Ref.2 "Vesl, a gene encoding VASP/Ena family related protein, is upregulated during seizure, long-term potentiation and synaptogenesis." Kato A., Ozawa F., Saitoh Y., Hirai K., Inokuchi K. FEBS Lett. 412:183-189(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION. Ref.3 "Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins." Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D., Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F. Neuron 21:707-716(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), CHARACTERIZATION, INTERACTION WITH GRM1 AND GRM5. Ref.4 "Isolation of PSD-Zip45, a novel Homer/vesl family protein containing leucine zipper motifs, from rat brain." Sun J., Tadokoro S., Imanaka T., Murakami S.D., Nakamura M., Kashiwada K., Ko J., Nishida W., Sobue K. FEBS Lett. 437:304-308(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Ref.6 "Evidence for the presence of two homer 1 transcripts in skeletal and cardiac muscles." Sandona D., Tibaldo E., Volpe P. Biochem. Biophys. Res. Commun. 279:348-353(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY.	VSP_009067	Add BLAST
Alternative sequenceⁱ	187 – 366	180	Missing in isoform 3. 5 Publications Manual assertion based on opinion inⁱ Ref.1 "Homer: a protein that selectively binds metabotropic glutamate receptors." Brakeman P.R., Lanahan A.A., O'Brien R., Roche K., Barnes C.A., Huganir R.L., Worley P.F. Nature 386:284-288(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH GRM1 AND GRM5. Ref.2 "Vesl, a gene encoding VASP/Ena family related protein, is upregulated during seizure, long-term potentiation and synaptogenesis." Kato A., Ozawa F., Saitoh Y., Hirai K., Inokuchi K. FEBS Lett. 412:183-189(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION. Ref.3 "Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins." Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D., Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F. Neuron 21:707-716(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), CHARACTERIZATION, INTERACTION WITH GRM1 AND GRM5. Ref.4 "Isolation of PSD-Zip45, a novel Homer/vesl family protein containing leucine zipper motifs, from rat brain." Sun J., Tadokoro S., Imanaka T., Murakami S.D., Nakamura M., Kashiwada K., Ko J., Nishida W., Sobue K. FEBS Lett. 437:304-308(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Ref.6 "Evidence for the presence of two homer 1 transcripts in skeletal and cardiac muscles." Sandona D., Tibaldo E., Volpe P. Biochem. Biophys. Res. Commun. 279:348-353(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY.	VSP_009068	Add BLAST

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U92079 mRNA. Translation: AAC53113.1. Different initiation. AB003726 mRNA. Translation: BAA21671.1. AF093267 mRNA. Translation: AAC71031.1. AF093268 mRNA. Translation: AAC71032.1. AB017140 mRNA. Translation: BAA34311.1. AB007688 mRNA. Translation: BAA32477.1. AJ276327 mRNA. Translation: CAB77249.1. AJ276328 mRNA. Translation: CAB77250.1.
RefSeqⁱ	NP_113895.1. NM_031707.1. [Q9Z214-1] XP_006231837.1. XM_006231775.2. [Q9Z214-2]
UniGeneⁱ	Rn.37500.

Genome annotation databases

Ensemblⁱ	ENSRNOT00000073871; ENSRNOP00000066634; ENSRNOG00000047014. [Q9Z214-2]
GeneIDⁱ	29546.
KEGGⁱ	rno:29546.

Keywords - Coding sequence diversityⁱ

Alternative splicing

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U92079 mRNA. Translation: AAC53113.1. Different initiation. AB003726 mRNA. Translation: BAA21671.1. AF093267 mRNA. Translation: AAC71031.1. AF093268 mRNA. Translation: AAC71032.1. AB017140 mRNA. Translation: BAA34311.1. AB007688 mRNA. Translation: BAA32477.1. AJ276327 mRNA. Translation: CAB77249.1. AJ276328 mRNA. Translation: CAB77250.1.
RefSeqⁱ	NP_113895.1. NM_031707.1. [Q9Z214-1] XP_006231837.1. XM_006231775.2. [Q9Z214-2]
UniGeneⁱ	Rn.37500.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DDV	X-ray	1.90	A	1-111	[»]
1DDW	X-ray	1.70	A	1-120	[»]
1I2H	X-ray	1.80	A	1-163	[»]
3CVE	X-ray	1.75	A/B/C/D	302-366	[»]

ProteinModelPortalⁱ

Q9Z214.

SMRⁱ

Q9Z214. Positions 1-143.

ModBaseⁱ

Search...

MobiDBⁱ

Search...

Protein-protein interaction databases

BioGridⁱ	248180. 11 interactions.
IntActⁱ	Q9Z214. 9 interactions.
MINTⁱ	MINT-1891037.
STRINGⁱ	10116.ENSRNOP00000065989.

PTM databases

iPTMnetⁱ	Q9Z214.
PhosphoSiteⁱ	Q9Z214.

Proteomic databases

PaxDbⁱ	Q9Z214.
PRIDEⁱ	Q9Z214.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000073871; ENSRNOP00000066634; ENSRNOG00000047014. [Q9Z214-2]
GeneIDⁱ	29546.
KEGGⁱ	rno:29546.

Organism-specific databases

CTDⁱ	9456.
RGDⁱ	628725. Homer1.

Phylogenomic databases

eggNOGⁱ	ENOG410IGRQ. Eukaryota. ENOG410XQWT. LUCA.
GeneTreeⁱ	ENSGT00390000017850.
HOVERGENⁱ	HBG051918.
InParanoidⁱ	Q9Z214.
KOⁱ	K15010.
OrthoDBⁱ	EOG091G0CQ0.
PhylomeDBⁱ	Q9Z214.

Miscellaneous databases

EvolutionaryTraceⁱ	Q9Z214.
PROⁱ	Q9Z214.

Gene expression databases

Bgeeⁱ	ENSRNOG00000047014.
ExpressionAtlasⁱ	Q9Z214. baseline and differential.
Genevisibleⁱ	Q9Z214. RN.

Family and domain databases

Gene3Dⁱ	2.30.29.30. 1 hit.
InterProⁱ	IPR011993. PH_dom-like. IPR000697. WH1/EVH1_dom. [Graphical view]
Pfamⁱ	PF00568. WH1. 1 hit. [Graphical view]
SMARTⁱ	SM00461. WH1. 1 hit. [Graphical view]
SUPFAMⁱ	SSF50729. SSF50729. 1 hit.
PROSITEⁱ	PS50229. WH1. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

HOME1_RAT

Accessionⁱ

Primary (citable) accession number: Q9Z214
Secondary accession number(s): O08567

Q9QWN5

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	November 28, 2003
Last modified:	September 7, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9Z214 (HOME1_RAT)

UniProt

Q9Z214 - HOME1_RAT

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Homer protein homolog 1

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/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><p><a href='../manual/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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

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

Mutagenesis

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

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

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

Gene expression databases

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

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

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

Domains and Repeats

Coiled coil

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>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><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

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

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM 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>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/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

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (3)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ