Q14CM0 (FRPD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FRMPD4
Synonyms:	KIAA0316, PDZD10, PDZK10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Positive regulator of dendritic spine morphogenesis and density. Required for the maintenance of excitatory synaptic transmission. Binds phosphatidylinositol 4,5-bisphosphate. Ref.5
Subunit structure	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. Ref.5
Subcellular location	Cell projection › dendritic spine Ref.5.
Domain	The FERM domain mediates the interaction with phosphatidylinositol 4,5-bisphosphate. Ref.5
Sequence similarities	Contains 1 FERM domain. Contains 1 PDZ (DHR) domain. Contains 1 WW domain.

Ontologies

Keywords
Cellular component	Cell projection
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of synapse structural plasticity Inferred from mutant phenotype Ref.5. Source: UniProtKB
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: InterPro dendritic spine Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	phosphatidylinositol-4,5-bisphosphate binding Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1322	1322	FERM and PDZ domain-containing protein 4		PRO_0000307132
Regions
	Domain	33 – 66	34	WW
	Domain	78 – 155	78	PDZ
	Domain	204 – 519	316	FERM
Amino acid modifications
	Modified residue	1252	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	102	1	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. Ref.5
	Mutagenesis	1319 – 1322	4	Missing: Abolishes the interaction with DLG1, DLG2, DLG3 and DLG4/PSD95. Reduces protein localization to dendritic spines. Ref.5
	Mutagenesis	1320	1	T → D: Abolishes the interaction with DLG4/PSD95. Reduces protein localization to dendritic spines. Ref.5
	Sequence conflict	130	1	A → T in BAA20774. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q14CM0 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 79B73E41B89E2D08	FASTA	1,322	144,379
	10 20 30 40 50 60 MDVFSFVKIA KLSSHRTKSS GWPPPSGTWG LSQVPPYGWE MTANRDGRDY FINHMTQAIP 70 80 90 100 110 120 FDDPRLESCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV VRSVTPGGPS EGKLIPGDQI 130 140 150 160 170 180 VMINDEPVSA APRERVIDLV RSCKESILLT VIQPYPSPKS AFISAAKKAR LKSNPVKVRF 190 200 210 220 230 240 SEEVIINGQV SETVKDNSLL FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK 250 260 270 280 290 300 GIEHFSLMLE QRTEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR 310 320 330 340 350 360 DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK ISLKYIEKEW 370 380 390 400 410 420 GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL SALQAKVHYL KFLSDLRLYG 430 440 450 460 470 480 GRVFKATLVQ AEKRSEVTLL VGPRYGISHV INTKTNLVAL LADFSHVNRI EMFSEEESLV 490 500 510 520 530 540 RVELHVLDVK PITLLMESSD AMNLACLTAG YYRLLVDSRR SIFNMANKKN TATQETGPEN 550 560 570 580 590 600 KGKHNLLGPD WNCIPQMTTF IGEGEQEAQI TYIDSKQKTV EITDSTMCPK EHRHLYIDNA 610 620 630 640 650 660 YSSDGLNQQL SQPGEAPCEA DYRSLAQRSL LTLSGPETLK KAQESPRGAK VSFIFGDFAL 670 680 690 700 710 720 DDGISPPTLG YETLLDEGPE MLEKQRNLYI GSANDMKGLD LTPEAEGIQF VENSVYANIG 730 740 750 760 770 780 DVKSFQAAEG IEEPLLHDIC YAENTDDAED EDEVSCEEDL VVGEMNQPAI LNLSGSSDDI 790 800 810 820 830 840 IDLTSLPPPE GDDNEDDFLL RSLNMAIAAP PPGFRDSSDE EDSQSQAASF PEDKEKGSSL 850 860 870 880 890 900 QNDEIPVSLI DAVPTSAEGK CEKGLDNAVV STLGALEALS VSEEQQTSDN SGVAILRAYS 910 920 930 940 950 960 PESSSDSGNE TNSSEMTESS ELATAQKQSE NLSRMFLATH EGYHPLAEEQ TEFPASKTPA 970 980 990 1000 1010 1020 GGLPPKSSHA LAARPATDLP PKVVPSKQLL HSDHMEMEPE TMETKSVTDY FSKLHMGSVA 1030 1040 1050 1060 1070 1080 YSCTSKRKSK LADGEGKAPP NGNTTGKKQQ GTKTAEMEEE ASGKFGTVSS RDSQHLSTFN 1090 1100 1110 1120 1130 1140 LERTAFRKDS QRWYVATEGG MAEKSGLEAA TGKTFPRASG LGAREAEGKE EGAPDGETSD 1150 1160 1170 1180 1190 1200 GSGLGQGDRF LTDVTCASSA KDLDNPEDAD SSTCDHPSKL PEADESVARL CDYHLAKRMS 1210 1220 1230 1240 1250 1260 SLQSEGHFSL QSSQGSSVDA GCGTGSSGSA CATPVESPLC PSLGKHLIPD ASGKGVNYIP 1270 1280 1290 1300 1310 1320 SEERAPGLPN HGATFKELHP QTEGMCPRMT VPALHTAINT EPLFGTLRDG CHRLPKIKET TV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[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]. Tissue: Brain.
[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.
[6]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB002314 mRNA. Translation: BAA20774.3. AK289694 mRNA. Translation: BAF82383.1. BC113700 mRNA. Translation: AAI13701.1. BC113702 mRNA. Translation: AAI13703.1.
IPI	IPI00187159.
RefSeq	NP_055543.2. NM_014728.3.
UniGene	Hs.657507.
3D structure databases
ProteinModelPortal	Q14CM0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14CM0. 3 interactions.
MINT	MINT-2795491.
STRING	9606.ENSP00000370057.
PTM databases
PhosphoSite	Q14CM0.
Polymorphism databases
DMDM	121948742.
Proteomic databases
PaxDb	Q14CM0.
PRIDE	Q14CM0.
Protocols and materials databases
DNASU	9758.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380682; ENSP00000370057; ENSG00000169933.
GeneID	9758.
KEGG	hsa:9758.
UCSC	uc004cuz.2. human.
Organism-specific databases
CTD	9758.
GeneCards	GC0XP012066.
H-InvDB	HIX0016653.
HGNC	HGNC:29007. FRMPD4.
HPA	HPA035580.
MIM	300838. gene.
neXtProt	NX_Q14CM0.
PharmGKB	PA134977575.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG237011.
HOGENOM	HOG000090222.
HOVERGEN	HBG106593.
OMA	QETGTEN.
OrthoDB	EOG461438.
Gene expression databases
Bgee	Q14CM0.
CleanEx	HS_FRMPD4.
Genevestigator	Q14CM0.
Family and domain databases
Gene3D	1.20.80.10. 1 hit.
InterPro	IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR000299. FERM_domain. IPR001478. PDZ. IPR001202. WW_dom. [Graphical view]
Pfam	PF00373. FERM_M. 1 hit. PF00595. PDZ. 1 hit. [Graphical view]
SMART	SM00295. B41. 1 hit. SM00228. PDZ. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit. SSF50156. PDZ. 1 hit.
PROSITE	PS00660. FERM_1. False negative. PS00661. FERM_2. False negative. PS50057. FERM_3. 1 hit. PS50106. PDZ. 1 hit. PS01159. WW_DOMAIN_1. False negative. PS50020. WW_DOMAIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FRMPD4. human.
GenomeRNAi	9758.
NextBio	36727.
SOURCE	Search...

Entry information

Entry name

FRPD4_HUMAN

Accession

Primary (citable) accession number: Q14CM0
Secondary accession number(s): A8K0X9, O15032

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	August 22, 2006
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.