Q9Y4F1 (FARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FERM, RhoGEF and pleckstrin domain-containing protein 1

Alternative name(s):
Chondrocyte-derived ezrin-like protein
Pleckstrin homology domain-containing family C member 2
Short name=PH domain-containing family C member 2

Gene names

Name:	FARP1
Synonyms:	CDEP, PLEKHC2

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	1045 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses By similarity.
Subunit structure	Interacts with CADM1. Interacts with RAC1 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction › synapse. Cell junction › synapse › synaptosome By similarity. Cytoplasm › cytosol By similarity. Cell projection › filopodium By similarity. Cell projection › dendrite By similarity. Cell projection › dendritic spine By similarity. Note: Recruited to the cell membrane via interaction with CADM1 By similarity.
Tissue specificity	Detected in cAMP-treated chondrocytes, but not in untreated chondrocytes. Detected in fetal brain, heart and spleen, and in adult testis, kidney and lung. Ref.1
Induction	Up-regulated in response to cAMP in cultured embryonic chondrocytes. Ref.1
Domain	Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation. Ref.12
Sequence similarities	Contains 1 DH (DBL-homology) domain. Contains 1 FERM domain. Contains 2 PH domains.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Developmental protein Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dendrite morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of phosphatase activity Inferred from direct assay PubMed 19389623. Source: UniProtKB regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro synapse assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoskeleton Traceable author statement Ref.1. Source: ProtInc cytosol Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from sequence or structural similarity. Source: UniProtKB extrinsic to internal side of plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	Rac guanyl-nucleotide exchange factor activity Inferred from sequence or structural similarity. Source: UniProtKB phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y4F1-1)

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.

Isoform 2 (identifier: Q9Y4F1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     758-758: R → RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9Y4F1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     58-129: QRAPGKVLLD...FPPDHTQLQE → MVSSSSFLKA...TVTEELLNLF
     130-1045: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1045	1045	FERM, RhoGEF and pleckstrin domain-containing protein 1		PRO_0000232753
Regions
	Domain	40 – 320	281	FERM
	Domain	540 – 730	191	DH
	Domain	759 – 856	98	PH 1
	Domain	932 – 1029	98	PH 2
	Compositional bias	449 – 453	5	Poly-Glu
Amino acid modifications
	Modified residue	24	1	Phosphothreonine Ref.7 Ref.9
	Modified residue	340	1	Phosphoserine Ref.7
	Modified residue	427	1	Phosphoserine Ref.5 Ref.6 Ref.9
	Modified residue	510	1	Phosphoserine Ref.9
	Modified residue	514	1	Phosphoserine Ref.9
	Modified residue	872	1	Phosphoserine Ref.11
	Modified residue	889	1	Phosphoserine Ref.8 Ref.11
Natural variations
	Alternative sequence	58 – 129	72	QRAPG…TQLQE → MVSSSSFLKATGSSWTGWVL RCSMKPKHHSHLIEKFGEDR ILTHLTGSISYTNWAGSRSL AVTVTEELLNLF in isoform 3.		VSP_040989
	Alternative sequence	130 – 1045	916	Missing in isoform 3.		VSP_040990
	Alternative sequence	758	1	R → RPGSFSLMRTPHLGQARRIP CAPERRPLLLVK in isoform 2.		VSP_017976
	Natural variant	8	1	P → L. Corresponds to variant rs9300466 [ dbSNP | Ensembl ].		VAR_048362
	Natural variant	714	1	R → L in a breast cancer sample; somatic mutation. Ref.13		VAR_035851
Experimental info
	Sequence conflict	644	1	H → Y in AAH71592. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 0E8B2D61C0F58417	FASTA	1,045	118,633
	10 20 30 40 50 60 MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA 70 80 90 100 110 120 PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF 130 140 150 160 170 180 PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL 190 200 210 220 230 240 AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI 250 260 270 280 290 300 NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD 310 320 330 340 350 360 FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ 370 380 390 400 410 420 FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG 430 440 450 460 470 480 EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL 490 500 510 520 530 540 SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK 550 560 570 580 590 600 AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK 610 620 630 640 650 660 EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR 670 680 690 700 710 720 LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI 730 740 750 760 770 780 TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGREF IRLGSLSKLS GKGLQQRMFF 790 800 810 820 830 840 LFNDVLLYTS RGLTASNQFK VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS 850 860 870 880 890 900 RSEMEKWVED IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL 910 920 930 940 950 960 ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ KLWVVFTNFC 970 980 990 1000 1010 1020 LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL HFKSHVYYFR AESEYTFERW 1030 1040 MEVIRSATSS ASRPHVLSHK ESLVY
	Isoform 2 [UniParc]. Checksum: 25A71B2C8C60A280	FASTA	1,076	122,113
	10 20 30 40 50 60 MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA 70 80 90 100 110 120 PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF 130 140 150 160 170 180 PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL 190 200 210 220 230 240 AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI 250 260 270 280 290 300 NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD 310 320 330 340 350 360 FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ 370 380 390 400 410 420 FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG 430 440 450 460 470 480 EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL 490 500 510 520 530 540 SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK 550 560 570 580 590 600 AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK 610 620 630 640 650 660 EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR 670 680 690 700 710 720 LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI 730 740 750 760 770 780 TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGRPG SFSLMRTPHL GQARRIPCAP 790 800 810 820 830 840 ERRPLLLVKE FIRLGSLSKL SGKGLQQRMF FLFNDVLLYT SRGLTASNQF KVHGQLPLYG 850 860 870 880 890 900 MTIEESEDEW GVPHCLTLRG QRQSIIVAAS SRSEMEKWVE DIQMAIDLAE KSSSPAPEFL 910 920 930 940 950 960 ASSPPDNKSP DEATAADQES EDDLSASRTS LERQAPHRGN TMVHVCWHRN TSVSMVDFSI 970 980 990 1000 1010 1020 AVENQLSGNL LRKFKNSNGW QKLWVVFTNF CLFFYKSHQD NHPLASLPLL GYSLTIPSES 1030 1040 1050 1060 1070 ENIQKDYVFK LHFKSHVYYF RAESEYTFER WMEVIRSATS SASRPHVLSH KESLVY
	Isoform 3 [UniParc]. Checksum: ED33383FA354AB1E	FASTA	129	14,138
	10 20 30 40 50 60 MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPMVS 70 80 90 100 110 120 SSSFLKATGS SWTGWVLRCS MKPKHHSHLI EKFGEDRILT HLTGSISYTN WAGSRSLAVT VTEELLNLF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of CDEP, a novel human protein containing the ezrin-like domain of the band 4.1 superfamily and the Dbl homology domain of rho guanine nucleotide exchange factors." Koyano Y., Kawamoto T., Shen M., Yan W., Noshiro M., Fujii K., Kato Y. Biochem. Biophys. Res. Commun. 241:369-375(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY. Tissue: Cartilage.
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORMS 1; 2 AND 3). Tissue: Brain, Placenta and Skin.
[4]	"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(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[5]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, MASS SPECTROMETRY. Tissue: Liver.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-427; SER-510 AND SER-514, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"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-872 AND SER-889, MASS SPECTROMETRY.
[12]	"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2." He X., Kuo Y.C., Rosche T.J., Zhang X. Structure 21:355-364(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.09 ANGSTROMS) OF 539-1035, DOMAIN.
[13]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-714.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB008430 mRNA. Translation: BAA24267.1.
AL136300, AL445223 Genomic DNA. Translation: CAI10952.1.
AL136300, AL137249, AL161896 Genomic DNA. Translation: CAI10953.1.
AL161896, AL136300, AL137249 Genomic DNA. Translation: CAI12946.1.
AL445223, AL136300 Genomic DNA. Translation: CAI15981.1.
AL137249, AL136300, AL161896 Genomic DNA. Translation: CAI39458.1.
BC041595 mRNA. Translation: AAH41595.1.
BC065020 mRNA. No translation available.
BC071592 mRNA. Translation: AAH71592.1.

IPI

IPI00024773.
IPI00418590.
IPI00746455.

PIR

JC5795.

RefSeq

NP_001001715.2. NM_001001715.2.
NP_005757.1. NM_005766.2.

UniGene

Hs.403917.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4H6Y	X-ray	4.09	A/B	539-1035	[»]

ProteinModelPortal

Q9Y4F1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y4F1. 1 interaction.

STRING

9606.ENSP00000322926.

PTM databases

PhosphoSite

Q9Y4F1.

Polymorphism databases

DMDM

74762059.

Proteomic databases

PaxDb

Q9Y4F1.

PRIDE

Q9Y4F1.

Protocols and materials databases

DNASU

10160.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000319562; ENSP00000322926; ENSG00000152767.
ENST00000376581; ENSP00000365765; ENSG00000152767.

GeneID

10160.

KEGG

hsa:10160.

UCSC

uc001vni.3. human.
uc001vnj.3. human.

Organism-specific databases

CTD

10160.

GeneCards

GC13P098795.

HGNC

HGNC:3591. FARP1.

HPA

HPA000760.

MIM

602654. gene.

neXtProt

NX_Q9Y4F1.

PharmGKB

PA28004.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282099.

HOGENOM

HOG000007957.

HOVERGEN

HBG081521.

OrthoDB

EOG4J3WG7.

PhylomeDB

Q9Y4F1.

Gene expression databases

ArrayExpress

Q9Y4F1.

Bgee

Q9Y4F1.

CleanEx

HS_FARP1.

Genevestigator

Q9Y4F1.

GermOnline

ENSG00000152767. Homo sapiens.

Family and domain databases

Gene3D

1.20.80.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 3 hits.

InterPro

IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR000219. DH-domain.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

Pfam

PF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]

PRINTS

PR00935. BAND41.
PR00661. ERMFAMILY.

SMART

SM00295. B41. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]

SUPFAM

SSF48065. DH-domain. 1 hit.
SSF47031. FERM_3-hlx. 1 hit.

PROSITE

PS00741. DH_1. False negative.
PS50010. DH_2. 1 hit.
PS00660. FERM_1. 1 hit.
PS00661. FERM_2. False negative.
PS50057. FERM_3. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

FARP1. human.

GenomeRNAi

10160.

NextBio

38464.

SOURCE

Search...

Entry information

Entry name

FARP1_HUMAN

Accession

Primary (citable) accession number: Q9Y4F1
Secondary accession number(s): Q5JVI9, Q6IQ29

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	November 1, 1999
Last modified:	May 29, 2013
This is version 105 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.