Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y4F1

- FARP1_HUMAN

UniProt

Q9Y4F1 - FARP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

FERM, RhoGEF and pleckstrin domain-containing protein 1

Gene

FARP1

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

Functioni

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).By similarity

GO - Molecular functioni

  1. Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
  2. Rho guanyl-nucleotide exchange factor activity Source: ProtInc

GO - Biological processi

  1. dendrite morphogenesis Source: UniProtKB
  2. negative regulation of phosphatase activity Source: UniProtKB
  3. positive regulation of Rac GTPase activity Source: GOC
  4. positive regulation of Rho GTPase activity Source: GOC
  5. synapse assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Guanine-nucleotide releasing factor

Names & Taxonomyi

Protein namesi
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 namesi
Name:FARP1
Synonyms:CDEP, PLEKHC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:3591. FARP1.

Subcellular locationi

Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junctionsynapse. Cell junctionsynapsesynaptosome By similarity. Cytoplasmcytosol By similarity. Cell projectionfilopodium By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity
Note: Recruited to the cell membrane via interaction with CADM1.By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: HPA
  3. cytoskeleton Source: ProtInc
  4. cytosol Source: UniProtKB
  5. dendrite Source: UniProtKB
  6. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  7. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28004.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10451045FERM, RhoGEF and pleckstrin domain-containing protein 1PRO_0000232753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphothreonine2 Publications
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei427 – 4271Phosphoserine3 Publications
Modified residuei510 – 5101Phosphoserine1 Publication
Modified residuei514 – 5141Phosphoserine1 Publication
Modified residuei872 – 8721Phosphoserine1 Publication
Modified residuei889 – 8891Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y4F1.
PaxDbiQ9Y4F1.
PRIDEiQ9Y4F1.

PTM databases

PhosphoSiteiQ9Y4F1.

Expressioni

Tissue specificityi

Detected in cAMP-treated chondrocytes, but not in untreated chondrocytes. Detected in fetal brain, heart and spleen, and in adult testis, kidney and lung.1 Publication

Inductioni

Up-regulated in response to cAMP in cultured embryonic chondrocytes.1 Publication

Gene expression databases

BgeeiQ9Y4F1.
CleanExiHS_FARP1.
ExpressionAtlasiQ9Y4F1. baseline and differential.
GenevestigatoriQ9Y4F1.

Organism-specific databases

HPAiHPA000760.

Interactioni

Subunit structurei

Interacts with CADM1. Interacts with RAC1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi115462. 3 interactions.
IntActiQ9Y4F1. 1 interaction.
STRINGi9606.ENSP00000322926.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4H6YX-ray4.09A/B539-1035[»]
ProteinModelPortaliQ9Y4F1.
SMRiQ9Y4F1. Positions 43-317, 539-1029.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 320281FERMPROSITE-ProRule annotationAdd
BLAST
Domaini540 – 730191DHPROSITE-ProRule annotationAdd
BLAST
Domaini759 – 85698PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini932 – 102998PH 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi449 – 4535Poly-Glu

Domaini

Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation.1 Publication

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG282099.
GeneTreeiENSGT00760000118823.
HOGENOMiHOG000007957.
HOVERGENiHBG081521.
InParanoidiQ9Y4F1.
KOiK17477.
OMAiEDRILTH.
OrthoDBiEOG7B5WVD.
PhylomeDBiQ9Y4F1.
TreeFamiTF351276.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 3 hits.
InterProiIPR019749. 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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08736. 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]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS00660. FERM_1. 1 hit.
PS50057. FERM_3. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4F1-1) [UniParc]FASTAAdd to Basket

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
MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT
60 70 80 90 100
QEAFEVPQRA PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP
110 120 130 140 150
IVKQIRRPKH VVVKFVVKFF PPDHTQLQEE LTRYLFALQV KQDLAQGRLT
160 170 180 190 200
CNDTSAALLI SHIVQSEIGD FDEALDREHL AKNKYIPQQD ALEDKIVEFH
210 220 230 240 250
HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI NLAVANTGIL
260 270 280 290 300
VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD
310 320 330 340 350
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY
360 370 380 390 400
VKEGGHKKVQ FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG
410 420 430 440 450
AESPGGQSCR RGKEPKVSAG EPGSHPSPAP RRSPAGNKQA DGAASAPTEE
460 470 480 490 500
EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL SELSVNSQGG VAPANVTLSP
510 520 530 540 550
NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK AYFIAKEVST
560 570 580 590 600
TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK
610 620 630 640 650
EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA
660 670 680 690 700
LENGIKSSRR LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC
710 720 730 740 750
KHHPPSHADF RDCRAALAEI TEMVAQLHGT MIKMENFQKL HELKKDLIGI
760 770 780 790 800
DNLVVPGREF IRLGSLSKLS GKGLQQRMFF LFNDVLLYTS RGLTASNQFK
810 820 830 840 850
VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS RSEMEKWVED
860 870 880 890 900
IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL
910 920 930 940 950
ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ
960 970 980 990 1000
KLWVVFTNFC LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL
1010 1020 1030 1040
HFKSHVYYFR AESEYTFERW MEVIRSATSS ASRPHVLSHK ESLVY
Length:1,045
Mass (Da):118,633
Last modified:November 1, 1999 - v1
Checksum:i0E8B2D61C0F58417
GO
Isoform 2 (identifier: Q9Y4F1-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,076
Mass (Da):122,113
Checksum:i25A71B2C8C60A280
GO
Isoform 3 (identifier: Q9Y4F1-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:129
Mass (Da):14,138
Checksum:iED33383FA354AB1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti644 – 6441H → Y in AAH71592. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81P → L.
Corresponds to variant rs9300466 [ dbSNP | Ensembl ].
VAR_048362
Natural varianti714 – 7141R → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_035851

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 12972QRAPG…TQLQE → MVSSSSFLKATGSSWTGWVL RCSMKPKHHSHLIEKFGEDR ILTHLTGSISYTNWAGSRSL AVTVTEELLNLF in isoform 3. 1 PublicationVSP_040989Add
BLAST
Alternative sequencei130 – 1045916Missing in isoform 3. 1 PublicationVSP_040990Add
BLAST
Alternative sequencei758 – 7581R → RPGSFSLMRTPHLGQARRIP CAPERRPLLLVK in isoform 2. 1 PublicationVSP_017976

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32000.1. [Q9Y4F1-3]
CCDS66572.1. [Q9Y4F1-2]
CCDS9487.1. [Q9Y4F1-1]
PIRiJC5795.
RefSeqiNP_001001715.2. NM_001001715.3. [Q9Y4F1-3]
NP_001273768.1. NM_001286839.1.
NP_005757.1. NM_005766.3. [Q9Y4F1-1]
XP_006719976.1. XM_006719913.1. [Q9Y4F1-1]
UniGeneiHs.403917.
Hs.709933.
Hs.729583.

Genome annotation databases

EnsembliENST00000319562; ENSP00000322926; ENSG00000152767. [Q9Y4F1-1]
ENST00000376581; ENSP00000365765; ENSG00000152767. [Q9Y4F1-3]
GeneIDi10160.
KEGGihsa:10160.
UCSCiuc001vni.3. human. [Q9Y4F1-3]
uc001vnj.3. human. [Q9Y4F1-1]

Polymorphism databases

DMDMi74762059.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32000.1. [Q9Y4F1-3 ]
CCDS66572.1. [Q9Y4F1-2 ]
CCDS9487.1. [Q9Y4F1-1 ]
PIRi JC5795.
RefSeqi NP_001001715.2. NM_001001715.3. [Q9Y4F1-3 ]
NP_001273768.1. NM_001286839.1.
NP_005757.1. NM_005766.3. [Q9Y4F1-1 ]
XP_006719976.1. XM_006719913.1. [Q9Y4F1-1 ]
UniGenei Hs.403917.
Hs.709933.
Hs.729583.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4H6Y X-ray 4.09 A/B 539-1035 [» ]
ProteinModelPortali Q9Y4F1.
SMRi Q9Y4F1. Positions 43-317, 539-1029.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115462. 3 interactions.
IntActi Q9Y4F1. 1 interaction.
STRINGi 9606.ENSP00000322926.

PTM databases

PhosphoSitei Q9Y4F1.

Polymorphism databases

DMDMi 74762059.

Proteomic databases

MaxQBi Q9Y4F1.
PaxDbi Q9Y4F1.
PRIDEi Q9Y4F1.

Protocols and materials databases

DNASUi 10160.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319562 ; ENSP00000322926 ; ENSG00000152767 . [Q9Y4F1-1 ]
ENST00000376581 ; ENSP00000365765 ; ENSG00000152767 . [Q9Y4F1-3 ]
GeneIDi 10160.
KEGGi hsa:10160.
UCSCi uc001vni.3. human. [Q9Y4F1-3 ]
uc001vnj.3. human. [Q9Y4F1-1 ]

Organism-specific databases

CTDi 10160.
GeneCardsi GC13P098795.
HGNCi HGNC:3591. FARP1.
HPAi HPA000760.
MIMi 602654. gene.
neXtProti NX_Q9Y4F1.
PharmGKBi PA28004.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282099.
GeneTreei ENSGT00760000118823.
HOGENOMi HOG000007957.
HOVERGENi HBG081521.
InParanoidi Q9Y4F1.
KOi K17477.
OMAi EDRILTH.
OrthoDBi EOG7B5WVD.
PhylomeDBi Q9Y4F1.
TreeFami TF351276.

Miscellaneous databases

ChiTaRSi FARP1. human.
GeneWikii FARP1.
GenomeRNAii 10160.
NextBioi 38464.
PROi Q9Y4F1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y4F1.
CleanExi HS_FARP1.
ExpressionAtlasi Q9Y4F1. baseline and differential.
Genevestigatori Q9Y4F1.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 3 hits.
InterProi 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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami 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 ]
PRINTSi PR00935. BAND41.
PR00661. ERMFAMILY.
SMARTi SM00295. B41. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF47031. SSF47031. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50010. DH_2. 1 hit.
PS00660. FERM_1. 1 hit.
PS50057. FERM_3. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-714.

Entry informationi

Entry nameiFARP1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4F1
Secondary accession number(s): Q5JVI9, Q6IQ29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 119 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, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3