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Q7L576 (CYFP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic FMR1-interacting protein 1
Alternative name(s):
Specifically Rac1-associated protein 1
Short name=Sra-1
p140sra-1
Gene names
Name:CYFIP1
Synonyms:KIAA0068
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1253 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA By similarity. Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers. Ref.7 Ref.8 Ref.9 Ref.11

Subunit structure

Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterdimer containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by WAVE1, ABI2 and BRK1. Component of the CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not bind to related proteins FXR1 or FXR2. Interaction with EIF4E stimulates FMR1 binding. Component of the WAVE2 complex composed of ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Interacts with the active GTP-bound form of RAC1. Interacts through its C-terminus with the C-terminus of DPYSL2/CRMP2 which is necessary for DPYSL2-induced axon outgrowth. Interacts with NYAP1, NYAP2 and MYO16. Ref.8 Ref.11

Subcellular location

Cytoplasmperinuclear region By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Cell junctionsynapsesynaptosome By similarity. Note: Highly expressed in the perinuclear region. Enriched in synaptosomes, membrane ruffles and at the tips of lamellipodia By similarity.

Miscellaneous

Breakpoint hotspot for the Prader-Willi/Angelman syndromes and may be implicated in autism. Commonly altered in tumors.

Sequence similarities

Belongs to the CYFIP family.

Sequence caution

The sequence BAA07552.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell shape
Differentiation
Neurogenesis
   Cellular componentCell junction
Cell projection
Cytoplasm
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandActin-binding
   Molecular functionDevelopmental protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from mutant phenotype Ref.11. Source: UniProt

axon extension

Inferred from mutant phenotype Ref.8. Source: UniProtKB

cognition

Inferred from mutant phenotype PubMed 17519220. Source: UniProt

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Arp2/3 complex-mediated actin nucleation

Inferred from mutant phenotype Ref.11. Source: UniProt

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

ruffle organization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentSCAR complex

Inferred from mutant phenotype Ref.11. Source: UniProt

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA cap binding complex

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRac GTPase binding

Inferred from sequence or structural similarity. Source: UniProtKB

actin filament binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 18560548. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Eif4eP630732EBI-1048143,EBI-2000006From a different organism.
FMR1Q067874EBI-1048143,EBI-366305
NCKAP1Q9Y2A73EBI-1048143,EBI-389845

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.8 (identifier: Q7L576-1)

Also known as: 3;

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 Ref.8 (identifier: Q7L576-2)

Also known as: 4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-431: Missing.
     432-557: AEEYERATRY...PRRAVGPSST → MAESLGSAEL...SPPQMFPWII
Isoform 3 Ref.8 (identifier: Q7L576-3)

Also known as: 5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-806: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12531253Cytoplasmic FMR1-interacting protein 1
PRO_0000279706

Natural variations

Alternative sequence1 – 806806Missing in isoform 3. Ref.8
VSP_052345
Alternative sequence1 – 431431Missing in isoform 2. Ref.8
VSP_052346
Alternative sequence432 – 557126AEEYE…GPSST → MAESLGSAELLRQLKSLGME RLLHAVNTFLRQSCTYLPLL TFGGKTSFVSLDVYGTEANC SATSCSFPKAAATWPRRQAP GPLGELVRGPPDQGVAEQSF SHGLFEFGITNVPCIFSPPQ MFPWII in isoform 2. Ref.8
VSP_052347
Natural variant5321A → P.
Corresponds to variant rs34683919 [ dbSNP | Ensembl ].
VAR_053849
Natural variant8201G → D.
Corresponds to variant rs17137190 [ dbSNP | Ensembl ].
VAR_053850
Natural variant8201G → S. Ref.1 Ref.3
Corresponds to variant rs7170637 [ dbSNP | Ensembl ].
VAR_053851

Experimental info

Mutagenesis1791C → R: Reduced interaction with RAC1. Ref.11
Mutagenesis1901R → D: Reduced interaction with RAC1. Ref.11
Mutagenesis4341E → K: Reduced interaction with RAC1; when associated with A-626. Ref.11
Mutagenesis6261F → A: Reduced interaction with RAC1; when associated with K-434. Ref.11
Mutagenesis6321M → D: Reduced interaction with RAC1. Ref.11
Mutagenesis6971L → D: Constitutive induction of the formation of actin filaments; when associated with D-704. Ref.11
Mutagenesis7041Y → D: Constitutive induction of the formation of actin filaments; when associated with D-697. Ref.11
Mutagenesis8411L → A: Constitutive induction of the formation of actin filaments; when associated with 844-A-A-845. Ref.11
Mutagenesis844 – 8452FW → AA: Constitutive induction of the formation of actin filaments; when associated with A-841.
Sequence conflict5831S → N in AAW51478. Ref.1
Sequence conflict5831S → N in BAC86825. Ref.3
Sequence conflict8981Y → H in AAW51478. Ref.1
Sequence conflict8981Y → H in BAC86825. Ref.3
Sequence conflict9301M → R in AAW51478. Ref.1
Sequence conflict9301M → R in BAC86825. Ref.3
Sequence conflict11761V → A in AAW51479. Ref.1

Secondary structure

................................................................................................................................................................. 1253
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (3) [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D8F45E13207BEF16

FASTA1,253145,182
        10         20         30         40         50         60 
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN AFVTGIARYI 

        70         80         90        100        110        120 
EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT 

       130        140        150        160        170        180 
KLMNFMYFQR NAIERFCGEV RRLCHAERRK DFVSEAYLIT LGKFINMFAV LDELKNMKCS 

       190        200        210        220        230        240 
VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD 

       250        260        270        280        290        300 
IVNLCVDYYE NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK 

       310        320        330        340        350        360 
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCTSSGSS PQYNICEQMI QIREDHMRFI 

       370        380        390        400        410        420 
SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL LSQWSAHVME VYSWKLVHPT 

       430        440        450        460        470        480 
DKYSNKDCPD SAEEYERATR YNYTSEEKFA LVEVIAMIKG LQVLMGRMES VFNHAIRHTV 

       490        500        510        520        530        540 
YAALQDFSQV TLREPLRQAI KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK 

       550        560        570        580        590        600 
SGFDIKVPRR AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF 

       610        620        630        640        650        660 
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD HILETKEASM 

       670        680        690        700        710        720 
MEYVLYSLDL YNDSAHYALT RFNKQFLYDE IEAEVNLCFD QFVYKLADQI FAYYKVMAGS 

       730        740        750        760        770        780 
LLLDKRLRSE CKNQGATIHL PPSNRYETLL KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL 

       790        800        810        820        830        840 
ELAIGRFESE DLTSIVELDG LLEINRMTHK LLSRYLTLDG FDAMFREANH NVSAPYGRIT 

       850        860        870        880        890        900 
LHVFWELNYD FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS 

       910        920        930        940        950        960 
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK TLMEVMPKIC 

       970        980        990       1000       1010       1020 
RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV GNAILFCLLI EQSLSLEEVC 

      1030       1040       1050       1060       1070       1080 
DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL ESKYAPLHLV PLIERLGTPQ QIAIAREGDL 

      1090       1100       1110       1120       1130       1140 
LTKERLCCGL SMFEVILTRI RSFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI 

      1150       1160       1170       1180       1190       1200 
PVGTHEFTVE QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP 

      1210       1220       1230       1240       1250 
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GEGTPVEHVR CFQPPIHQSL ASS 

« Hide

Isoform 2 (4) [UniParc].

Checksum: 035E45763DC5F6C4
Show »

FASTA82294,467
Isoform 3 (5) [UniParc].

Checksum: 1D9F2A088E5891A2
Show »

FASTA44751,534

References

« Hide 'large scale' references
[1]Jiang Y.-H., Beaudet A.L.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-820.
[2]"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2), VARIANT SER-820.
Tissue: Brain and Placenta.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Brain and Placenta.
[6]Bienvenut W.V., Claeys D., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 50-58; 111-130; 151-163; 366-377; 441-448; 505-515; 564-573; 754-760; 815-826; 867-877; 1054-1076; 1211-1224 AND 1228-1240, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Hepatoma.
[7]"p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase."
Kobayashi K., Kuroda S., Fukata M., Nakamura T., Nagase T., Nomura N., Matsuura Y., Yoshida-Kubomura N., Iwamatsu A., Kaibuchi K.
J. Biol. Chem. 273:291-295(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation."
Kawano Y., Yoshimura T., Tsuboi D., Kawabata S., Kaneko-Kawano T., Shirataki H., Takenawa T., Kaibuchi K.
Mol. Cell. Biol. 25:9920-9935(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DPYSL2.
[9]"Cyfip1 is a putative invasion suppressor in epithelial cancers."
Silva J.M., Ezhkova E., Silva J., Heart S., Castillo M., Campos Y., Castro V., Bonilla F., Cordon-Cardo C., Muthuswamy S.K., Powers S., Fuchs E., Hannon G.J.
Cell 137:1047-1061(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"Structure and control of the actin regulatory WAVE complex."
Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M., Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.
Nature 468:533-538(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, FUNCTION, INTERACTION WITH RAC1, MUTAGENESIS OF CYS-179; ARG-190; GLU-434; PHE-626; MET-632; LEU-697; TYR-704; LEU-841 AND 844-PHE-TRP-845, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY763577 mRNA. Translation: AAW51476.1.
AY763578 mRNA. Translation: AAW51477.1.
AY763579 mRNA. Translation: AAW51478.1.
AY763580 mRNA. Translation: AAW51479.1.
D38549 mRNA. Translation: BAA07552.1. Different initiation.
AK127094 mRNA. Translation: BAC86825.1.
AK291604 mRNA. Translation: BAF84293.1.
CH471258 Genomic DNA. Translation: EAW65555.1.
BC001306 mRNA. Translation: AAH01306.2.
BC005097 mRNA. Translation: AAH05097.1.
CCDSCCDS10009.1. [Q7L576-1]
CCDS45189.1. [Q7L576-2]
RefSeqNP_001028200.1. NM_001033028.1. [Q7L576-2]
NP_001274739.1. NM_001287810.1. [Q7L576-1]
NP_055423.1. NM_014608.3. [Q7L576-1]
XP_005272600.1. XM_005272543.1. [Q7L576-1]
UniGeneHs.26704.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29A1-1253[»]
4N78X-ray2.43A1-1253[»]
ProteinModelPortalQ7L576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116800. 26 interactions.
DIPDIP-38873N.
IntActQ7L576. 23 interactions.
MINTMINT-1731056.
STRING9606.ENSP00000324549.

PTM databases

PhosphoSiteQ7L576.

Polymorphism databases

DMDM74738589.

Proteomic databases

MaxQBQ7L576.
PaxDbQ7L576.
PRIDEQ7L576.

Protocols and materials databases

DNASU23191.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313077; ENSP00000324549; ENSG00000068793. [Q7L576-1]
ENST00000435939; ENSP00000405956; ENSG00000068793. [Q7L576-2]
ENST00000560848; ENSP00000454199; ENSG00000068793. [Q7L576-1]
GeneID23191.
KEGGhsa:23191.
UCSCuc001yus.3. human. [Q7L576-1]
uc001yuu.3. human. [Q7L576-2]
uc001yuv.3. human. [Q7L576-3]

Organism-specific databases

CTD23191.
GeneCardsGC15P023873.
HGNCHGNC:13759. CYFIP1.
MIM606322. gene.
neXtProtNX_Q7L576.
Orphanet72. Angelman syndrome.
PharmGKBPA38367.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306641.
HOGENOMHOG000272573.
HOVERGENHBG053209.
InParanoidQ7L576.
KOK05749.
OMASSNIYKL.
OrthoDBEOG7ZSHS2.
PhylomeDBQ7L576.
TreeFamTF312925.

Gene expression databases

ArrayExpressQ7L576.
BgeeQ7L576.
CleanExHS_CYFIP1.
GenevestigatorQ7L576.

Family and domain databases

InterProIPR008081. Cytoplasmic_FMR1-int.
IPR016536. Cytoplasmic_FMR1-int_sub.
[Graphical view]
PANTHERPTHR12195. PTHR12195. 1 hit.
PfamPF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFPIRSF008153. FMR1_interacting. 1 hit.
PRINTSPR01698. CYTOFMRPINTP.
ProtoNetSearch...

Other

ChiTaRSCYFIP1. human.
EvolutionaryTraceQ7L576.
GeneWikiCYFIP1.
GenomeRNAi23191.
NextBio44673.
PROQ7L576.
SOURCESearch...

Entry information

Entry nameCYFP1_HUMAN
AccessionPrimary (citable) accession number: Q7L576
Secondary accession number(s): A8K6D9 expand/collapse secondary AC list , Q14467, Q5IED0, Q6ZSX1, Q9BSD9, Q9BVC7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM