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Protein

Cytoplasmic FMR1-interacting protein 1

Gene

CYFIP1

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

Functioni

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.By similarity4 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB

GO - Biological processi

  • axon extension Source: UniProtKB
  • cognition Source: UniProtKB
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • lamellipodium assembly Source: UniProtKB
  • positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKB
  • Rac protein signal transduction Source: UniProtKB
  • regulation of cell shape Source: UniProtKB-KW
  • ruffle organization Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell shape, Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic FMR1-interacting protein 1
Alternative name(s):
Specifically Rac1-associated protein 1
Short name:
Sra-1
p140sra-1
Gene namesi
Name:CYFIP1Imported
Synonyms:KIAA0068Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:13759. CYFIP1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmperinuclear region By similarity
  • Cell projectionlamellipodium By similarity
  • Cell projectionruffle By similarity
  • Cell junctionsynapsesynaptosome By similarity

  • Note: Highly expressed in the perinuclear region (By similarity). Enriched in synaptosomes (By similarity). Also enriched in membrane ruffles and at the tips of lamellipodia (By similarity).By similarity

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • mRNA cap binding complex Source: UniProtKB
  • neuron projection Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • ruffle Source: UniProtKB
  • SCAR complex Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi179C → R: Reduced interaction with RAC1. 1 Publication1
Mutagenesisi190R → D: Reduced interaction with RAC1. 1 Publication1
Mutagenesisi434E → K: Reduced interaction with RAC1; when associated with A-626. 1 Publication1
Mutagenesisi626F → A: Reduced interaction with RAC1; when associated with K-434. 1 Publication1
Mutagenesisi632M → D: Reduced interaction with RAC1. 1 Publication1
Mutagenesisi697L → D: Constitutive induction of the formation of actin filaments; when associated with D-704. 1 Publication1
Mutagenesisi704Y → D: Constitutive induction of the formation of actin filaments; when associated with D-697. 1 Publication1
Mutagenesisi841L → A: Constitutive induction of the formation of actin filaments; when associated with 844-A-A-845. 1 Publication1
Mutagenesisi844 – 845FW → AA: Constitutive induction of the formation of actin filaments; when associated with A-841. 1 Publication2

Organism-specific databases

DisGeNETi23191.
MalaCardsiCYFIP1.
OpenTargetsiENSG00000273749.
Orphaneti72. Angelman syndrome.
PharmGKBiPA38367.

Polymorphism and mutation databases

BioMutaiCYFIP1.
DMDMi74738589.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002797061 – 1253Cytoplasmic FMR1-interacting protein 1Add BLAST1253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei583PhosphoserineCombined sources1
Modified residuei1234PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7L576.
MaxQBiQ7L576.
PaxDbiQ7L576.
PeptideAtlasiQ7L576.
PRIDEiQ7L576.

PTM databases

iPTMnetiQ7L576.
PhosphoSitePlusiQ7L576.
SwissPalmiQ7L576.

Expressioni

Gene expression databases

BgeeiENSG00000068793.
CleanExiHS_CYFIP1.
ExpressionAtlasiQ7L576. baseline and differential.
GenevisibleiQ7L576. HS.

Organism-specific databases

HPAiHPA068106.

Interactioni

Subunit structurei

Component of the WAVE1 complex composed of ABI2, CYFIP1 or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer 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 MYO16.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eif4eP630732EBI-1048143,EBI-2000006From a different organism.
FMR1Q067874EBI-1048143,EBI-366305
NCKAP1Q9Y2A73EBI-1048143,EBI-389845

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • protein complex binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116800. 61 interactors.
DIPiDIP-38873N.
IntActiQ7L576. 41 interactors.
MINTiMINT-1731056.
STRINGi9606.ENSP00000324549.

Structurei

Secondary structure

11253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 17Combined sources11
Helixi59 – 84Combined sources26
Helixi90 – 92Combined sources3
Helixi104 – 143Combined sources40
Helixi148 – 150Combined sources3
Helixi155 – 177Combined sources23
Helixi179 – 193Combined sources15
Turni194 – 196Combined sources3
Helixi201 – 215Combined sources15
Helixi219 – 229Combined sources11
Helixi234 – 250Combined sources17
Helixi257 – 274Combined sources18
Beta strandi275 – 278Combined sources4
Helixi281 – 286Combined sources6
Helixi292 – 301Combined sources10
Beta strandi304 – 308Combined sources5
Beta strandi311 – 314Combined sources4
Helixi316 – 320Combined sources5
Turni323 – 325Combined sources3
Helixi326 – 331Combined sources6
Helixi346 – 365Combined sources20
Helixi384 – 417Combined sources34
Turni422 – 424Combined sources3
Helixi434 – 438Combined sources5
Helixi440 – 442Combined sources3
Helixi445 – 467Combined sources23
Helixi469 – 489Combined sources21
Turni490 – 492Combined sources3
Helixi493 – 501Combined sources9
Helixi505 – 518Combined sources14
Beta strandi522 – 525Combined sources4
Helixi531 – 534Combined sources4
Helixi556 – 570Combined sources15
Turni580 – 583Combined sources4
Helixi586 – 598Combined sources13
Helixi599 – 601Combined sources3
Helixi602 – 606Combined sources5
Helixi608 – 615Combined sources8
Helixi619 – 621Combined sources3
Helixi625 – 630Combined sources6
Turni631 – 633Combined sources3
Helixi640 – 642Combined sources3
Helixi644 – 655Combined sources12
Helixi658 – 660Combined sources3
Turni661 – 663Combined sources3
Helixi664 – 668Combined sources5
Helixi670 – 680Combined sources11
Helixi685 – 721Combined sources37
Helixi725 – 733Combined sources9
Helixi747 – 750Combined sources4
Beta strandi755 – 757Combined sources3
Beta strandi760 – 762Combined sources3
Helixi764 – 788Combined sources25
Helixi792 – 794Combined sources3
Helixi795 – 813Combined sources19
Helixi821 – 828Combined sources8
Beta strandi832 – 836Combined sources5
Helixi838 – 849Combined sources12
Helixi851 – 854Combined sources4
Beta strandi855 – 858Combined sources4
Turni859 – 862Combined sources4
Beta strandi863 – 866Combined sources4
Helixi869 – 871Combined sources3
Helixi885 – 887Combined sources3
Helixi892 – 901Combined sources10
Helixi902 – 906Combined sources5
Helixi911 – 942Combined sources32
Helixi944 – 955Combined sources12
Helixi965 – 967Combined sources3
Helixi969 – 979Combined sources11
Helixi981 – 984Combined sources4
Turni987 – 992Combined sources6
Helixi993 – 1025Combined sources33
Helixi1026 – 1029Combined sources4
Helixi1043 – 1053Combined sources11
Helixi1055 – 1057Combined sources3
Helixi1059 – 1066Combined sources8
Helixi1069 – 1083Combined sources15
Helixi1086 – 1088Combined sources3
Beta strandi1090 – 1092Combined sources3
Helixi1093 – 1101Combined sources9
Turni1107 – 1110Combined sources4
Beta strandi1121 – 1123Combined sources3
Helixi1127 – 1139Combined sources13
Helixi1149 – 1153Combined sources5
Helixi1156 – 1167Combined sources12
Helixi1171 – 1177Combined sources7
Helixi1179 – 1190Combined sources12
Helixi1201 – 1225Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29A1-1253[»]
4N78X-ray2.43A1-1253[»]
ProteinModelPortaliQ7L576.
SMRiQ7L576.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7L576.

Family & Domainsi

Sequence similaritiesi

Belongs to the CYFIP family.Sequence analysis

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
HOGENOMiHOG000272573.
HOVERGENiHBG053209.
InParanoidiQ7L576.
KOiK05749.
OMAiMESVFSH.
OrthoDBiEOG091G0105.
PhylomeDBiQ7L576.
TreeFamiTF312925.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR009828. DUF1394.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 1 hit.
PfamiPF07159. DUF1394. 1 hit.
PF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
PRINTSiPR01698. CYTOFMRPINTP.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7L576-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN
60 70 80 90 100
AFVTGIARYI EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE
110 120 130 140 150
QPNRVEIYEK TVEVLEPEVT KLMNFMYFQR NAIERFCGEV RRLCHAERRK
160 170 180 190 200
DFVSEAYLIT LGKFINMFAV LDELKNMKCS VKNDHSAYKR AAQFLRKMAD
210 220 230 240 250
PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD IVNLCVDYYE
260 270 280 290 300
NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK
310 320 330 340 350
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCTSSGSS PQYNICEQMI
360 370 380 390 400
QIREDHMRFI SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL
410 420 430 440 450
LSQWSAHVME VYSWKLVHPT DKYSNKDCPD SAEEYERATR YNYTSEEKFA
460 470 480 490 500
LVEVIAMIKG LQVLMGRMES VFNHAIRHTV YAALQDFSQV TLREPLRQAI
510 520 530 540 550
KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK SGFDIKVPRR
560 570 580 590 600
AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
610 620 630 640 650
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD
660 670 680 690 700
HILETKEASM MEYVLYSLDL YNDSAHYALT RFNKQFLYDE IEAEVNLCFD
710 720 730 740 750
QFVYKLADQI FAYYKVMAGS LLLDKRLRSE CKNQGATIHL PPSNRYETLL
760 770 780 790 800
KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL ELAIGRFESE DLTSIVELDG
810 820 830 840 850
LLEINRMTHK LLSRYLTLDG FDAMFREANH NVSAPYGRIT LHVFWELNYD
860 870 880 890 900
FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS
910 920 930 940 950
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK
960 970 980 990 1000
TLMEVMPKIC RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV
1010 1020 1030 1040 1050
GNAILFCLLI EQSLSLEEVC DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL
1060 1070 1080 1090 1100
ESKYAPLHLV PLIERLGTPQ QIAIAREGDL LTKERLCCGL SMFEVILTRI
1110 1120 1130 1140 1150
RSFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI PVGTHEFTVE
1160 1170 1180 1190 1200
QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP
1210 1220 1230 1240 1250
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GEGTPVEHVR CFQPPIHQSL

ASS
Length:1,253
Mass (Da):145,182
Last modified:July 5, 2004 - v1
Checksum:iD8F45E13207BEF16
GO
Isoform 2 (identifier: Q7L576-2) [UniParc]FASTAAdd to basket
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

Show »
Length:822
Mass (Da):94,467
Checksum:i035E45763DC5F6C4
GO
Isoform 3 (identifier: Q7L576-3) [UniParc]FASTAAdd to basket
Also known as: 5

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

Show »
Length:447
Mass (Da):51,534
Checksum:i1D9F2A088E5891A2
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti583S → N in AAW51478 (Ref. 1) Curated1
Sequence conflicti583S → N in BAC86825 (PubMed:14702039).Curated1
Sequence conflicti898Y → H in AAW51478 (Ref. 1) Curated1
Sequence conflicti898Y → H in BAC86825 (PubMed:14702039).Curated1
Sequence conflicti930M → R in AAW51478 (Ref. 1) Curated1
Sequence conflicti930M → R in BAC86825 (PubMed:14702039).Curated1
Sequence conflicti1176V → A in AAW51479 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_053849532A → P.Corresponds to variant rs34683919dbSNPEnsembl.1
Natural variantiVAR_053850820G → D.Corresponds to variant rs17137190dbSNPEnsembl.1
Natural variantiVAR_053851820G → S.2 PublicationsCorresponds to variant rs7170637dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0523451 – 806Missing in isoform 3. 1 PublicationAdd BLAST806
Alternative sequenceiVSP_0523461 – 431Missing in isoform 2. 2 PublicationsAdd BLAST431
Alternative sequenceiVSP_052347432 – 557AEEYE…GPSST → MAESLGSAELLRQLKSLGME RLLHAVNTFLRQSCTYLPLL TFGGKTSFVSLDVYGTEANC SATSCSFPKAAATWPRRQAP GPLGELVRGPPDQGVAEQSF SHGLFEFGITNVPCIFSPPQ MFPWII in isoform 2. 2 PublicationsAdd BLAST126

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS73695.1. [Q7L576-2]
CCDS73696.1. [Q7L576-1]
RefSeqiNP_001028200.1. NM_001033028.1. [Q7L576-2]
NP_001274739.1. NM_001287810.2. [Q7L576-1]
NP_001311049.1. NM_001324120.1. [Q7L576-1]
NP_001311052.1. NM_001324123.1. [Q7L576-1]
NP_055423.1. NM_014608.4. [Q7L576-1]
UniGeneiHs.26704.

Genome annotation databases

EnsembliENST00000610365; ENSP00000478779; ENSG00000273749. [Q7L576-1]
ENST00000617556; ENSP00000480525; ENSG00000273749. [Q7L576-2]
ENST00000617928; ENSP00000481038; ENSG00000273749. [Q7L576-1]
GeneIDi23191.
KEGGihsa:23191.
UCSCiuc001yus.5. human. [Q7L576-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS73695.1. [Q7L576-2]
CCDS73696.1. [Q7L576-1]
RefSeqiNP_001028200.1. NM_001033028.1. [Q7L576-2]
NP_001274739.1. NM_001287810.2. [Q7L576-1]
NP_001311049.1. NM_001324120.1. [Q7L576-1]
NP_001311052.1. NM_001324123.1. [Q7L576-1]
NP_055423.1. NM_014608.4. [Q7L576-1]
UniGeneiHs.26704.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29A1-1253[»]
4N78X-ray2.43A1-1253[»]
ProteinModelPortaliQ7L576.
SMRiQ7L576.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116800. 61 interactors.
DIPiDIP-38873N.
IntActiQ7L576. 41 interactors.
MINTiMINT-1731056.
STRINGi9606.ENSP00000324549.

PTM databases

iPTMnetiQ7L576.
PhosphoSitePlusiQ7L576.
SwissPalmiQ7L576.

Polymorphism and mutation databases

BioMutaiCYFIP1.
DMDMi74738589.

Proteomic databases

EPDiQ7L576.
MaxQBiQ7L576.
PaxDbiQ7L576.
PeptideAtlasiQ7L576.
PRIDEiQ7L576.

Protocols and materials databases

DNASUi23191.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000610365; ENSP00000478779; ENSG00000273749. [Q7L576-1]
ENST00000617556; ENSP00000480525; ENSG00000273749. [Q7L576-2]
ENST00000617928; ENSP00000481038; ENSG00000273749. [Q7L576-1]
GeneIDi23191.
KEGGihsa:23191.
UCSCiuc001yus.5. human. [Q7L576-1]

Organism-specific databases

CTDi23191.
DisGeNETi23191.
GeneCardsiCYFIP1.
HGNCiHGNC:13759. CYFIP1.
HPAiHPA068106.
MalaCardsiCYFIP1.
MIMi606322. gene.
neXtProtiNX_Q7L576.
OpenTargetsiENSG00000273749.
Orphaneti72. Angelman syndrome.
PharmGKBiPA38367.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
HOGENOMiHOG000272573.
HOVERGENiHBG053209.
InParanoidiQ7L576.
KOiK05749.
OMAiMESVFSH.
OrthoDBiEOG091G0105.
PhylomeDBiQ7L576.
TreeFamiTF312925.

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiCYFIP1. human.
EvolutionaryTraceiQ7L576.
GeneWikiiCYFIP1.
GenomeRNAii23191.
PROiQ7L576.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000068793.
CleanExiHS_CYFIP1.
ExpressionAtlasiQ7L576. baseline and differential.
GenevisibleiQ7L576. HS.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR009828. DUF1394.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 1 hit.
PfamiPF07159. DUF1394. 1 hit.
PF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
PRINTSiPR01698. CYTOFMRPINTP.
ProtoNetiSearch...

Entry informationi

Entry nameiCYFP1_HUMAN
AccessioniPrimary (citable) accession number: Q7L576
Secondary accession number(s): A8K6D9
, Q14467, Q5IED0, Q6ZSX1, Q9BSD9, Q9BVC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 118 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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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

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.