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Q7L576

- CYFP1_HUMAN

UniProt

Q7L576 - CYFP1_HUMAN

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Protein

Cytoplasmic FMR1-interacting protein 1

Gene

CYFIP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. actin filament binding Source: UniProtKB
  2. protein complex binding Source: UniProt
  3. Rac GTPase binding Source: UniProtKB

GO - Biological processi

  1. axon extension Source: UniProtKB
  2. cognition Source: UniProt
  3. lamellipodium assembly Source: UniProtKB
  4. positive regulation of Arp2/3 complex-mediated actin nucleation Source: UniProt
  5. Rac protein signal transduction Source: UniProt
  6. regulation of cell shape Source: UniProtKB-KW
  7. ruffle organization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell shape, Differentiation, Neurogenesis

Keywords - Ligandi

Actin-binding

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
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:13759. CYFIP1.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. focal adhesion Source: UniProtKB
  3. lamellipodium Source: UniProtKB
  4. mRNA cap binding complex Source: UniProtKB
  5. neuron projection Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB
  7. ruffle Source: UniProtKB
  8. SCAR complex Source: UniProt
  9. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi179 – 1791C → R: Reduced interaction with RAC1. 1 Publication
Mutagenesisi190 – 1901R → D: Reduced interaction with RAC1. 1 Publication
Mutagenesisi434 – 4341E → K: Reduced interaction with RAC1; when associated with A-626. 1 Publication
Mutagenesisi626 – 6261F → A: Reduced interaction with RAC1; when associated with K-434. 1 Publication
Mutagenesisi632 – 6321M → D: Reduced interaction with RAC1. 1 Publication
Mutagenesisi697 – 6971L → D: Constitutive induction of the formation of actin filaments; when associated with D-704. 1 Publication
Mutagenesisi704 – 7041Y → D: Constitutive induction of the formation of actin filaments; when associated with D-697. 1 Publication
Mutagenesisi841 – 8411L → A: Constitutive induction of the formation of actin filaments; when associated with 844-A-A-845. 1 Publication
Mutagenesisi844 – 8452FW → AA: Constitutive induction of the formation of actin filaments; when associated with A-841. 1 Publication

Organism-specific databases

Orphaneti72. Angelman syndrome.
PharmGKBiPA38367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12531253Cytoplasmic FMR1-interacting protein 1PRO_0000279706Add
BLAST

Proteomic databases

MaxQBiQ7L576.
PaxDbiQ7L576.
PRIDEiQ7L576.

PTM databases

PhosphoSiteiQ7L576.

Expressioni

Gene expression databases

BgeeiQ7L576.
CleanExiHS_CYFIP1.
ExpressionAtlasiQ7L576. differential.
GenevestigatoriQ7L576.

Interactioni

Subunit structurei

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 MYO16.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi116800. 35 interactions.
DIPiDIP-38873N.
IntActiQ7L576. 28 interactions.
MINTiMINT-1731056.
STRINGi9606.ENSP00000324549.

Structurei

Secondary structure

1
1253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 1711Combined sources
Helixi59 – 8426Combined sources
Helixi90 – 923Combined sources
Helixi104 – 14340Combined sources
Helixi148 – 1503Combined sources
Helixi155 – 17723Combined sources
Helixi179 – 19315Combined sources
Turni194 – 1963Combined sources
Helixi201 – 21515Combined sources
Helixi219 – 22911Combined sources
Helixi234 – 25017Combined sources
Helixi257 – 27418Combined sources
Beta strandi275 – 2784Combined sources
Helixi281 – 2866Combined sources
Helixi292 – 30110Combined sources
Beta strandi304 – 3085Combined sources
Beta strandi311 – 3144Combined sources
Helixi316 – 3205Combined sources
Turni323 – 3253Combined sources
Helixi326 – 3316Combined sources
Helixi346 – 36520Combined sources
Helixi384 – 41734Combined sources
Turni422 – 4243Combined sources
Helixi434 – 4385Combined sources
Helixi440 – 4423Combined sources
Helixi445 – 46723Combined sources
Helixi469 – 48921Combined sources
Turni490 – 4923Combined sources
Helixi493 – 5019Combined sources
Helixi505 – 51814Combined sources
Beta strandi522 – 5254Combined sources
Helixi531 – 5344Combined sources
Helixi556 – 57015Combined sources
Turni580 – 5834Combined sources
Helixi586 – 59813Combined sources
Helixi599 – 6013Combined sources
Helixi602 – 6065Combined sources
Helixi608 – 6158Combined sources
Helixi619 – 6213Combined sources
Helixi625 – 6306Combined sources
Turni631 – 6333Combined sources
Helixi640 – 6423Combined sources
Helixi644 – 65512Combined sources
Helixi658 – 6603Combined sources
Turni661 – 6633Combined sources
Helixi664 – 6685Combined sources
Helixi670 – 68011Combined sources
Helixi685 – 72137Combined sources
Helixi725 – 7339Combined sources
Helixi747 – 7504Combined sources
Beta strandi755 – 7573Combined sources
Beta strandi760 – 7623Combined sources
Helixi764 – 78825Combined sources
Helixi792 – 7943Combined sources
Helixi795 – 81319Combined sources
Helixi821 – 8288Combined sources
Beta strandi832 – 8365Combined sources
Helixi838 – 84912Combined sources
Helixi851 – 8544Combined sources
Beta strandi855 – 8584Combined sources
Turni859 – 8624Combined sources
Beta strandi863 – 8664Combined sources
Helixi869 – 8713Combined sources
Helixi885 – 8873Combined sources
Helixi892 – 90110Combined sources
Helixi902 – 9065Combined sources
Helixi911 – 94232Combined sources
Helixi944 – 95512Combined sources
Helixi965 – 9673Combined sources
Helixi969 – 97911Combined sources
Helixi981 – 9844Combined sources
Turni987 – 9926Combined sources
Helixi993 – 102533Combined sources
Helixi1026 – 10294Combined sources
Helixi1043 – 105311Combined sources
Helixi1055 – 10573Combined sources
Helixi1059 – 10668Combined sources
Helixi1069 – 108315Combined sources
Helixi1086 – 10883Combined sources
Beta strandi1090 – 10923Combined sources
Helixi1093 – 11019Combined sources
Turni1107 – 11104Combined sources
Beta strandi1121 – 11233Combined sources
Helixi1127 – 113913Combined sources
Helixi1149 – 11535Combined sources
Helixi1156 – 116712Combined sources
Helixi1171 – 11777Combined sources
Helixi1179 – 119012Combined sources
Helixi1201 – 122525Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7L576.

Family & Domainsi

Sequence similaritiesi

Belongs to the CYFIP family.Sequence Analysis

Phylogenomic databases

eggNOGiNOG306641.
GeneTreeiENSGT00500000044831.
HOGENOMiHOG000272573.
HOVERGENiHBG053209.
InParanoidiQ7L576.
KOiK05749.
OMAiSSNIYKL.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ7L576.
TreeFamiTF312925.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR016536. Cytoplasmic_FMR1-int_sub.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 1 hit.
PfamiPF05994. 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. Align

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti583 – 5831S → N in AAW51478. 1 PublicationCurated
Sequence conflicti583 – 5831S → N in BAC86825. (PubMed:14702039)Curated
Sequence conflicti898 – 8981Y → H in AAW51478. 1 PublicationCurated
Sequence conflicti898 – 8981Y → H in BAC86825. (PubMed:14702039)Curated
Sequence conflicti930 – 9301M → R in AAW51478. 1 PublicationCurated
Sequence conflicti930 – 9301M → R in BAC86825. (PubMed:14702039)Curated
Sequence conflicti1176 – 11761V → A in AAW51479. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti532 – 5321A → P.
Corresponds to variant rs34683919 [ dbSNP | Ensembl ].
VAR_053849
Natural varianti820 – 8201G → D.
Corresponds to variant rs17137190 [ dbSNP | Ensembl ].
VAR_053850
Natural varianti820 – 8201G → S.2 Publications
Corresponds to variant rs7170637 [ dbSNP | Ensembl ].
VAR_053851

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 806806Missing in isoform 3. 1 PublicationVSP_052345Add
BLAST
Alternative sequencei1 – 431431Missing in isoform 2. 2 PublicationsVSP_052346Add
BLAST
Alternative sequencei432 – 557126AEEYE…GPSST → MAESLGSAELLRQLKSLGME RLLHAVNTFLRQSCTYLPLL TFGGKTSFVSLDVYGTEANC SATSCSFPKAAATWPRRQAP GPLGELVRGPPDQGVAEQSF SHGLFEFGITNVPCIFSPPQ MFPWII in isoform 2. 2 PublicationsVSP_052347Add
BLAST

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_001287810.1. [Q7L576-1]
NP_055423.1. NM_014608.3. [Q7L576-1]
XP_005272600.1. XM_005272543.1. [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.3. human. [Q7L576-1]
uc001yuu.3. human. [Q7L576-2]
uc001yuv.3. human. [Q7L576-3]

Polymorphism databases

DMDMi74738589.

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 .
CCDSi CCDS73695.1. [Q7L576-2 ]
CCDS73696.1. [Q7L576-1 ]
RefSeqi NP_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 ]
UniGenei Hs.26704.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P8C X-ray 2.29 A 1-1253 [» ]
4N78 X-ray 2.43 A 1-1253 [» ]
ProteinModelPortali Q7L576.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116800. 35 interactions.
DIPi DIP-38873N.
IntActi Q7L576. 28 interactions.
MINTi MINT-1731056.
STRINGi 9606.ENSP00000324549.

PTM databases

PhosphoSitei Q7L576.

Polymorphism databases

DMDMi 74738589.

Proteomic databases

MaxQBi Q7L576.
PaxDbi Q7L576.
PRIDEi Q7L576.

Protocols and materials databases

DNASUi 23191.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000610365 ; ENSP00000478779 ; ENSG00000273749 . [Q7L576-1 ]
ENST00000617556 ; ENSP00000480525 ; ENSG00000273749 . [Q7L576-2 ]
ENST00000617928 ; ENSP00000481038 ; ENSG00000273749 . [Q7L576-1 ]
GeneIDi 23191.
KEGGi hsa:23191.
UCSCi uc001yus.3. human. [Q7L576-1 ]
uc001yuu.3. human. [Q7L576-2 ]
uc001yuv.3. human. [Q7L576-3 ]

Organism-specific databases

CTDi 23191.
GeneCardsi GC15P023905.
HGNCi HGNC:13759. CYFIP1.
MIMi 606322. gene.
neXtProti NX_Q7L576.
Orphaneti 72. Angelman syndrome.
PharmGKBi PA38367.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306641.
GeneTreei ENSGT00500000044831.
HOGENOMi HOG000272573.
HOVERGENi HBG053209.
InParanoidi Q7L576.
KOi K05749.
OMAi SSNIYKL.
OrthoDBi EOG7ZSHS2.
PhylomeDBi Q7L576.
TreeFami TF312925.

Miscellaneous databases

ChiTaRSi CYFIP1. human.
EvolutionaryTracei Q7L576.
GeneWikii CYFIP1.
GenomeRNAii 23191.
NextBioi 44673.
PROi Q7L576.
SOURCEi Search...

Gene expression databases

Bgeei Q7L576.
CleanExi HS_CYFIP1.
ExpressionAtlasi Q7L576. differential.
Genevestigatori Q7L576.

Family and domain databases

InterProi IPR008081. Cytoplasmic_FMR1-int.
IPR016536. Cytoplasmic_FMR1-int_sub.
[Graphical view ]
PANTHERi PTHR12195. PTHR12195. 1 hit.
Pfami PF05994. FragX_IP. 1 hit.
[Graphical view ]
PIRSFi PIRSF008153. FMR1_interacting. 1 hit.
PRINTSi PR01698. CYTOFMRPINTP.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 marrow1 Publication.
  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] (ISOFORMS 1 AND 2), VARIANT SER-820.
    Tissue: BrainImported and Placenta.
  4. 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: BrainImported and PlacentaImported.
  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. Cited for: FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. 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.

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 26, 2014
This is version 96 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

External Data

Dasty 3