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Q7L576

- CYFP1_HUMAN

UniProt

Q7L576 - CYFP1_HUMAN

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Protein
Cytoplasmic FMR1-interacting protein 1
Gene
CYFIP1, KIAA0068
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.4 Publications

GO - Molecular functioni

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

GO - Biological processi

  1. Rac protein signal transduction Source: UniProt
  2. axon extension Source: UniProtKB
  3. cognition Source: UniProt
  4. lamellipodium assembly Source: UniProtKB
  5. positive regulation of Arp2/3 complex-mediated actin nucleation 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:CYFIP1
Synonyms:KIAA0068
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.

GO - Cellular componenti

  1. SCAR complex Source: UniProt
  2. cell junction Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProt
  4. lamellipodium Source: UniProtKB
  5. mRNA cap binding complex Source: UniProtKB
  6. neuron projection Source: UniProtKB
  7. perinuclear region of cytoplasm Source: UniProtKB
  8. ruffle Source: UniProtKB
  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.

Organism-specific databases

Orphaneti72. Angelman syndrome.
PharmGKBiPA38367.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ7L576.
PaxDbiQ7L576.
PRIDEiQ7L576.

PTM databases

PhosphoSiteiQ7L576.

Expressioni

Gene expression databases

ArrayExpressiQ7L576.
BgeeiQ7L576.
CleanExiHS_CYFIP1.
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. 26 interactions.
DIPiDIP-38873N.
IntActiQ7L576. 24 interactions.
MINTiMINT-1731056.
STRINGi9606.ENSP00000324549.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P8CX-ray2.29A1-1253[»]
4N78X-ray2.43A1-1253[»]
ProteinModelPortaliQ7L576.

Miscellaneous databases

EvolutionaryTraceiQ7L576.

Family & Domainsi

Sequence similaritiesi

Belongs to the CYFIP family.

Phylogenomic databases

eggNOGiNOG306641.
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 11 Publication (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

MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN     50
AFVTGIARYI EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE 100
QPNRVEIYEK TVEVLEPEVT KLMNFMYFQR NAIERFCGEV RRLCHAERRK 150
DFVSEAYLIT LGKFINMFAV LDELKNMKCS VKNDHSAYKR AAQFLRKMAD 200
PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD IVNLCVDYYE 250
NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK 300
QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCTSSGSS PQYNICEQMI 350
QIREDHMRFI SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL 400
LSQWSAHVME VYSWKLVHPT DKYSNKDCPD SAEEYERATR YNYTSEEKFA 450
LVEVIAMIKG LQVLMGRMES VFNHAIRHTV YAALQDFSQV TLREPLRQAI 500
KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK SGFDIKVPRR 550
AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF 600
FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD 650
HILETKEASM MEYVLYSLDL YNDSAHYALT RFNKQFLYDE IEAEVNLCFD 700
QFVYKLADQI FAYYKVMAGS LLLDKRLRSE CKNQGATIHL PPSNRYETLL 750
KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL ELAIGRFESE DLTSIVELDG 800
LLEINRMTHK LLSRYLTLDG FDAMFREANH NVSAPYGRIT LHVFWELNYD 850
FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS 900
IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK 950
TLMEVMPKIC RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV 1000
GNAILFCLLI EQSLSLEEVC DLLHAAPFQN ILPRVHVKEG ERLDAKMKRL 1050
ESKYAPLHLV PLIERLGTPQ QIAIAREGDL LTKERLCCGL SMFEVILTRI 1100
RSFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI PVGTHEFTVE 1150
QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP 1200
LKKMVERIRK FQILNDEIIT ILDKYLKSGD GEGTPVEHVR CFQPPIHQSL 1250
ASS 1253
Length:1,253
Mass (Da):145,182
Last modified:July 5, 2004 - v1
Checksum:iD8F45E13207BEF16
GO
Isoform 21 Publication (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 31 Publication (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.

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 Publication
VSP_052345Add
BLAST
Alternative sequencei1 – 431431Missing in isoform 2. 1 Publication
VSP_052346Add
BLAST
Alternative sequencei432 – 557126AEEYE…GPSST → MAESLGSAELLRQLKSLGME RLLHAVNTFLRQSCTYLPLL TFGGKTSFVSLDVYGTEANC SATSCSFPKAAATWPRRQAP GPLGELVRGPPDQGVAEQSF SHGLFEFGITNVPCIFSPPQ MFPWII in isoform 2. 1 Publication
VSP_052347Add
BLAST

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS10009.1. [Q7L576-1]
CCDS45189.1. [Q7L576-2]
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

EnsembliENST00000313077; ENSP00000324549; ENSG00000068793. [Q7L576-1]
ENST00000435939; ENSP00000405956; ENSG00000068793. [Q7L576-2]
ENST00000560848; ENSP00000454199; ENSG00000068793. [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:
EMBL
GenBank
DDBJ
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 CCDS10009.1. [Q7L576-1 ]
CCDS45189.1. [Q7L576-2 ]
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:
PDBe
RCSB PDB
PDBj
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. 26 interactions.
DIPi DIP-38873N.
IntActi Q7L576. 24 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 ENST00000313077 ; ENSP00000324549 ; ENSG00000068793 . [Q7L576-1 ]
ENST00000435939 ; ENSP00000405956 ; ENSG00000068793 . [Q7L576-2 ]
ENST00000560848 ; ENSP00000454199 ; ENSG00000068793 . [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 GC15P023873.
HGNCi HGNC:13759. CYFIP1.
MIMi 606322. gene.
neXtProti NX_Q7L576.
Orphaneti 72. Angelman syndrome.
PharmGKBi PA38367.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306641.
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

ArrayExpressi Q7L576.
Bgeei Q7L576.
CleanExi HS_CYFIP1.
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 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.
    , 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. 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. 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: September 3, 2014
This is version 93 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

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