Q7L576 (CYFP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1253 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.14
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. Ref.8 Ref.14
Subcellular location	Cytoplasm › perinuclear region By similarity. Cell projection › lamellipodium By similarity. Cell projection › ruffle By similarity. Cell junction › synapse › synaptosome 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 process	Cell shape Differentiation Neurogenesis
Cellular component	Cell junction Cell projection Cytoplasm Synapse Synaptosome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Actin-binding
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	axon extension Inferred from mutant phenotype Ref.8. Source: UniProtKB lamellipodium assembly Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW ruffle organization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB mRNA cap binding complex 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 synaptosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	Rac GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB actin filament binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Eif4e	P63073	2	EBI-1048143,EBI-2000006	From a different organism.
FMR1	Q06787	4	EBI-1048143,EBI-366305
NCKAP1	Q9Y2A7	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1253

1253

Cytoplasmic FMR1-interacting protein 1

PRO_0000279706

Amino acid modifications

Modified residue

108

1

Phosphotyrosine Ref.9

Modified residue

1068

1

Phosphothreonine Ref.10

Modified residue

1197

1

N6-acetyllysine Ref.12

Natural variations

Alternative sequence

1 – 806

806

Missing in isoform 3. Ref.8

VSP_052345

Alternative sequence

1 – 431

431

Missing in isoform 2. Ref.8

VSP_052346

Alternative sequence

432 – 557

126

AEEYE…GPSST → MAESLGSAELLRQLKSLGME RLLHAVNTFLRQSCTYLPLL TFGGKTSFVSLDVYGTEANC SATSCSFPKAAATWPRRQAP GPLGELVRGPPDQGVAEQSF SHGLFEFGITNVPCIFSPPQ MFPWII in isoform 2. Ref.8

VSP_052347

Natural variant

532

1

A → P.
Corresponds to variant rs34683919 [ dbSNP | Ensembl ].

VAR_053849

Natural variant

820

1

G → D.
Corresponds to variant rs17137190 [ dbSNP | Ensembl ].

VAR_053850

Natural variant

820

1

G → S. Ref.1 Ref.3
Corresponds to variant rs7170637 [ dbSNP | Ensembl ].

VAR_053851

Experimental info

Mutagenesis

179

1

C → R: Reduced interaction with RAC1. Ref.14

Mutagenesis

190

1

R → D: Reduced interaction with RAC1. Ref.14

Mutagenesis

434

1

E → K: Reduced interaction with RAC1; when associated with A-626. Ref.14

Mutagenesis

626

1

F → A: Reduced interaction with RAC1; when associated with K-434. Ref.14

Mutagenesis

632

1

M → D: Reduced interaction with RAC1. Ref.14

Mutagenesis

697

1

L → D: Constitutive induction of the formation of actin filaments; when associated with D-704. Ref.14

Mutagenesis

704

1

Y → D: Constitutive induction of the formation of actin filaments; when associated with D-697. Ref.14

Mutagenesis

841

1

L → A: Constitutive induction of the formation of actin filaments; when associated with 844-A-A-845. Ref.14

Mutagenesis

844 – 845

2

FW → AA: Constitutive induction of the formation of actin filaments; when associated with A-841.

Sequence conflict

583

1

S → N in AAW51478. Ref.1

Sequence conflict

583

1

S → N in BAC86825. Ref.3

Sequence conflict

898

1

Y → H in AAW51478. Ref.1

Sequence conflict

898

1

Y → H in BAC86825. Ref.3

Sequence conflict

930

1

M → R in AAW51478. Ref.1

Sequence conflict

930

1

M → R in BAC86825. Ref.3

Sequence conflict

1176

1

V → A in AAW51479. Ref.1

Secondary structure

1

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1253

Helix Strand Turn

Details...

Helix

7 – 17

11

Helix

59 – 74

16

Helix

78 – 84

7

Helix

90 – 92

3

Helix

104 – 136

33

Helix

140 – 143

4

Helix

148 – 150

3

Helix

155 – 160

6

Helix

164 – 177

14

Helix

179 – 193

15

Turn

194 – 196

3

Helix

201 – 215

15

Helix

219 – 229

11

Helix

235 – 250

16

Helix

257 – 266

10

Turn

272 – 274

3

Helix

281 – 286

6

Helix

292 – 301

10

Beta strand

304 – 306

3

Beta strand

312 – 314

3

Helix

316 – 320

5

Turn

323 – 325

3

Helix

326 – 331

6

Helix

346 – 365

20

Helix

384 – 396

13

Helix

399 – 417

19

Turn

422 – 424

3

Helix

434 – 438

5

Helix

440 – 442

3

Helix

445 – 458

14

Turn

462 – 464

3

Helix

469 – 489

21

Turn

490 – 492

3

Helix

493 – 501

9

Helix

505 – 518

14

Turn

531 – 533

3

Helix

556 – 570

15

Turn

580 – 583

4

Helix

588 – 598

11

Helix

599 – 601

3

Helix

602 – 606

5

Helix

608 – 615

8

Helix

619 – 621

3

Helix

625 – 630

6

Helix

640 – 642

3

Helix

644 – 655

12

Helix

658 – 660

3

Turn

661 – 663

3

Helix

664 – 668

5

Helix

670 – 680

11

Helix

685 – 717

33

Helix

725 – 733

9

Helix

747 – 750

4

Helix

764 – 783

20

Helix

787 – 789

3

Helix

792 – 794

3

Helix

795 – 798

4

Helix

802 – 813

12

Helix

822 – 828

7

Beta strand

832 – 834

3

Helix

839 – 849

11

Helix

851 – 854

4

Beta strand

855 – 858

4

Beta strand

863 – 866

4

Helix

869 – 871

3

Helix

885 – 887

3

Helix

892 – 901

10

Helix

912 – 920

9

Helix

927 – 941

15

Helix

945 – 955

11

Helix

973 – 979

7

Helix

981 – 984

4

Turn

987 – 992

6

Helix

993 – 999

7

Helix

1003 – 1025

23

Helix

1026 – 1029

4

Helix

1043 – 1053

11

Helix

1055 – 1057

3

Helix

1059 – 1065

7

Helix

1069 – 1076

8

Helix

1080 – 1083

4

Helix

1093 – 1101

9

Beta strand

1121 – 1123

3

Helix

1127 – 1139

13

Helix

1149 – 1152

4

Helix

1163 – 1167

5

Helix

1171 – 1177

7

Helix

1179 – 1189

11

Helix

1201 – 1225

25

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (3) [UniParc]. Last modified July 5, 2004. Version 1. Checksum: D8F45E13207BEF16	FASTA	1,253	145,182
	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
	Isoform 2 (4) [UniParc]. Checksum: 035E45763DC5F6C4	FASTA	822	94,467
	10 20 30 40 50 60 MAESLGSAEL LRQLKSLGME RLLHAVNTFL RQSCTYLPLL TFGGKTSFVS LDVYGTEANC 70 80 90 100 110 120 SATSCSFPKA AATWPRRQAP GPLGELVRGP PDQGVAEQSF SHGLFEFGIT NVPCIFSPPQ 130 140 150 160 170 180 MFPWIIQLYM VRTMLESLIA DKSGSKKTLR SSLEGPTILD IEKFHRESFF YTHLINFSET 190 200 210 220 230 240 LQQCCDLSQL WFREFFLELT MGRRIQFPIE MSMPWILTDH ILETKEASMM EYVLYSLDLY 250 260 270 280 290 300 NDSAHYALTR FNKQFLYDEI EAEVNLCFDQ FVYKLADQIF AYYKVMAGSL LLDKRLRSEC 310 320 330 340 350 360 KNQGATIHLP PSNRYETLLK QRHVQLLGRS IDLNRLITQR VSAAMYKSLE LAIGRFESED 370 380 390 400 410 420 LTSIVELDGL LEINRMTHKL LSRYLTLDGF DAMFREANHN VSAPYGRITL HVFWELNYDF 430 440 450 460 470 480 LPNYCYNGST NRFVRTVLPF SQEFQRDKQP NAQPQYLHGS KALNLAYSSI YGSYRNFVGP 490 500 510 520 530 540 PHFQVICRLL GYQGIAVVME ELLKVVKSLL QGTILQYVKT LMEVMPKICR LPRHEYGSPG 550 560 570 580 590 600 ILEFFHHQLK DIVEYAELKT VCFQNLREVG NAILFCLLIE QSLSLEEVCD LLHAAPFQNI 610 620 630 640 650 660 LPRVHVKEGE RLDAKMKRLE SKYAPLHLVP LIERLGTPQQ IAIAREGDLL TKERLCCGLS 670 680 690 700 710 720 MFEVILTRIR SFLDDPIWRG PLPSNGVMHV DECVEFHRLW SAMQFVYCIP VGTHEFTVEQ 730 740 750 760 770 780 CFGDGLHWAG CMIIVLLGQQ RRFAVLDFCY HLLKVQKHDG KDEIIKNVPL KKMVERIRKF 790 800 810 820 QILNDEIITI LDKYLKSGDG EGTPVEHVRC FQPPIHQSLA SS
	Isoform 3 (5) [UniParc]. Checksum: 1D9F2A088E5891A2	FASTA	447	51,534
	10 20 30 40 50 60 MTHKLLSRYL TLDGFDAMFR EANHNVSAPY GRITLHVFWE LNYDFLPNYC YNGSTNRFVR 70 80 90 100 110 120 TVLPFSQEFQ RDKQPNAQPQ YLHGSKALNL AYSSIYGSYR NFVGPPHFQV ICRLLGYQGI 130 140 150 160 170 180 AVVMEELLKV VKSLLQGTIL QYVKTLMEVM PKICRLPRHE YGSPGILEFF HHQLKDIVEY 190 200 210 220 230 240 AELKTVCFQN LREVGNAILF CLLIEQSLSL EEVCDLLHAA PFQNILPRVH VKEGERLDAK 250 260 270 280 290 300 MKRLESKYAP LHLVPLIERL GTPQQIAIAR EGDLLTKERL CCGLSMFEVI LTRIRSFLDD 310 320 330 340 350 360 PIWRGPLPSN GVMHVDECVE FHRLWSAMQF VYCIPVGTHE FTVEQCFGDG LHWAGCMIIV 370 380 390 400 410 420 LLGQQRRFAV LDFCYHLLKV QKHDGKDEII KNVPLKKMVE RIRKFQILND EIITILDKYL 430 440 KSGDGEGTPV EHVRCFQPPI HQSLASS

References

	« Hide 'large scale' referencesShow '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: 7584044] [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: 14702039] [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. , 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: 15489334] [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, 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: 9417078] [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: 16260607] [Abstract] Cited for: FUNCTION, INTERACTION WITH DPYSL2.
[9]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1068, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19524508] [Abstract] Cited for: FUNCTION.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1197, MASS SPECTROMETRY.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"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: 21107423] [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.

IPI

IPI00550212.
IPI00644231.
IPI00790673.

RefSeq

NP_001028200.1. NM_001033028.1.
NP_055423.1. NM_014608.2.

UniGene

Hs.26704.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3P8C	X-ray	2.29	A	1-1253	[»]

ProteinModelPortal

Q7L576.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38873N.

IntAct

Q7L576. 15 interactions.

MINT

MINT-1731056.

STRING

Q7L576.

PTM databases

PhosphoSite

Q7L576.

Polymorphism databases

DMDM

74738589.

Proteomic databases

PRIDE

Q7L576.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313077; ENSP00000324549; ENSG00000068793.

GeneID

23191.

KEGG

hsa:23191.

UCSC

uc001yus.1. human.
uc001yuu.1. human.

Organism-specific databases

CTD

23191.

GeneCards

GC15P023761.

H-InvDB

HIX0012039.

HGNC

HGNC:13759. CYFIP1.

MIM

606322. gene.

neXtProt

NX_Q7L576.

Orphanet

72. Angelman syndrome.

PharmGKB

PA38367.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13389.

GeneTree

ENSGT00500000044831.

HOVERGEN

HBG053209.

InParanoid

Q7L576.

OrthoDB

EOG4R7V8X.

PhylomeDB

Q7L576.

Gene expression databases

ArrayExpress

Q7L576.

Bgee

Q7L576.

CleanEx

HS_CYFIP1.

Genevestigator

Q7L576.

Family and domain databases

InterPro

IPR008081. Cytoplasmic_FMR1-int.
IPR016536. Cytoplasmic_FMR1-int_sub.
[Graphical view]

KO

K05749.

PANTHER

PTHR12195. FragX_IP. 1 hit.

Pfam

PF05994. FragX_IP. 1 hit.
[Graphical view]

PIRSF

PIRSF008153. FMR1_interacting. 1 hit.

PRINTS

PR01698. CYTOFMRPINTP.

ProtoNet

Search...

Other

NextBio

44673.

SOURCE

Search...

Entry information

Entry name

CYFP1_HUMAN

Accession

Primary (citable) accession number: Q7L576
Secondary accession number(s): A8K6D9 , Q14467, Q5IED0, Q6ZSX1, Q9BSD9, Q9BVC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.