Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ankyrin repeat domain-containing protein 54 (Lyn-interacting ankyrin repeat protein)

 ANR54_MOUSE             Reviewed;         299 AA.
Q91WK7; Q3UPC5; Q3UZL7;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-APR-2018, entry version 120.
RecName: Full=Ankyrin repeat domain-containing protein 54;
AltName: Full=Lyn-interacting ankyrin repeat protein;
Name=Ankrd54; Synonyms=Liar;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY.
PubMed=17971504; DOI=10.1152/physiolgenomics.00128.2007;
McClintock T.S., Glasser C.E., Bose S.C., Bergman D.A.;
"Tissue expression patterns identify mouse cilia genes.";
Physiol. Genomics 32:198-206(2008).
[4]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF
ARG-98; ARG-99; LEU-289 AND LEU-291, AND INTERACTION WITH LYN; HCLS1;
ITSN2; VAV1; DBNL AND LASP1.
PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
Samuels A.L., Klinken S.P., Ingley E.;
"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
influences erythropoietin-induced differentiation.";
Blood 113:3845-3856(2009).
-!- FUNCTION: Plays an important role in regulating intracellular
signaling events associated with erythroid terminal
differentiation. {ECO:0000269|PubMed:19064729}.
-!- SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-
domain) in an activation-independent status of LYN. Forms a
multiprotein complex with LYN and HCLS1. Interacts with TSN2,
VAV1, DBNL AND LASP1. {ECO:0000269|PubMed:19064729}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19064729}.
Cytoplasm {ECO:0000269|PubMed:19064729}. Midbody
{ECO:0000269|PubMed:19064729}. Note=Shuttles between nucleus and
cytoplasm during the cell cycle. EPO stimulation induces nuclear
accumulation.
-!- TISSUE SPECIFICITY: Expressed in a variety of hemopoietic cell
lines and tissue with high levels in testis. Highly expressed in
ciliated cells. {ECO:0000269|PubMed:17971504,
ECO:0000269|PubMed:19064729}.
-!- DEVELOPMENTAL STAGE: Expressed in brachial arches, maxillary
process, fore and hind limb buds and in the developing
gastrointestinal tract of day 10 embryos.
-!- SEQUENCE CAUTION:
Sequence=BAE25471.1; Type=Frameshift; Positions=291; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK133785; BAE21840.1; -; mRNA.
EMBL; AK143625; BAE25471.1; ALT_FRAME; mRNA.
EMBL; BC014743; AAH14743.1; -; mRNA.
CCDS; CCDS37139.1; -.
RefSeq; NP_659098.1; NM_144849.1.
UniGene; Mm.24262; -.
ProteinModelPortal; Q91WK7; -.
SMR; Q91WK7; -.
IntAct; Q91WK7; 2.
STRING; 10090.ENSMUSP00000047042; -.
iPTMnet; Q91WK7; -.
PhosphoSitePlus; Q91WK7; -.
EPD; Q91WK7; -.
MaxQB; Q91WK7; -.
PaxDb; Q91WK7; -.
PRIDE; Q91WK7; -.
Ensembl; ENSMUST00000040676; ENSMUSP00000047042; ENSMUSG00000033055.
GeneID; 223690; -.
KEGG; mmu:223690; -.
UCSC; uc007wsi.1; mouse.
CTD; 129138; -.
MGI; MGI:2444209; Ankrd54.
eggNOG; KOG0504; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00910000144039; -.
HOGENOM; HOG000008674; -.
HOVERGEN; HBG080858; -.
InParanoid; Q91WK7; -.
KO; K21442; -.
OMA; WQQDAEP; -.
OrthoDB; EOG091G0WXS; -.
PhylomeDB; Q91WK7; -.
TreeFam; TF330790; -.
PRO; PR:Q91WK7; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000033055; -.
CleanEx; MM_ANKRD54; -.
ExpressionAtlas; Q91WK7; baseline and differential.
Genevisible; Q91WK7; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030496; C:midbody; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0019887; F:protein kinase regulator activity; IDA:MGI.
GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:MGI.
GO; GO:1902531; P:regulation of intracellular signal transduction; IDA:MGI.
GO; GO:0045859; P:regulation of protein kinase activity; IDA:MGI.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
SMART; SM00248; ANK; 4.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
1: Evidence at protein level;
Acetylation; ANK repeat; Complete proteome; Cytoplasm; Nucleus;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q6NXT1}.
CHAIN 2 299 Ankyrin repeat domain-containing protein
54.
/FTId=PRO_0000274494.
REPEAT 108 137 ANK 1.
REPEAT 141 170 ANK 2.
REPEAT 174 203 ANK 3.
REPEAT 207 239 ANK 4.
REGION 140 240 LYN-binding.
MOTIF 98 116 Nuclear localization signal (NLS).
MOTIF 282 292 Nuclear export signal (NES).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q6NXT1}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:Q6NXT1}.
MUTAGEN 98 98 R->A: Increases the cytoplasmic protein
content; when associated with A-99.
{ECO:0000269|PubMed:19064729}.
MUTAGEN 99 99 R->A: Increases the cytoplasmic protein
content; when associated with A-98.
{ECO:0000269|PubMed:19064729}.
MUTAGEN 289 289 L->A: Accumulation within the nucleus;
when associated with A-291.
{ECO:0000269|PubMed:19064729}.
MUTAGEN 291 291 L->A: Accumulation within the nucleus;
when associated with A-289.
{ECO:0000269|PubMed:19064729}.
CONFLICT 173 173 G -> N (in Ref. 1; BAE21840).
{ECO:0000305}.
SEQUENCE 299 AA; 32486 MW; 88E91A10F1953AC3 CRC64;
MAATGGGADD ESRSGRSSSD GECAVAPEPL AEAGGLVSFA DFGVSLGSGA GLPGRSVGRA
QSSLRYLQVL WQQDVEPRDE LRCKIPAGRL RRAARPHRRL GPTGKEVHAL KRLRDSANAN
DVETVQQLLE DGADPCAADD KGRTALHFAS CNGNDQIVQL LLDHGADPNQ QDGLGNTPLH
LAACTNHVPV ITTLLRGGAR VDALDRAGRT PLHLAKSKLN ILQEGHSQCL EAVRLEVKQI
IHMLREYLER LGRHEQRERL DDLCTRLQMT STKEQVDEVT DLLASFTSLS LQMQSMEKR


Related products :

Catalog number Product name Quantity
18-003-42394 Ankyrin repeat domain-containing protein 12 - Ankyrin repeat-containing cofactor 2; GAC-1 protein Polyclonal 0.1 mg Protein A
EIAAB34872 ANKRD3,Ankyrin repeat domain-containing protein 3,DIK,Homo sapiens,Human,PKC-delta-interacting protein kinase,Receptor-interacting serine_threonine-protein kinase 4,RIPK4
30-770 ASB11 is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. They contain ankyrin repeat sequence and SOCS box domain. The SOCS box serves to couple suppressor of cytokine 0.05 mg
26-655 ASB12 is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. They contain ankyrin repeat sequence and a SOCS box domain. The SOCS box serves to couple suppressor of cytoki 0.05 mg
18-001-30036 SH3 and multiple ankyrin repeat domains protein 1 - Shank1; Somatostatin receptor-interacting protein; SSTR-interacting protein; SSTRIP Polyclonal 0.1 mg
18-001-30037 SH3 and multiple ankyrin repeat domains protein 1 - Shank1; Somatostatin receptor-interacting protein; SSTR-interacting protein; SSTRIP Polyclonal 0.1 mg
EIAAB38255 GKAP_SAPAP-interacting protein,Rat,Rattus norvegicus,SH3 and multiple ankyrin repeat domains protein 1,Shank1,Shank1,Somatostatin receptor-interacting protein,SPANK-1,SSTR-interacting protein,SSTRIP,S
EIAAB41359 Homo sapiens,Human,KIAA1728,Protein TANC1,TANC1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EIAAB41360 Homo sapiens,Human,KIAA1148,KIAA1636,Protein TANC2,TANC2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41361 Kiaa1148,Mouse,Mus musculus,Protein TANC2,Tanc2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB34873 Ankrd3,Ankyrin repeat domain-containing protein 3,Mouse,Mus musculus,PKC-associated protein kinase,PKC-regulated protein kinase,Pkk,Receptor-interacting serine_threonine-protein kinase 4,Ripk4
EIAAB41358 Mouse,Mus musculus,Protein TANC1,Tanc1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EIAAB31841 A26B3,ANKRD21,ANKRD26-like family B member 3,Ankyrin repeat domain-containing protein 21,Homo sapiens,Human,POTE,POTE ankyrin domain family member D,POTED,Prostate, ovary, testis-expressed protein,Pro
LF-PA40055 anti-Ankyrin Repeat Domain 32 (ANKRD32) , Rabbit polyclonal to Ankyrin Repeat Domain 32 (ANKRD32) , Isotype IgG, Host Rabbit 50 ug
EIAAB46368 DXImx38e,Mouse,Mus musculus,WD repeat domain phosphoinositide-interacting protein 4,WD repeat domain X-linked 1,WD repeat-containing protein 45,Wdr45,Wdrx1,Wipi4,WIPI-4
EIAAB38256 Homo sapiens,Human,SH3 and multiple ankyrin repeat domains protein 1,Shank1,SHANK1,Somatostatin receptor-interacting protein,SSTR-interacting protein,SSTRIP
E02A0077 Rat Ankyrin repeat domain-containing protein 1 ELISA 96T/kit
ANKS6_RAT Rat ELISA Kit FOR Ankyrin repeat and SAM domain-containing protein 6 96T
ANKL2_RAT Rat ELISA Kit FOR Ankyrin repeat and LEM domain-containing protein 2 96T
ANR54_RAT Rat ELISA Kit FOR Ankyrin repeat domain-containing protein 54 96T
EH1832 Ankyrin repeat domain-containing protein 30A Elisa Kit 96T
E1432h Rat ELISA Kit FOR Ankyrin repeat and SAM domain-containing protein 3 96T
ABTB1_RAT Rat ELISA Kit FOR Ankyrin repeat and BTB per POZ domain-containing protein 1 96T
E7326h Human Ankyrin Repeat Domain Protein 42 ELISA Kit 96T
E6876h Human Ankyrin Repeat Domain Protein 30B ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur