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

Adherens junction-associated protein 1 (Membrane protein shrew-1)

 AJAP1_HUMAN             Reviewed;         411 AA.
Q9UKB5; Q9Y229;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 121.
RecName: Full=Adherens junction-associated protein 1;
AltName: Full=Membrane protein shrew-1;
Name=AJAP1; Synonyms=MOT8, SHREW1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
TOPOLOGY, AND INTERACTION WITH CDH1 AND CTNNB1.
TISSUE=Brain;
PubMed=14595118; DOI=10.1091/mbc.E03-05-0281;
Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A.,
Baumann R., Starzinski-Powitz A.;
"Novel membrane protein shrew-1 targets to cadherin-mediated junctions
in polarized epithelial cells.";
Mol. Biol. Cell 15:397-406(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibrosarcoma;
Kudoh S., Chung I.M., Tsuiji M., Tsuji T., Irimura T.;
"Identification of genes differentially expressed in HT1080 human
fibrosarcoma cells selected for invasive capacity in vitro.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 179-411.
Rhodes S.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND VARIANT ARG-263.
PubMed=16410724; DOI=10.4161/cbt.5.3.2391;
McDonald J.M., Dunlap S., Cogdell D., Dunmire V., Wei Q.,
Starzinski-Powitz A., Sawaya R., Bruner J., Fuller G.N., Aldape K.,
Zhang W.;
"The SHREW1 gene, frequently deleted in oligodendrogliomas, functions
to inhibit cell adhesion and migration.";
Cancer Biol. Ther. 5:300-304(2006).
[6]
SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-303; TYR-350; TYR-368;
TYR-380; LEU-396 AND 396-LEU--ILE-397, AND INTERACTION WITH AP1M2.
PubMed=16707570; DOI=10.1091/mbc.E05-11-1034;
Jakob V., Schreiner A., Tikkanen R., Starzinski-Powitz A.;
"Targeting of transmembrane protein shrew-1 to adherens junctions is
controlled by cytoplasmic sorting motifs.";
Mol. Biol. Cell 17:3397-3408(2006).
[7]
FUNCTION, AND INTERACTION WITH BSG.
PubMed=17267690; DOI=10.1091/mbc.E06-07-0637;
Schreiner A., Ruonala M., Jakob V., Suthaus J., Boles E., Wouters F.,
Starzinski-Powitz A.;
"junction protein shrew-1 influences cell invasion and interacts with
invasion-promoting protein CD147.";
Mol. Biol. Cell 18:1272-1281(2007).
-!- FUNCTION: Plays a role in cell adhesion and cell migration.
{ECO:0000269|PubMed:16410724, ECO:0000269|PubMed:17267690}.
-!- SUBUNIT: Forms a complex with CDH1 and CTNNB1; interacts directly
with CTNNB1. Interacts with AP1M2 and BSG/CD147.
{ECO:0000269|PubMed:14595118, ECO:0000269|PubMed:16707570,
ECO:0000269|PubMed:17267690}.
-!- SUBCELLULAR LOCATION: Basolateral cell membrane; Single-pass type
III membrane protein. Apical cell membrane; Single-pass type III
membrane protein. Cell junction, adherens junction. Note=Mainly
basolateral. Localization is mediated by AP1M2.
-!- TISSUE SPECIFICITY: Expressed in uterus and pancreas (at protein
level). {ECO:0000269|PubMed:14595118}.
-!- PTM: Thr-237 and Ser-239 may be phosphorylated; however as this
position is probably extracellular, the in vivo relevance is not
proven.
-!- SEQUENCE CAUTION:
Sequence=CAB41245.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAB41246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY282806; AAP35025.1; -; mRNA.
EMBL; AF175409; AAD53278.1; -; mRNA.
EMBL; AL391808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL023586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z98886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049672; CAB41245.1; ALT_INIT; mRNA.
EMBL; AL049673; CAB41246.1; ALT_INIT; mRNA.
CCDS; CCDS54.1; -.
RefSeq; NP_001035943.1; NM_001042478.1.
RefSeq; NP_061324.1; NM_018836.3.
RefSeq; XP_011540088.1; XM_011541786.2.
UniGene; Hs.12473; -.
UniGene; Hs.25924; -.
ProteinModelPortal; Q9UKB5; -.
SMR; Q9UKB5; -.
BioGrid; 121012; 2.
IntAct; Q9UKB5; 2.
MINT; Q9UKB5; -.
STRING; 9606.ENSP00000367432; -.
iPTMnet; Q9UKB5; -.
PhosphoSitePlus; Q9UKB5; -.
BioMuta; AJAP1; -.
DMDM; 74761984; -.
MaxQB; Q9UKB5; -.
PaxDb; Q9UKB5; -.
PeptideAtlas; Q9UKB5; -.
PRIDE; Q9UKB5; -.
ProteomicsDB; 84765; -.
DNASU; 55966; -.
Ensembl; ENST00000378190; ENSP00000367432; ENSG00000196581.
Ensembl; ENST00000378191; ENSP00000367433; ENSG00000196581.
GeneID; 55966; -.
KEGG; hsa:55966; -.
UCSC; uc001alm.2; human.
CTD; 55966; -.
DisGeNET; 55966; -.
EuPathDB; HostDB:ENSG00000196581.10; -.
GeneCards; AJAP1; -.
H-InvDB; HIX0028526; -.
HGNC; HGNC:30801; AJAP1.
MIM; 610972; gene.
neXtProt; NX_Q9UKB5; -.
OpenTargets; ENSG00000196581; -.
PharmGKB; PA142672629; -.
eggNOG; ENOG410IHN1; Eukaryota.
eggNOG; ENOG410YW4K; LUCA.
GeneTree; ENSGT00510000048586; -.
HOGENOM; HOG000033873; -.
HOVERGEN; HBG096853; -.
InParanoid; Q9UKB5; -.
KO; K21387; -.
OMA; DFRGSRP; -.
OrthoDB; EOG091G0GGA; -.
PhylomeDB; Q9UKB5; -.
TreeFam; TF336539; -.
ChiTaRS; AJAP1; human.
GenomeRNAi; 55966; -.
PRO; PR:Q9UKB5; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000196581; Expressed in 114 organ(s), highest expression level in orbitofrontal cortex.
CleanEx; HS_AJAP1; -.
Genevisible; Q9UKB5; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
GO; GO:0044291; C:cell-cell contact zone; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0044214; C:spanning component of plasma membrane; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0061045; P:negative regulation of wound healing; IDA:UniProtKB.
GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; IDA:UniProtKB.
InterPro; IPR039239; AJAP1.
InterPro; IPR029198; AJAP1_PANP_C.
PANTHER; PTHR32422; PTHR32422; 1.
Pfam; PF15298; AJAP1_PANP_C; 1.
1: Evidence at protein level;
Cell adhesion; Cell junction; Cell membrane; Complete proteome;
Membrane; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 411 Adherens junction-associated protein 1.
/FTId=PRO_0000284801.
TOPO_DOM 1 282 Extracellular. {ECO:0000255}.
TRANSMEM 283 303 Helical; Signal-anchor for type III
membrane protein. {ECO:0000255}.
TOPO_DOM 304 411 Cytoplasmic. {ECO:0000255}.
REGION 303 411 Targeting signals.
COMPBIAS 175 237 Thr-rich.
VARIANT 263 263 G -> R (in dbSNP:rs242056).
{ECO:0000269|PubMed:16410724}.
/FTId=VAR_031821.
MUTAGEN 303 303 L->A: Mistargeting to the apical
membrane. {ECO:0000269|PubMed:16707570}.
MUTAGEN 350 350 Y->A: Mistargeting to the apical
membrane. {ECO:0000269|PubMed:16707570}.
MUTAGEN 368 368 Y->A: Mistargeting to the apical
membrane. {ECO:0000269|PubMed:16707570}.
MUTAGEN 380 380 Y->A: Mistargeting to the apical
membrane. {ECO:0000269|PubMed:16707570}.
MUTAGEN 396 397 LI->HV: Mistargeting to the apical
membrane. {ECO:0000269|PubMed:16707570}.
MUTAGEN 396 396 L->A: Mistargeting to the apical
membrane. {ECO:0000269|PubMed:16707570}.
SEQUENCE 411 AA; 44536 MW; 42C1C5F56B9FC975 CRC64;
MWIQQLLGLS SMSIRWPGRP LGSHAWILIA MFQLAVDLPA CEALGPGPEF WLLPRSPPRP
PRLWSFRSGQ PARVPAPVWS PRPPRVERIH GQMQMPRARR AHRPRDQAAA LVPKAGLAKP
PAAAKSSPSL ASSSSSSSSA VAGGAPEQQA LLRRGKRHLQ GDGLSSFDSR GSRPTTETEF
IAWGPTGDEE ALESNTFPGV YGPTTVSILQ TRKTTVAATT TTTTTATPMT LQTKGFTESL
DPRRRIPGGV STTEPSTSPS NNGEVTQPPR ILGEASGLAV HQIITITVSL IMVIAALITT
LVLKNCCAQS GNTRRNSHQR KTNQQEESCQ NLTDFPSARV PSSLDIFTAY NETLQCSHEC
VRASVPVYTD ETLHSTTGEY KSTFNGNRPS SSDRHLIPVA FVSEKWFEIS C


Related products :

Catalog number Product name Quantity
AJAP1_HUMAN Human ELISA Kit FOR Adherens junction-associated protein 1 96T
CSB-EL001507RA Rat Adherens junction-associated protein 1(AJAP1) ELISA kit 96T
CSB-EL001507RA Rat Adherens junction-associated protein 1(AJAP1) ELISA kit SpeciesRat 96T
CSB-EL001507MO Mouse Adherens junction-associated protein 1(AJAP1) ELISA kit 96T
CSB-EL001507HU Human Adherens junction-associated protein 1(AJAP1) ELISA kit 96T
CSB-EL001507HU Human Adherens junction-associated protein 1(AJAP1) ELISA kit SpeciesHuman 96T
CSB-EL001507MO Mouse Adherens junction-associated protein 1(AJAP1) ELISA kit SpeciesMouse 96T
EIAAB10183 Connexin-31.9,Cx31.9,Gap junction alpha-11 protein,Gap junction chi-1 protein,Gap junction delta-3 protein,GJA11,GJC1,GJD3,Homo sapiens,Human
EIAAB10182 Connexin-30.2,Cx30.2,Gap junction alpha-11 protein,Gap junction chi-1 protein,Gap junction delta-3 protein,Gja11,Gjc1,Gjd3,Mouse,Mus musculus
29-815 OCLN is an integral membrane protein which is located at tight junctions. This protein may be involved in the formation and maintenance of the tight junction. The possibility of several alternatively 0.1 mg
EIAAB10188 Connexin-45,Cx45,Cxn-45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,Gja7,Gjc1,Mouse,Mus musculus
EIAAB10181 Bos taurus,Bovine,Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,GJA9,GJD2
EIAAB10179 Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,Gja9,Gjd2,Mouse,Mus musculus
EIAAB10195 Connexin-47,Cx47,Gap junction alpha-12 protein,Gap junction gamma-2 protein,Gja12,Gjc2,Rat,Rattus norvegicus
EIAAB10178 Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,Gja9,Gjd2,Rat,Rattus norvegicus
EIAAB10198 Connexin-47,Cx47,Gap junction alpha-12 protein,Gap junction gamma-2 protein,Gja12,Gjc2,Mouse,Mus musculus
EIAAB10189 Connexin-45,Cx45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,Gja7,Gjc1,Rat,Rattus norvegicus
EIAAB10109 Connexin-43,Cx43,Gap junction 43 kDa heart protein,Gap junction alpha-1 protein,GJA1,GJAL,Homo sapiens,Human
EIAAB10180 Connexin-36,Cx36,Gap junction alpha-9 protein,Gap junction delta-2 protein,GJA9,GJD2,Homo sapiens,Human
EIAAB10191 Connexin-45,Cx45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,GJA7,GJC1,Homo sapiens,Human
EIAAB10190 Connexin-45,Cx45,Gap junction alpha-7 protein,Gap junction gamma-1 protein,GJA7,GJC1,Pig,Sus scrofa
EIAAB10147 Connexin-32,Cx32,Cxn-32,GAP junction 28 kDa liver protein,Gap junction beta-1 protein,Gjb1,Rat,Rattus norvegicus
EIAAB10110 Connexin-43,Cx43,Cxn-43,Gap junction 43 kDa heart protein,Gap junction alpha-1 protein,Gja1,Mouse,Mus musculus
EIAAB10113 Connexin-43,Cx43,Cxn-43,Gap junction 43 kDa heart protein,Gap junction alpha-1 protein,Gja1,Rat,Rattus norvegicus
EIAAB47994 Homo sapiens,Human,Tight junction protein 2,Tight junction protein ZO-2,TJP2,X104,ZO2,Zona occludens protein 2,Zonula occludens protein 2


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






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