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HCLS1-associated protein X-1 (HS1-associating protein X-1) (HAX-1) (HS1-binding protein 1) (HSP1BP-1)

 HAX1_HUMAN              Reviewed;         279 AA.
O00165; A8W4W9; A8W4X0; B4DUJ7; Q5VYD5; Q5VYD7; Q96AU4; Q9BS80;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
12-SEP-2018, entry version 174.
RecName: Full=HCLS1-associated protein X-1;
AltName: Full=HS1-associating protein X-1;
Short=HAX-1;
AltName: Full=HS1-binding protein 1;
Short=HSP1BP-1;
Name=HAX1; Synonyms=HS1BP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, INTERACTION WITH HCLS1, AND TISSUE SPECIFICITY.
TISSUE=Cervix adenocarcinoma;
PubMed=9058808;
Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U.,
Watanabe T.;
"HAX-1, a novel intracellular protein, localized on mitochondria,
directly associates with HS1, a substrate of Src family tyrosine
kinases.";
J. Immunol. 158:2736-2744(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
PubMed=18472110; DOI=10.1016/j.jmb.2008.04.020;
Lees D.M., Hart I.R., Marshall J.F.;
"Existence of multiple isoforms of HS1-associated protein X-1 in
murine and human tissues.";
J. Mol. Biol. 379:645-655(2008).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
TISSUE=Lung;
Trebinska A., Grzybowska E.A.;
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Amygdala, Heart, and Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLY-151.
TISSUE=Brain, Lung, and Skin;
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).
[8]
PROTEIN SEQUENCE OF 2-17 AND 140-150, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
Submitted (JUL-2007) to UniProtKB.
[9]
INTERACTION WITH PKD2.
PubMed=10760273; DOI=10.1073/pnas.97.8.4017;
Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R.;
"The polycystic kidney disease protein PKD2 interacts with Hax-1, a
protein associated with the actin cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000).
[10]
INTERACTION WITH GNA13, AND FUNCTION.
PubMed=15339924; DOI=10.1074/jbc.M408836200;
Radhika V., Onesime D., Ha J.H., Dhanasekaran N.;
"Galpha13 stimulates cell migration through cortactin-interacting
protein Hax-1.";
J. Biol. Chem. 279:49406-49413(2004).
[11]
INTERACTION WITH CASP9, AND FUNCTION.
PubMed=16857965; DOI=10.1161/01.RES.0000237387.05259.a5;
Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T.,
Kang P.M.;
"Overexpression of HAX-1 protects cardiac myocytes from apoptosis
through caspase-9 inhibition.";
Circ. Res. 99:415-423(2006).
[12]
INTERACTION WITH ITGB6, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17545607; DOI=10.1158/0008-5472.CAN-07-0318;
Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M.,
Violette S., Weinreb P., Hart I.R., Marshall J.F.;
"HS1-associated protein X-1 regulates carcinoma cell migration and
invasion via clathrin-mediated endocytosis of integrin alphavbeta6.";
Cancer Res. 67:5275-5284(2007).
[13]
INTERACTION WITH PLN.
PubMed=17241641; DOI=10.1016/j.jmb.2006.10.057;
Vafiadaki E., Sanoudou D., Arvanitis D.A., Catino D.H., Kranias E.G.,
Kontrogianni-Konstantopoulos A.;
"Phospholamban interacts with HAX-1, a mitochondrial protein with
anti-apoptotic function.";
J. Mol. Biol. 367:65-79(2007).
[14]
INVOLVEMENT IN SCN3.
PubMed=17187068; DOI=10.1038/ng1940;
Klein C., Grudzien M., Appaswamy G., Germeshausen M., Sandrock I.,
Schaeffer A.A., Rathinam C., Boztug K., Schwinzer B., Rezaei N.,
Bohn G., Melin M., Carlsson G., Fadeel B., Dahl N., Palmblad J.,
Henter J.-I., Zeidler C., Grimbacher B., Welte K.;
"HAX1 deficiency causes autosomal recessive severe congenital
neutropenia (Kostmann disease).";
Nat. Genet. 39:86-92(2007).
[15]
INVOLVEMENT IN SCN3, AND ISOFORM DEPENDENT GENOTYPE-PHENOTYPE
ASSOCIATIONS.
PubMed=18337561; DOI=10.1182/blood-2007-11-120667;
Germeshausen M., Grudzien M., Zeidler C., Abdollahpour H., Yetgin S.,
Rezaei N., Ballmaier M., Grimbacher B., Welte K., Klein C.;
"Novel HAX1 mutations in patients with severe congenital neutropenia
reveal isoform-dependent genotype-phenotype associations.";
Blood 111:4954-4957(2008).
[16]
CLEAVAGE SITE, AND FUNCTION.
PubMed=18319618;
Lee A.Y., Lee Y., Park Y.K., Bae K.-H., Cho S., Lee do H., Park B.C.,
Kang S., Park S.G.;
"HS 1-associated protein X-1 is cleaved by caspase-3 during
apoptosis.";
Mol. Cells 25:86-90(2008).
[17]
INTERACTION WITH ATP2A2 AND PLN, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18971376; DOI=10.1091/mbc.E08-06-0587;
Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D.,
Kontrogianni-Konstantopoulos A., Kranias E.G.;
"The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates
its protein levels to promote cell survival.";
Mol. Biol. Cell 20:306-318(2009).
[18]
INTERACTION WITH XIAP/BIRC4.
PubMed=20171186; DOI=10.1016/j.bbrc.2010.02.084;
Kang Y.J., Jang M., Park Y.K., Kang S., Bae K.H., Cho S., Lee C.K.,
Park B.C., Chi S.W., Park S.G.;
"Molecular interaction between HAX-1 and XIAP inhibits apoptosis.";
Biochem. Biophys. Res. Commun. 393:794-799(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH GRB7.
PubMed=20665473; DOI=10.1002/jmr.1062;
Siamakpour-Reihani S., Peterson T.A., Bradford A.M., Argiros H.J.,
Haas L.L., Lor S.N., Haulsee Z.M., Spuches A.M., Johnson D.L.,
Rohrschneider L.R., Shuster C.B., Lyons B.A.;
"Grb7 binds to Hax-1 and undergoes an intramolecular domain
association that offers a model for Grb7 regulation.";
J. Mol. Recognit. 24:314-321(2011).
[21]
ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (ISOFORMS 1; 3; 4 AND 5),
AND INTERACTION WITH XPO1.
PubMed=23164465; DOI=10.1111/febs.12066;
Grzybowska E.A., Zayat V., Konopinski R., Trebinska A., Szwarc M.,
Sarnowska E., Macech E., Korczynski J., Knapp A., Siedlecki J.A.;
"HAX-1 is a nucleocytoplasmic shuttling protein with a possible role
in mRNA processing.";
FEBS J. 280:256-272(2013).
[22]
INTERACTION WITH TPC2.
PubMed=24188827; DOI=10.1016/j.febslet.2013.10.031;
Lam A.K., Galione A., Lai F.A., Zissimopoulos S.;
"Hax-1 identified as a two-pore channel (TPC)-binding protein.";
FEBS Lett. 587:3782-3786(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-192, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
FUNCTION, INTERACTION WITH KCNC3, AND SUBCELLULAR LOCATION.
PubMed=26997484; DOI=10.1016/j.cell.2016.02.009;
Zhang Y., Zhang X.F., Fleming M.R., Amiri A., El-Hassar L.,
Surguchev A.A., Hyland C., Jenkins D.P., Desai R., Brown M.R.,
Gazula V.R., Waters M.F., Large C.H., Horvath T.L., Navaratnam D.,
Vaccarino F.M., Forscher P., Kaczmarek L.K.;
"Kv3.3 channels bind Hax-1 and Arp2/3 to assemble a stable local actin
network that regulates channel gating.";
Cell 165:434-448(2016).
[27]
VARIANT SCN3 LEU-141.
PubMed=19796188; DOI=10.1111/j.1399-0004.2009.01244.x;
Faiyaz-Ul-Haque M., Al-Jefri A., Abalkhail H.A., Toulimat M.,
Al-Muallimi M.A., Pulicat M.S., Gaafar A., Alaiya A.A., Al-Dayel F.,
Peltekova I., Zaidi S.H.;
"A novel missense mutation in the HAX1 gene in severe congenital
neutropenia patients (Kostmann disease).";
Clin. Genet. 76:569-572(2009).
[28]
VARIANTS SCN3 ARG-130 AND ILE-172.
PubMed=20220065; DOI=10.3324/haematol.2009.017665;
Germeshausen M., Zeidler C., Stuhrmann M., Lanciotti M., Ballmaier M.,
Welte K.;
"Digenic mutations in severe congenital neutropenia.";
Haematologica 95:1207-1210(2010).
-!- FUNCTION: Recruits the Arp2/3 complex to the cell cortex and
regulates reorganization of the cortical actin cytoskeleton via
its interaction with KCNC3 and the Arp2/3 complex
(PubMed:26997484). Slows down the rate of inactivation of KCNC3
channels (PubMed:26997484). Promotes GNA13-mediated cell
migration. Involved in the clathrin-mediated endocytosis pathway.
May be involved in internalization of ABC transporters such as
ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May
regulate intracellular calcium pools.
{ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16857965,
ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:18319618,
ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:26997484,
ECO:0000269|PubMed:9058808}.
-!- SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (By similarity).
Directly associates with HCLS1/HS1, through binding to its N-
terminal region (PubMed:9058808). Interacts with CTTN (By
similarity). Interacts with PKD2 (PubMed:10760273). Interacts with
GNA13 (PubMed:15339924). Interacts with CASP9 (PubMed:16857965).
Interacts with ITGB6 (PubMed:17545607). Interacts with PLN and
ATP2A2; these interactions are inhibited by calcium
(PubMed:17241641, PubMed:18971376). Interacts with GRB7
(PubMed:20665473). Interacts (via C-terminus) with XIAP/BIRC4 (via
BIR 2 domain and BIR 3 domain) and this interaction blocks
ubiquitination of XIAP/BIRC4 (PubMed:20171186). Interacts with
TPC2 (PubMed:24188827). Interacts with KCNC3 (PubMed:26997484).
Interacts with XPO1 (PubMed:23164465).
{ECO:0000250|UniProtKB:Q7TSE9, ECO:0000269|PubMed:10760273,
ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16857965,
ECO:0000269|PubMed:17241641, ECO:0000269|PubMed:17545607,
ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:20171186,
ECO:0000269|PubMed:20665473, ECO:0000269|PubMed:23164465,
ECO:0000269|PubMed:24188827, ECO:0000269|PubMed:26997484,
ECO:0000269|PubMed:9058808}.
-!- INTERACTION:
Q68871:- (xeno); NbExp=3; IntAct=EBI-357001, EBI-12522528;
P03372:ESR1; NbExp=2; IntAct=EBI-357001, EBI-78473;
Q14451:GRB7; NbExp=2; IntAct=EBI-357001, EBI-970191;
P01583:IL1A; NbExp=3; IntAct=EBI-357001, EBI-1749782;
Q9BRX2:PELO; NbExp=7; IntAct=EBI-357001, EBI-1043580;
Q9H4B6:SAV1; NbExp=7; IntAct=EBI-357001, EBI-1017775;
Q9ULQ1:TPCN1; NbExp=2; IntAct=EBI-357001, EBI-5239895;
Q8NHX9:TPCN2; NbExp=4; IntAct=EBI-357001, EBI-5239949;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18971376,
ECO:0000269|PubMed:9058808}. Endoplasmic reticulum
{ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Nucleus
membrane {ECO:0000269|PubMed:9058808}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:O35387}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:26997484}. Cell membrane
{ECO:0000269|PubMed:26997484}; Peripheral membrane protein
{ECO:0000269|PubMed:26997484}; Cytoplasmic side
{ECO:0000269|PubMed:26997484}. Sarcoplasmic reticulum
{ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body
{ECO:0000269|PubMed:23164465}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:23164465}. Nucleus
{ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic.
Also detected in the nucleus when nuclear export is inhibited, and
in response to cellular stress caused by arsenite (in vitro).
{ECO:0000269|PubMed:23164465}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm
{ECO:0000269|PubMed:23164465}. Nucleus
{ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic.
Also detected in the nucleus when nuclear export is inhibited (in
vitro). {ECO:0000269|PubMed:23164465}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm
{ECO:0000269|PubMed:23164465}. Nucleus
{ECO:0000269|PubMed:23164465}. Note=Shuttles between nucleus and
cytoplasm. {ECO:0000269|PubMed:23164465}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm
{ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic.
{ECO:0000269|PubMed:23164465}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=O00165-1; Sequence=Displayed;
Name=2;
IsoId=O00165-2; Sequence=VSP_038537;
Name=3;
IsoId=O00165-3; Sequence=VSP_038536;
Name=4;
IsoId=O00165-4; Sequence=VSP_038538, VSP_038539;
Name=5;
IsoId=O00165-5; Sequence=VSP_038543;
Name=6;
IsoId=O00165-6; Sequence=VSP_038544, VSP_038545;
-!- TISSUE SPECIFICITY: Ubiquitous. Up-regulated in oral cancers.
{ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:9058808}.
-!- PTM: Proteolytically cleaved by caspase-3 during apoptosis.
{ECO:0000269|PubMed:18319618}.
-!- DISEASE: Neutropenia, severe congenital 3, autosomal recessive
(SCN3) [MIM:610738]: A disorder of hematopoiesis characterized by
maturation arrest of granulopoiesis at the level of promyelocytes
with peripheral blood absolute neutrophil counts below 0.5 x
10(9)/l and early onset of severe bacterial infections. Some
patients affected by severe congenital neutropenia type 3 have
neurological manifestations such as psychomotor retardation and
seizures. {ECO:0000269|PubMed:17187068,
ECO:0000269|PubMed:18337561, ECO:0000269|PubMed:19796188,
ECO:0000269|PubMed:20220065}. Note=The disease is caused by
mutations affecting the gene represented in this entry. The
clinical phenotype due to HAX1 deficiency appears to depend on the
localization of the mutations and their influence on the
transcript variants. Mutations affecting exclusively isoform 1 are
associated with isolated congenital neutropenia, whereas mutations
affecting both isoform 1 and isoform 5 are associated with
additional neurologic symptoms (PubMed:18337561).
{ECO:0000269|PubMed:18337561}.
-!- SIMILARITY: Belongs to the HAX1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=HAX1base; Note=HAX1 mutation db;
URL="http://structure.bmc.lu.se/idbase/HAX1base/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U68566; AAB51196.1; -; mRNA.
EMBL; EU190982; ABW73998.1; -; mRNA.
EMBL; EU190983; ABW73999.1; -; mRNA.
EMBL; AK290626; BAF83315.1; -; mRNA.
EMBL; AK294298; BAG57580.1; -; mRNA.
EMBL; AK300676; BAG62359.1; -; mRNA.
EMBL; AL354980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53212.1; -; Genomic_DNA.
EMBL; BC005240; AAH05240.1; -; mRNA.
EMBL; BC014314; AAH14314.1; -; mRNA.
EMBL; BC015209; AAH15209.1; -; mRNA.
EMBL; BC016730; AAH16730.1; -; mRNA.
CCDS; CCDS1064.1; -. [O00165-1]
CCDS; CCDS44230.1; -. [O00165-5]
RefSeq; NP_001018238.1; NM_001018837.1. [O00165-5]
RefSeq; NP_006109.2; NM_006118.3. [O00165-1]
UniGene; Hs.199625; -.
ProteinModelPortal; O00165; -.
BioGrid; 115719; 127.
CORUM; O00165; -.
DIP; DIP-36771N; -.
IntAct; O00165; 111.
MINT; O00165; -.
STRING; 9606.ENSP00000329002; -.
iPTMnet; O00165; -.
PhosphoSitePlus; O00165; -.
BioMuta; HAX1; -.
EPD; O00165; -.
MaxQB; O00165; -.
PaxDb; O00165; -.
PeptideAtlas; O00165; -.
PRIDE; O00165; -.
ProteomicsDB; 47750; -.
ProteomicsDB; 47751; -. [O00165-2]
ProteomicsDB; 47752; -. [O00165-3]
ProteomicsDB; 47753; -. [O00165-4]
ProteomicsDB; 47754; -. [O00165-5]
ProteomicsDB; 47755; -. [O00165-6]
TopDownProteomics; O00165-2; -. [O00165-2]
DNASU; 10456; -.
Ensembl; ENST00000328703; ENSP00000329002; ENSG00000143575. [O00165-1]
Ensembl; ENST00000447768; ENSP00000403848; ENSG00000143575. [O00165-6]
Ensembl; ENST00000457918; ENSP00000411448; ENSG00000143575. [O00165-5]
Ensembl; ENST00000483970; ENSP00000435088; ENSG00000143575. [O00165-2]
GeneID; 10456; -.
KEGG; hsa:10456; -.
UCSC; uc001fes.5; human. [O00165-1]
CTD; 10456; -.
DisGeNET; 10456; -.
EuPathDB; HostDB:ENSG00000143575.14; -.
GeneCards; HAX1; -.
HGNC; HGNC:16915; HAX1.
HPA; HPA055141; -.
HPA; HPA075289; -.
MalaCards; HAX1; -.
MIM; 605998; gene.
MIM; 610738; phenotype.
neXtProt; NX_O00165; -.
OpenTargets; ENSG00000143575; -.
Orphanet; 99749; Kostmann syndrome.
PharmGKB; PA142671700; -.
eggNOG; ENOG410IJQ0; Eukaryota.
eggNOG; ENOG411211U; LUCA.
GeneTree; ENSGT00390000018324; -.
HOVERGEN; HBG002991; -.
InParanoid; O00165; -.
KO; K16220; -.
OMA; PKPAPDW; -.
OrthoDB; EOG091G0MK9; -.
PhylomeDB; O00165; -.
TreeFam; TF328619; -.
SIGNOR; O00165; -.
GeneWiki; HAX1; -.
GenomeRNAi; 10456; -.
PMAP-CutDB; O00165; -.
PRO; PR:O00165; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143575; Expressed in 236 organ(s), highest expression level in apex of heart.
CleanEx; HS_HAX1; -.
ExpressionAtlas; O00165; baseline and differential.
Genevisible; O00165; HS.
GO; GO:0015629; C:actin cytoskeleton; ISS:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0019966; F:interleukin-1 binding; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IDA:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0030833; P:regulation of actin filament polymerization; IMP:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; TAS:ParkinsonsUK-UCL.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; TAS:ParkinsonsUK-UCL.
InterPro; IPR017248; HAX-1.
PIRSF; PIRSF037634; HS1-associating_X-1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
Disease mutation; Endoplasmic reticulum; Membrane; Mitochondrion;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Sarcoplasmic reticulum.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8}.
CHAIN 2 279 HCLS1-associated protein X-1.
/FTId=PRO_0000083906.
REGION 2 41 Required for localization in
mitochondria. {ECO:0000250}.
REGION 114 279 Involved in HCLS1 binding.
REGION 175 206 Involved in CASP9 binding.
REGION 176 247 Involved in GNA13 binding.
REGION 183 279 Required for localization in sarcoplasmic
reticulum. {ECO:0000250}.
REGION 184 279 Involved in PKD2 binding.
REGION 203 245 Involved in ATP2A2 binding.
REGION 203 225 Involved in PLN binding.
REGION 270 279 Required for ITGB6 binding.
COMPBIAS 30 40 Asp/Glu-rich (highly acidic).
SITE 127 128 Cleavage; by caspase-3.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 26 Missing (in isoform 3).
{ECO:0000303|PubMed:18472110,
ECO:0000303|Ref.3}.
/FTId=VSP_038536.
VAR_SEQ 18 65 Missing (in isoform 5).
{ECO:0000303|PubMed:18472110}.
/FTId=VSP_038543.
VAR_SEQ 85 264 VRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTL
RDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPF
HRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSY
FKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSS
PRGDPESPRPPALDDA -> NFQVLSQRHLVRDYGRDRHFG
TQCLSIQIVTSPGSLGGSWRVMQEVNPPNQHQTGAPRGHFI
GLMMYGLWTPILEPERTMILIPRFPRRVLARFYSPSPNPIS
RASL (in isoform 6).
{ECO:0000303|PubMed:18472110}.
/FTId=VSP_038544.
VAR_SEQ 105 105 P -> PANTCHLSA (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18472110}.
/FTId=VSP_038537.
VAR_SEQ 106 124 ELPGPESETPGERLREGQT -> GVWLSLRGNLWFLVGWWV
K (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18472110,
ECO:0000303|Ref.3}.
/FTId=VSP_038538.
VAR_SEQ 125 279 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18472110,
ECO:0000303|Ref.3}.
/FTId=VSP_038539.
VAR_SEQ 265 279 Missing (in isoform 6).
{ECO:0000303|PubMed:18472110}.
/FTId=VSP_038545.
VARIANT 49 49 P -> S (in dbSNP:rs11556344).
/FTId=VAR_062258.
VARIANT 130 130 L -> R (in SCN3; dbSNP:rs179363871).
{ECO:0000269|PubMed:20220065}.
/FTId=VAR_064514.
VARIANT 141 141 F -> L (in SCN3; mild form;
dbSNP:rs179363870).
{ECO:0000269|PubMed:19796188}.
/FTId=VAR_062259.
VARIANT 151 151 S -> G (in dbSNP:rs17851425).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_062260.
VARIANT 172 172 V -> I (in SCN3; dbSNP:rs141970914).
{ECO:0000269|PubMed:20220065}.
/FTId=VAR_064515.
VARIANT 278 278 S -> P (in dbSNP:rs1804715).
/FTId=VAR_062261.
CONFLICT 25 25 G -> V (in Ref. 3; BAG62359).
{ECO:0000305}.
CONFLICT 45 45 G -> R (in Ref. 1; AAB51196).
{ECO:0000305}.
CONFLICT 201 201 Q -> T (in Ref. 1; AAB51196).
{ECO:0000305}.
SEQUENCE 279 AA; 31621 MW; 87EEF0C46857704B CRC64;
MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE
FGFGFSFSPG GGIRFHDNFG FDDLVRDFNS IFSDMGAWTL PSHPPELPGP ESETPGERLR
EGQTLRDSML KYPDSHQPRI FGGVLESDAR SESPQPAPDW GSQRPFHRFD DVWPMDPHPR
TREDNDLDSQ VSQEGLGPVL QPQPKSYFKS ISVTKITKPD GIVEERRTVV DSEGRTETTV
TRHEADSSPR GDPESPRPPA LDDAFSILDL FLGRWFRSR


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