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O00165 (HAX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
HCLS1-associated protein X-1
Alternative name(s):
HS1-associating protein X-1
Short name=HAX-1
HS1-binding protein 1
Short name=HSP1BP-1
Gene names
Name:HAX1
Synonyms:HS1BP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes cell survival. Potentiates 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. May regulate intracellular calcium pools. Ref.1 Ref.10 Ref.11 Ref.12 Ref.16 Ref.17

Subunit structure

Interacts with ABCB1, ABCB4 and ABCB11 By similarity. Directly associates with HCLS1/HS1, through binding to its N-terminal region. Interacts with CTTN. Interacts with PKD2. Interacts with GNA13. Interacts with CASP9. Interacts with ITGB6. Interacts with PLN and ATP2A2; these interactions are inhibited by calcium. Interacts with GRB7. Interacts (via C-terminus) with XIAP/BIRC4 (via BIR 2 domain and BIR 3 domain) and this interaction blocks ubiquitination of XIAP/BIRC4. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18 Ref.20

Subcellular location

Mitochondrion. Endoplasmic reticulum. Nucleus membrane. Cytoplasmic vesicle By similarity. Sarcoplasmic reticulum By similarity Ref.1 Ref.17.

Tissue specificity

Ubiquitous. Up-regulated in oral cancers. Ref.1 Ref.12

Post-translational modification

Proteolytically cleaved by caspase-3 during apoptosis. Ref.8 Ref.16

Involvement in 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.
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 (Ref.15). Ref.14 Ref.15 Ref.21 Ref.22

Sequence similarities

Belongs to the HAX1 family.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Membrane
Mitochondrion
Nucleus
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cytokine stimulus

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of granulocyte differentiation

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

regulation of actin filament polymerization

Inferred from mutant phenotype PubMed 23001182. Source: BHF-UCL

   Cellular_componentactin cytoskeleton

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: BHF-UCL

lamellipodium

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrion

Inferred from direct assay Ref.1. Source: UniProtKB

nuclear envelope

Traceable author statement Ref.1. Source: ProtInc

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcription factor complex

Inferred from direct assay PubMed 23001182. Source: BHF-UCL

   Molecular_functioninterleukin-1 binding

Inferred from direct assay PubMed 11554782. Source: UniProtKB

protein N-terminus binding

Inferred from direct assay PubMed 11554782. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O00165-1)

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 (identifier: O00165-2)

The sequence of this isoform differs from the canonical sequence as follows:
     105-105: P → PANTCHLSA
Isoform 3 (identifier: O00165-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
Isoform 4 (identifier: O00165-4)

The sequence of this isoform differs from the canonical sequence as follows:
     106-124: ELPGPESETPGERLREGQT → GVWLSLRGNLWFLVGWWVK
     125-279: Missing.
Isoform 5 (identifier: O00165-5)

The sequence of this isoform differs from the canonical sequence as follows:
     18-65: Missing.
Isoform 6 (identifier: O00165-6)

The sequence of this isoform differs from the canonical sequence as follows:
     85-264: VRDFNSIFSD...SPRPPALDDA → NFQVLSQRHL...SPNPISRASL
     265-279: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 279278HCLS1-associated protein X-1
PRO_0000083906

Regions

Region2 – 4140Required for localization in mitochondria By similarity
Region114 – 279166Involved in HCLS1 binding
Region175 – 20632Involved in CASP9 binding
Region176 – 24772Involved in GNA13 binding
Region183 – 27997Required for localization in sarcoplasmic reticulum By similarity
Region184 – 27996Involved in PKD2 binding
Region203 – 24543Involved in ATP2A2 binding
Region203 – 22523Involved in PLN binding
Region270 – 27910Required for ITGB6 binding
Compositional bias30 – 4011Asp/Glu-rich (highly acidic)

Sites

Site127 – 1282Cleavage; by caspase-3

Amino acid modifications

Modified residue21N-acetylserine Ref.8

Natural variations

Alternative sequence1 – 2626Missing in isoform 3.
VSP_038536
Alternative sequence18 – 6548Missing in isoform 5.
VSP_038543
Alternative sequence85 – 264180VRDFN…ALDDA → NFQVLSQRHLVRDYGRDRHF GTQCLSIQIVTSPGSLGGSW RVMQEVNPPNQHQTGAPRGH FIGLMMYGLWTPILEPERTM ILIPRFPRRVLARFYSPSPN PISRASL in isoform 6.
VSP_038544
Alternative sequence1051P → PANTCHLSA in isoform 2.
VSP_038537
Alternative sequence106 – 12419ELPGP…REGQT → GVWLSLRGNLWFLVGWWVK in isoform 4.
VSP_038538
Alternative sequence125 – 279155Missing in isoform 4.
VSP_038539
Alternative sequence265 – 27915Missing in isoform 6.
VSP_038545
Natural variant491P → S.
Corresponds to variant rs11556344 [ dbSNP | Ensembl ].
VAR_062258
Natural variant1301L → R in SCN3. Ref.22
Corresponds to variant rs179363871 [ dbSNP | Ensembl ].
VAR_064514
Natural variant1411F → L in SCN3; mild form. Ref.21
Corresponds to variant rs179363870 [ dbSNP | Ensembl ].
VAR_062259
Natural variant1511S → G. Ref.7
Corresponds to variant rs17851425 [ dbSNP | Ensembl ].
VAR_062260
Natural variant1721V → I in SCN3. Ref.22
Corresponds to variant rs141970914 [ dbSNP | Ensembl ].
VAR_064515
Natural variant2781S → P.
Corresponds to variant rs1804715 [ dbSNP | Ensembl ].
VAR_062261

Experimental info

Sequence conflict251G → V in BAG62359. Ref.3
Sequence conflict451G → R in AAB51196. Ref.1
Sequence conflict2011Q → T in AAB51196. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 87EEF0C46857704B

FASTA27931,621
        10         20         30         40         50         60 
MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE 

        70         80         90        100        110        120 
FGFGFSFSPG GGIRFHDNFG FDDLVRDFNS IFSDMGAWTL PSHPPELPGP ESETPGERLR 

       130        140        150        160        170        180 
EGQTLRDSML KYPDSHQPRI FGGVLESDAR SESPQPAPDW GSQRPFHRFD DVWPMDPHPR 

       190        200        210        220        230        240 
TREDNDLDSQ VSQEGLGPVL QPQPKSYFKS ISVTKITKPD GIVEERRTVV DSEGRTETTV 

       250        260        270 
TRHEADSSPR GDPESPRPPA LDDAFSILDL FLGRWFRSR 

« Hide

Isoform 2 [UniParc].

Checksum: 762F6F8897C11AB9
Show »

FASTA28732,418
Isoform 3 [UniParc].

Checksum: A7F85EF8A7E6E0AB
Show »

FASTA25328,646
Isoform 4 [UniParc].

Checksum: B59B40DC8DF641E3
Show »

FASTA12414,235
Isoform 5 [UniParc].

Checksum: 25EF194EC019C474
Show »

FASTA23126,100
Isoform 6 [UniParc].

Checksum: E9D736737D3F978F
Show »

FASTA19121,801

References

« Hide 'large scale' references
[1]"HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases."
Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U., Watanabe T.
J. Immunol. 158:2736-2744(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HCLS1, TISSUE SPECIFICITY.
Tissue: Cervix adenocarcinoma.
[2]"Existence of multiple isoforms of HS1-associated protein X-1 in murine and human tissues."
Lees D.M., Hart I.R., Marshall J.F.
J. Mol. Biol. 379:645-655(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
[3]Trebinska A., Grzybowska E.A.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
Tissue: Lung.
[4]"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. expand/collapse author list , 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; 2 AND 4).
Tissue: Amygdala, Heart and Skeletal muscle.
[5]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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), VARIANT GLY-151.
Tissue: Brain, Lung and Skin.
[8]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17 AND 140-150, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[9]"The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton."
Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R.
Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKD2.
[10]"Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1."
Radhika V., Onesime D., Ha J.H., Dhanasekaran N.
J. Biol. Chem. 279:49406-49413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNA13, FUNCTION.
[11]"Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition."
Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T., Kang P.M.
Circ. Res. 99:415-423(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP9, FUNCTION.
[12]"HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin alphavbeta6."
Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M., Violette S., Weinreb P., Hart I.R., Marshall J.F.
Cancer Res. 67:5275-5284(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB6, FUNCTION, TISSUE SPECIFICITY.
[13]"Phospholamban interacts with HAX-1, a mitochondrial protein with anti-apoptotic function."
Vafiadaki E., Sanoudou D., Arvanitis D.A., Catino D.H., Kranias E.G., Kontrogianni-Konstantopoulos A.
J. Mol. Biol. 367:65-79(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLN.
[14]"HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease)."
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.
Nat. Genet. 39:86-92(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCN3.
[15]"Novel HAX1 mutations in patients with severe congenital neutropenia reveal isoform-dependent genotype-phenotype associations."
Germeshausen M., Grudzien M., Zeidler C., Abdollahpour H., Yetgin S., Rezaei N., Ballmaier M., Grimbacher B., Welte K., Klein C.
Blood 111:4954-4957(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SCN3, ISOFORM DEPENDENT GENOTYPE-PHENOTYPE ASSOCIATIONS.
[16]"HS 1-associated protein X-1 is cleaved by caspase-3 during apoptosis."
Lee A.Y., Lee Y., Park Y.K., Bae K.-H., Cho S., Lee do H., Park B.C., Kang S., Park S.G.
Mol. Cells 25:86-90(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE SITE, FUNCTION.
[17]"The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival."
Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., Kontrogianni-Konstantopoulos A., Kranias E.G.
Mol. Biol. Cell 20:306-318(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP2A2 AND PLN, FUNCTION, SUBCELLULAR LOCATION.
[18]"Molecular interaction between HAX-1 and XIAP inhibits apoptosis."
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.
Biochem. Biophys. Res. Commun. 393:794-799(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH XIAP/BIRC4.
[19]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Grb7 binds to Hax-1 and undergoes an intramolecular domain association that offers a model for Grb7 regulation."
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.
J. Mol. Recognit. 24:314-321(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB7.
[21]"A novel missense mutation in the HAX1 gene in severe congenital neutropenia patients (Kostmann disease)."
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.
Clin. Genet. 76:569-572(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCN3 LEU-141.
[22]"Digenic mutations in severe congenital neutropenia."
Germeshausen M., Zeidler C., Stuhrmann M., Lanciotti M., Ballmaier M., Welte K.
Haematologica 95:1207-1210(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCN3 ARG-130 AND ILE-172.
+Additional computationally mapped references.

Web resources

HAX1base

HAX1 mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U68566 mRNA. Translation: AAB51196.1.
EU190982 mRNA. Translation: ABW73998.1.
EU190983 mRNA. Translation: ABW73999.1.
AK290626 mRNA. Translation: BAF83315.1.
AK294298 mRNA. Translation: BAG57580.1.
AK300676 mRNA. Translation: BAG62359.1.
AL354980 Genomic DNA. Translation: CAH70479.1.
AL354980 Genomic DNA. Translation: CAH70481.1.
CH471121 Genomic DNA. Translation: EAW53212.1.
BC005240 mRNA. Translation: AAH05240.1.
BC014314 mRNA. Translation: AAH14314.1.
BC015209 mRNA. Translation: AAH15209.1.
BC016730 mRNA. Translation: AAH16730.1.
RefSeqNP_001018238.1. NM_001018837.1.
NP_006109.2. NM_006118.3.
UniGeneHs.199625.

3D structure databases

ProteinModelPortalO00165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115719. 39 interactions.
IntActO00165. 67 interactions.
MINTMINT-1137395.
STRING9606.ENSP00000329002.

PTM databases

PhosphoSiteO00165.

Proteomic databases

PaxDbO00165.
PRIDEO00165.

Protocols and materials databases

DNASU10456.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328703; ENSP00000329002; ENSG00000143575. [O00165-1]
ENST00000447768; ENSP00000403848; ENSG00000143575. [O00165-6]
ENST00000457918; ENSP00000411448; ENSG00000143575. [O00165-5]
ENST00000483970; ENSP00000435088; ENSG00000143575. [O00165-2]
GeneID10456.
KEGGhsa:10456.
UCSCuc001fes.3. human. [O00165-1]
uc001fet.3. human. [O00165-5]
uc009wou.3. human. [O00165-2]

Organism-specific databases

CTD10456.
GeneCardsGC01P154244.
HGNCHGNC:16915. HAX1.
HPAHPA055141.
MIM605998. gene.
610738. phenotype.
neXtProtNX_O00165.
Orphanet99749. Kostmann syndrome.
PharmGKBPA142671700.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45051.
HOVERGENHBG002991.
InParanoidO00165.
KOK16220.
OMAPKPAPDW.
OrthoDBEOG7HTHJ5.
PhylomeDBO00165.
TreeFamTF328619.

Gene expression databases

ArrayExpressO00165.
BgeeO00165.
CleanExHS_HAX1.
GenevestigatorO00165.

Family and domain databases

InterProIPR017248. HS1--assoc_X-1.
[Graphical view]
PANTHERPTHR14938:SF0. PTHR14938:SF0. 1 hit.
PIRSFPIRSF037634. HS1-associating_X-1. 1 hit.
ProtoNetSearch...

Other

GeneWikiHAX1.
GenomeRNAi10456.
NextBio39639.
PMAP-CutDBO00165.
PROO00165.
SOURCESearch...

Entry information

Entry nameHAX1_HUMAN
AccessionPrimary (citable) accession number: O00165
Secondary accession number(s): A8W4W9 expand/collapse secondary AC list , A8W4X0, B4DUJ7, Q5VYD5, Q5VYD7, Q96AU4, Q9BS80
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM