Reviewed, UniProtKB/Swiss-Prot O00165 (HAX1_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.15 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. Ref.1 Ref.10 Ref.11 Ref.12 Ref.17 Ref.9 Ref.13
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.15 Ref.8
Involvement in disease	Defects in HAX1 are the cause of autosomal recessive severe congenital neutropenia type 3 (SCN3) [MIM:610738]; also known as Kostmann disease. Autosomal recessive SCN constitutes a primary immunodeficiency syndrome associated with increased apoptosis in myeloid cells. Individuals show a paucity of mature neutrophils in peripheral blood and bone marrow and develop life-threatening bacterial infections. Ref.14
Sequence similarities	Belongs to the HAX1 family.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Endoplasmic reticulum Membrane Mitochondrion Nucleus Sarcoplasmic reticulum
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	actin cytoskeleton Ref.9 Non-traceable author statement. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Ref.1 Inferred from direct assay. Source: UniProtKB nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell sarcoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.1 Traceable author statement. Source: ProtInc
Molecular function	interleukin-1 binding Inferred from direct assay. Source: UniProtKB protein N-terminus binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Abcb11	O70127	1	EBI-357001,EBI-930036	From a different organism.
Abcb1a	Q6PSM0	1	EBI-357001,EBI-930055	From a different organism.

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 279	278	HCLS1-associated protein X-1		PRO_0000083906
Regions
	Region	2 – 41	40	Required for localization in mitochondria By similarity
	Region	114 – 279	166	Involved in HCLS1 binding
	Region	175 – 206	32	Involved in CASP9 binding
	Region	176 – 247	72	Involved in GNA13 binding
	Region	183 – 279	97	Required for localization in sarcoplasmic reticulum By similarity
	Region	184 – 279	96	Involved in PKD2 binding
	Region	203 – 245	43	Involved in ATP2A2 binding
	Region	203 – 225	23	Involved in PLN binding
	Region	270 – 279	10	Required for ITGB6 binding
	Compositional bias	30 – 40	11	Asp/Glu-rich (highly acidic)
Sites
	Site	127 – 128	2	Cleavage; by caspase-3
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.8
Natural variations
	Alternative sequence	1 – 26	26	Missing in isoform 3.		VSP_038536
	Alternative sequence	18 – 65	48	Missing in isoform 5.		VSP_038543
	Alternative sequence	85 – 264	180	VRDFN…ALDDA → NFQVLSQRHLVRDYGRDRHF GTQCLSIQIVTSPGSLGGSW RVMQEVNPPNQHQTGAPRGH FIGLMMYGLWTPILEPERTM ILIPRFPRRVLARFYSPSPN PISRASL in isoform 6.		VSP_038544
	Alternative sequence	105	1	P → PANTCHLSA in isoform 2.		VSP_038537
	Alternative sequence	106 – 124	19	ELPGP…REGQT → GVWLSLRGNLWFLVGWWVK in isoform 4.		VSP_038538
	Alternative sequence	125 – 279	155	Missing in isoform 4.		VSP_038539
	Alternative sequence	265 – 279	15	Missing in isoform 6.		VSP_038545
	Natural variant	49	1	P → S: dbSNP rs11556344.		VAR_062258
	Natural variant	141	1	F → L in SCN3; mild form.		VAR_062259
	Natural variant	151	1	S → G: dbSNP rs17851425. Ref.7		VAR_062260
	Natural variant	278	1	S → P: dbSNP rs1804715.		VAR_062261
Experimental info
	Sequence conflict	25	1	G → V in BAG62359. Ref.3
	Sequence conflict	45	1	G → R in AAB51196. Ref.1
	Sequence conflict	201	1	Q → T in AAB51196. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 87EEF0C46857704B	FASTA	279	31,621
	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
	Isoform 2. Checksum: 762F6F8897C11AB9	FASTA	287	32,418
	10 20 30 40 50 60 MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE 70 80 90 100 110 120 FGFGFSFSPG GGIRFHDNFG FDDLVRDFNS IFSDMGAWTL PSHPPANTCH LSAELPGPES 130 140 150 160 170 180 ETPGERLREG QTLRDSMLKY PDSHQPRIFG GVLESDARSE SPQPAPDWGS QRPFHRFDDV 190 200 210 220 230 240 WPMDPHPRTR EDNDLDSQVS QEGLGPVLQP QPKSYFKSIS VTKITKPDGI VEERRTVVDS 250 260 270 280 EGRTETTVTR HEADSSPRGD PESPRPPALD DAFSILDLFL GRWFRSR
	Isoform 3. Checksum: A7F85EF8A7E6E0AB	FASTA	253	28,646
	10 20 30 40 50 60 MTRDEDDDEE EEEEGGSWGR GNPRFHSPQH PPEEFGFGFS FSPGGGIRFH DNFGFDDLVR 70 80 90 100 110 120 DFNSIFSDMG AWTLPSHPPE LPGPESETPG ERLREGQTLR DSMLKYPDSH QPRIFGGVLE 130 140 150 160 170 180 SDARSESPQP APDWGSQRPF HRFDDVWPMD PHPRTREDND LDSQVSQEGL GPVLQPQPKS 190 200 210 220 230 240 YFKSISVTKI TKPDGIVEER RTVVDSEGRT ETTVTRHEAD SSPRGDPESP RPPALDDAFS 250 ILDLFLGRWF RSR
	Isoform 4. Checksum: B59B40DC8DF641E3	FASTA	124	14,235
	10 20 30 40 50 60 MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE 70 80 90 100 110 120 FGFGFSFSPG GGIRFHDNFG FDDLVRDFNS IFSDMGAWTL PSHPPGVWLS LRGNLWFLVG WWVK
	Isoform 5. Checksum: 25EF194EC019C474	FASTA	231	26,100
	10 20 30 40 50 60 MSLFDLFRGF FGFPGPRSFS PGGGIRFHDN FGFDDLVRDF NSIFSDMGAW TLPSHPPELP 70 80 90 100 110 120 GPESETPGER LREGQTLRDS MLKYPDSHQP RIFGGVLESD ARSESPQPAP DWGSQRPFHR 130 140 150 160 170 180 FDDVWPMDPH PRTREDNDLD SQVSQEGLGP VLQPQPKSYF KSISVTKITK PDGIVEERRT 190 200 210 220 230 VVDSEGRTET TVTRHEADSS PRGDPESPRP PALDDAFSIL DLFLGRWFRS R
	Isoform 6. Checksum: E9D736737D3F978F	FASTA	191	21,801
	10 20 30 40 50 60 MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE 70 80 90 100 110 120 FGFGFSFSPG GGIRFHDNFG FDDLNFQVLS QRHLVRDYGR DRHFGTQCLS IQIVTSPGSL 130 140 150 160 170 180 GGSWRVMQEV NPPNQHQTGA PRGHFIGLMM YGLWTPILEP ERTMILIPRF PRRVLARFYS 190 PSPNPISRAS L

References

	« Hide 'large scale' referencesShow '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: 9058808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HSCL1, 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: 18472110] [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. , 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; 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. , 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: 16710414] [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. , 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: 15489334] [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, 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: 10760273] [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: 15339924] [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: 16857965] [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: 17545607] [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: 17241641] [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: 17187068] [Abstract] Cited for: INVOLVEMENT IN SCN3.
[15]	"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: 18319618] [Abstract] Cited for: CLEAVAGE SITE, FUNCTION.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 18971376] [Abstract] Cited for: INTERACTION WITH ATP2A2 AND PLN, FUNCTION, SUBCELLULAR LOCATION.
[18]	"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: 19796188] [Abstract] Cited for: VARIANT SCN3 LEU-141.
+	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.
IPI	IPI00010440. IPI00604587. IPI00641973. IPI00878396. IPI00954512. IPI00954523.
RefSeq	NP_001018238.1. NP_006109.2.
UniGene	Hs.199625
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O00165. 10 interactions.
STRING	O00165.
Proteomic databases
PRIDE	O00165.
Genome annotation databases
Ensembl	ENST00000328703; ENSP00000329002; ENSG00000143575; Homo sapiens. [Genome view] ENST00000447768; ENSP00000403848; ENSG00000143575; Homo sapiens. [Genome view]
GeneID	10456.
KEGG	hsa:10456.
UCSC	uc001fes.1. human.
Organism-specific databases
CTD	10456.
GeneCards	GC01P152512.
H-InvDB	HIX0001103.
HGNC	HGNC:16915. HAX1.
MIM	605998. gene. 610738. phenotype.
Orphanet	99749. Kostmann syndrome.
PharmGKB	PA142671700.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12670.
HOVERGEN	HBG002991.
InParanoid	O00165.
PhylomeDB	O00165.
Gene expression databases
ArrayExpress	O00165.
Bgee	O00165.
CleanEx	HS_HAX1.
Genevestigator	O00165.
GermOnline	ENSG00000143575. Homo sapiens.
Family and domain databases
InterPro	IPR017248. HS1--assoc_X-1. [Graphical view]
PIRSF	PIRSF037634. HS1-associating_X-1. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	39639.
PMAP-CutDB	O00165.
SOURCE	Search...

Entry information

Entry name

HAX1_HUMAN

Accession

Primary (citable) accession number: O00165
Secondary accession number(s): A8W4W9 , A8W4X0, B4DUJ7, Q5VYD5, Q5VYD7, Q96AU4, Q9BS80

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2002
Last modified:	March 2, 2010
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.