Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

HCLS1-associated protein X-1

Gene

Hax1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
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 namesi
Name:Hax1
Synonyms:Hs1bp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1346319. Hax1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: BHF-UCL
  • lamellipodium Source: BHF-UCL
  • mitochondrial intermembrane space Source: MGI
  • mitochondrial outer membrane Source: MGI
  • mitochondrion Source: MGI
  • nuclear membrane Source: UniProtKB-SubCell
  • sarcoplasmic reticulum Source: CACAO
  • transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus, Sarcoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mice lacking Hax1 fail to survive longer than 14 weeks, due to a loss of motor coordination and activity, leading to failure to eat and drink. They display extensive apoptosis of neurons in the striatum and cerebellum, and a loss of lymphocytes in spleen, bone marrow and thymus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 280279HCLS1-associated protein X-1PRO_0000083907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei128 – 1292Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO35387.
MaxQBiO35387.
PaxDbiO35387.
PRIDEiO35387.

PTM databases

iPTMnetiO35387.
PhosphoSiteiO35387.

Expressioni

Tissue specificityi

Ubiquitous, with highest levels in kidney and liver (at protein level).1 Publication

Gene expression databases

BgeeiO35387.
CleanExiMM_HAX1.
ExpressionAtlasiO35387. baseline.
GenevisibleiO35387. MM.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Arrb1Q8BWG86EBI-642449,EBI-641778
PKD2Q135633EBI-642449,EBI-7813714From a different organism.
Stat3P4222711EBI-642449,EBI-602878

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204783. 15 interactions.
DIPiDIP-49445N.
IntActiO35387. 19 interactions.
MINTiMINT-1592061.
STRINGi10090.ENSMUSP00000078661.

Structurei

3D structure databases

ProteinModelPortaliO35387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 4544Required for localization in mitochondriaBy similarityAdd
BLAST
Regioni115 – 280166Involved in HCLS1 bindingBy similarityAdd
BLAST
Regioni176 – 20732Involved in CASP9 bindingBy similarityAdd
BLAST
Regioni177 – 24872Involved in GNA13 bindingBy similarityAdd
BLAST
Regioni184 – 28097Required for localization in sarcoplasmic reticulumBy similarityAdd
BLAST
Regioni185 – 28096Involved in PKD2 bindingAdd
BLAST
Regioni204 – 24643Involved in ATP2A2 bindingBy similarityAdd
BLAST
Regioni204 – 22623Involved in PLN bindingBy similarityAdd
BLAST
Regioni271 – 28010Required for ITGB6 bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi30 – 4415Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the HAX1 family.Curated

Phylogenomic databases

eggNOGiENOG410IJQ0. Eukaryota.
ENOG411211U. LUCA.
GeneTreeiENSGT00390000018324.
HOGENOMiHOG000090247.
HOVERGENiHBG002991.
InParanoidiO35387.
KOiK16220.
OMAiPKPAPDW.
OrthoDBiEOG7HTHJ5.
PhylomeDBiO35387.
TreeFamiTF328619.

Family and domain databases

InterProiIPR017248. HAX-1.
[Graphical view]
PIRSFiPIRSF037634. HS1-associating_X-1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVFDLFRGF FGFPGPRSHR DPFFGGMTRD DDDDDDDDDE AEEDRGAWGR
60 70 80 90 100
ESYAFDGSQP PEEFGFSFSP RGGMRFHGNF GFDDLVRDFN SIFSEMGAWT
110 120 130 140 150
LPSHSPELPG PESETPGERL REGQTLRDSM LKYPDSHQPR IFEGVLESHA
160 170 180 190 200
KPESPKPAPD WGSQGPFHRL DDTWPVSPHS RAKEDKDLDS QVSQEGLGPL
210 220 230 240 250
LQPQPKSYFK SISVTKITKP DGTVEERRTV VDSEGRRETT VTHQEAHDSS
260 270 280
RSDPDSQRSS ALDDPFSILD LLLGRWFRSR
Length:280
Mass (Da):31,654
Last modified:January 1, 1998 - v1
Checksum:i3123979BA10B45D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023482 mRNA. Translation: AAB81081.1.
AK002256 mRNA. Translation: BAB21969.1.
AK010633 mRNA. Translation: BAB27077.1.
AK088746 mRNA. Translation: BAC40544.1.
BC006688 mRNA. Translation: AAH06688.1.
BC098225 mRNA. Translation: AAH98225.1.
CCDSiCCDS17519.1.
RefSeqiNP_035956.1. NM_011826.4.
UniGeneiMm.256035.
Mm.416677.

Genome annotation databases

EnsembliENSMUST00000079724; ENSMUSP00000078661; ENSMUSG00000027944.
GeneIDi23897.
KEGGimmu:23897.
UCSCiuc008qaj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF023482 mRNA. Translation: AAB81081.1.
AK002256 mRNA. Translation: BAB21969.1.
AK010633 mRNA. Translation: BAB27077.1.
AK088746 mRNA. Translation: BAC40544.1.
BC006688 mRNA. Translation: AAH06688.1.
BC098225 mRNA. Translation: AAH98225.1.
CCDSiCCDS17519.1.
RefSeqiNP_035956.1. NM_011826.4.
UniGeneiMm.256035.
Mm.416677.

3D structure databases

ProteinModelPortaliO35387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204783. 15 interactions.
DIPiDIP-49445N.
IntActiO35387. 19 interactions.
MINTiMINT-1592061.
STRINGi10090.ENSMUSP00000078661.

PTM databases

iPTMnetiO35387.
PhosphoSiteiO35387.

Proteomic databases

EPDiO35387.
MaxQBiO35387.
PaxDbiO35387.
PRIDEiO35387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079724; ENSMUSP00000078661; ENSMUSG00000027944.
GeneIDi23897.
KEGGimmu:23897.
UCSCiuc008qaj.2. mouse.

Organism-specific databases

CTDi10456.
MGIiMGI:1346319. Hax1.

Phylogenomic databases

eggNOGiENOG410IJQ0. Eukaryota.
ENOG411211U. LUCA.
GeneTreeiENSGT00390000018324.
HOGENOMiHOG000090247.
HOVERGENiHBG002991.
InParanoidiO35387.
KOiK16220.
OMAiPKPAPDW.
OrthoDBiEOG7HTHJ5.
PhylomeDBiO35387.
TreeFamiTF328619.

Miscellaneous databases

PROiO35387.
SOURCEiSearch...

Gene expression databases

BgeeiO35387.
CleanExiMM_HAX1.
ExpressionAtlasiO35387. baseline.
GenevisibleiO35387. MM.

Family and domain databases

InterProiIPR017248. HAX-1.
[Graphical view]
PIRSFiPIRSF037634. HS1-associating_X-1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse HAX-1 short form (HAX-1s)."
    Watanabe T., Takeshita H.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Kidney and Thymus.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "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 AND CTTN, SUBCELLULAR LOCATION.
  5. "Expression and tissue distribution of mouse Hax1."
    Hippe A., Bylaite M., Chen M., von Mikecz A., Wolf R., Ruzicka T., Walz M.
    Gene 379:116-126(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons."
    Chao J.R., Parganas E., Boyd K., Hong C.Y., Opferman J.T., Ihle J.N.
    Nature 452:98-102(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver and Spleen.

Entry informationi

Entry nameiHAX1_MOUSE
AccessioniPrimary (citable) accession number: O35387
Secondary accession number(s): Q542F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.