CPLM-000014

Genbank Nucleotide ID

HCLS1-associated protein X-1

Protein Synonyms/Alias

HS1-associating protein X-1; HAX-1; HS1-binding protein 1; HSP1BP-1

Homo sapiens (Human)

Position	Peptide	Type	References
131	TLRDSMLKYPDSHQP	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8]
205	PVLQPQPKSYFKSIS	ubiquitination	[2]
209	PQPKSYFKSISVTKI	ubiquitination	[2]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]

Functional Description

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.

REGION 2 41 Required for localization in mitochondria
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
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.
MOD_RES 2 2 N-acetylserine.

Acetylation; Alternative splicing; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Disease mutation; Endoplasmic reticulum; Membrane; Mitochondrion; Nucleus; Polymorphism; Reference proteome; Sarcoplasmic reticulum.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0015629; C:actin cytoskeleton; ISS:BHF-UCL.
GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
GO:0030027; C:lamellipodium; ISS:BHF-UCL.
GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0005635; C:nuclear envelope; TAS:ProtInc.
GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO:0019966; F:interleukin-1 binding; IDA:UniProtKB.
GO:0047485; F:protein N-terminus binding; IDA:UniProtKB.
GO:0071345; P:cellular response to cytokine stimulus; IMP:BHF-UCL.
GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:BHF-UCL.
GO:0030854; P:positive regulation of granulocyte differentiation; IMP:BHF-UCL.
GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; IMP:BHF-UCL.
GO:0051897; P:positive regulation of protein kinase B signaling cascade; IMP:BHF-UCL.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO:0030833; P:regulation of actin filament polymerization; IMP:BHF-UCL.

IPR017248; HS1--assoc_X-1.