AT1B4_HUMAN
ID AT1B4_HUMAN Reviewed; 357 AA.
AC Q9UN42; Q17RR0; Q9UN41;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein ATP1B4;
DE AltName: Full=X,K-ATPase subunit beta-m;
DE AltName: Full=X/potassium-transporting ATPase subunit beta-m;
GN Name=ATP1B4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=10456317; DOI=10.1016/s0014-5793(99)00954-0;
RA Pestov N.B., Adams G., Shakhparonov M.I., Modyanov N.N.;
RT "Identification of a novel gene of the X,K-ATPase beta-subunit family that
RT is predominantly expressed in skeletal and heart muscles.";
RL FEBS Lett. 456:243-248(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=14656723; DOI=10.1152/ajpcell.00358.2003;
RA Zhao H., Pestov N.B., Korneenko T.V., Shakhparonov M.I., Modyanov N.N.;
RT "Accumulation of beta (m), a structural member of X,K-ATPase beta-subunit
RT family, in nuclear envelopes of perinatal myocytes.";
RL Am. J. Physiol. 286:C757-C767(2004).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17592128; DOI=10.1073/pnas.0704809104;
RA Pestov N.B., Ahmad N., Korneenko T.V., Zhao H., Radkov R., Schaer D.,
RA Roy S., Bibert S., Geering K., Modyanov N.N.;
RT "Evolution of Na,K-ATPase betam-subunit into a coregulator of transcription
RT in placental mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11215-11220(2007).
CC -!- FUNCTION: May act as a transcriptional coregulator during muscle
CC development through its interaction with SNW1. Has lost its ancestral
CC function as a Na,K-ATPase beta-subunit. {ECO:0000269|PubMed:17592128}.
CC -!- SUBUNIT: Associates with a SMAD7-transcriptional complex. Interacts
CC with SNW1 and TOR1AIP1 (By similarity). According to PubMed:17592128,
CC does not associate with known Na,K-ATPase alpha-subunits.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UN42; P07306: ASGR1; NbExp=3; IntAct=EBI-12894731, EBI-1172335;
CC Q9UN42; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-12894731, EBI-10267100;
CC Q9UN42; Q07325: CXCL9; NbExp=3; IntAct=EBI-12894731, EBI-3911467;
CC Q9UN42; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-12894731, EBI-10976398;
CC Q9UN42; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-12894731, EBI-741850;
CC Q9UN42; O60636: TSPAN2; NbExp=3; IntAct=EBI-12894731, EBI-3914288;
CC Q9UN42; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-12894731, EBI-10243654;
CC Q9UN42; Q9CSN1: Snw1; Xeno; NbExp=2; IntAct=EBI-12894731, EBI-2551848;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}. Note=Detected in nuclear
CC envelops. {ECO:0000269|PubMed:14656723, ECO:0000269|PubMed:17592128}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9UN42-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9UN42-2; Sequence=VSP_000351;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and at a lower
CC level in heart. {ECO:0000269|PubMed:10456317}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; AF158383; AAD49692.1; -; mRNA.
DR EMBL; AF158384; AAD49693.1; -; mRNA.
DR EMBL; BC117227; AAI17228.1; -; mRNA.
DR CCDS; CCDS14598.1; -. [Q9UN42-2]
DR CCDS; CCDS48158.1; -. [Q9UN42-1]
DR RefSeq; NP_001135919.1; NM_001142447.2. [Q9UN42-1]
DR RefSeq; NP_036201.1; NM_012069.4. [Q9UN42-2]
DR AlphaFoldDB; Q9UN42; -.
DR SMR; Q9UN42; -.
DR BioGRID; 117007; 60.
DR DIP; DIP-60961N; -.
DR IntAct; Q9UN42; 26.
DR STRING; 9606.ENSP00000218008; -.
DR iPTMnet; Q9UN42; -.
DR PhosphoSitePlus; Q9UN42; -.
DR BioMuta; ATP1B4; -.
DR DMDM; 17367154; -.
DR jPOST; Q9UN42; -.
DR MassIVE; Q9UN42; -.
DR PaxDb; Q9UN42; -.
DR PeptideAtlas; Q9UN42; -.
DR PRIDE; Q9UN42; -.
DR ProteomicsDB; 85249; -. [Q9UN42-1]
DR ProteomicsDB; 85250; -. [Q9UN42-2]
DR Antibodypedia; 44620; 48 antibodies from 13 providers.
DR DNASU; 23439; -.
DR Ensembl; ENST00000218008.8; ENSP00000218008.3; ENSG00000101892.12. [Q9UN42-1]
DR Ensembl; ENST00000361319.3; ENSP00000355346.3; ENSG00000101892.12. [Q9UN42-2]
DR GeneID; 23439; -.
DR KEGG; hsa:23439; -.
DR MANE-Select; ENST00000218008.8; ENSP00000218008.3; NM_001142447.3; NP_001135919.1.
DR UCSC; uc004esq.4; human. [Q9UN42-1]
DR CTD; 23439; -.
DR DisGeNET; 23439; -.
DR GeneCards; ATP1B4; -.
DR HGNC; HGNC:808; ATP1B4.
DR HPA; ENSG00000101892; Group enriched (skeletal muscle, tongue).
DR MIM; 301073; gene.
DR neXtProt; NX_Q9UN42; -.
DR OpenTargets; ENSG00000101892; -.
DR PharmGKB; PA410; -.
DR VEuPathDB; HostDB:ENSG00000101892; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_0_1; -.
DR InParanoid; Q9UN42; -.
DR OMA; GVQYDTH; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; Q9UN42; -.
DR TreeFam; TF314618; -.
DR PathwayCommons; Q9UN42; -.
DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR SignaLink; Q9UN42; -.
DR BioGRID-ORCS; 23439; 12 hits in 695 CRISPR screens.
DR GenomeRNAi; 23439; -.
DR Pharos; Q9UN42; Tdark.
DR PRO; PR:Q9UN42; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UN42; protein.
DR Bgee; ENSG00000101892; Expressed in skeletal muscle tissue of rectus abdominis and 49 other tissues.
DR ExpressionAtlas; Q9UN42; baseline and differential.
DR Genevisible; Q9UN42; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IEA:InterPro.
DR GO; GO:0022890; F:inorganic cation transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Nucleus; Reference proteome; Signal-anchor;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..357
FT /note="Protein ATP1B4"
FT /id="PRO_0000219122"
FT TOPO_DOM 1..110
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..357
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 15..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..72
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 107..110
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10456317"
FT /id="VSP_000351"
FT VARIANT 48
FT /note="V -> A (in dbSNP:rs2072452)"
FT /id="VAR_055535"
SQ SEQUENCE 357 AA; 41598 MW; 94926EB1BB637ACA CRC64;
MRRQLRSRRA PSFPYSYRYR LDDPDEANQN YLADEEEEAE EEARVTVVPK SEEEEEEEEK
EEEEEEEKEE EEGQGQPTGN AWWQKLQIMS EYLWDPERRM FLARTGQSWS LILLIYFFFY
ASLAAVITLC MYTLFLTISP YIPTFTERVK PPGVMIRPFA HSLNFNFNVS EPDTWQHYVI
SLNGFLQGYN DSLQEEMNVD CPPGQYFIQD GNEDEDKKAC QFKRSFLKNC SGLEDPTFGY
STGQPCILLK MNRIVGFRPE LGDPVKVSCK VQRGDENDIR SISYYPESAS FDLRYYPYYG
KLTHVNYTSP LVAMHFTDVV KNQAVPVQCQ LKGKGVINDV INDRFVGRVI FTLNIET
