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   24-JAN-2024, entry version 172.
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; 61.
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; 9606-ENSP00000218008; -.
DR   PeptideAtlas; Q9UN42; -.
DR   ProteomicsDB; 85249; -. [Q9UN42-1]
DR   ProteomicsDB; 85250; -. [Q9UN42-2]
DR   Antibodypedia; 44620; 53 antibodies from 14 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   AGR; HGNC:808; -.
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; KNIRCTH; -.
DR   OrthoDB; 2880589at2759; -.
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 769 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 cell types or tissues.
DR   ExpressionAtlas; Q9UN42; baseline and differential.
DR   GO; GO:0005635; C:nuclear envelope; TAS:Reactome.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
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 DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   Gene3D; 2.60.40.1660; Na, k-atpase alpha subunit; 1.
DR   InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR   InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR   NCBIfam; TIGR01107; Na_K_ATPase_bet; 1.
DR   PANTHER; PTHR11523:SF12; PROTEIN ATP1B4; 1.
DR   PANTHER; PTHR11523; SODIUM/POTASSIUM-DEPENDENT ATPASE BETA SUBUNIT; 1.
DR   Pfam; PF00287; Na_K-ATPase; 1.
DR   PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR   PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
DR   Genevisible; Q9UN42; HS.
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
//