LOCUS       NP_060204                551 aa            linear   PRI 06-JUN-2024
DEFINITION  palmdelphin [Homo sapiens].
ACCESSION   NP_060204
VERSION     NP_060204.1
DBSOURCE    REFSEQ: accession NM_017734.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Su,Y., Du,Y., Ye,S., Jia,G., Ding,B. and Yu,J.
  TITLE     Clinical importance and PI3K/Akt pathway-dependent
            anti-proliferative role of PALMD and DPT in breast cancer
  JOURNAL   Pathol Res Pract 249, 154717 (2023)
   PUBMED   37556876
  REMARK    GeneRIF: Clinical importance and PI3K/Akt pathway-dependent
            anti-proliferative role of PALMD and DPT in breast cancer.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Wang,S., Yu,H., Gao,J., Chen,J., He,P., Zhong,H., Tan,X.,
            Staines,K.A., Macrae,V.E., Fu,X., Jiang,L. and Zhu,D.
  TITLE     PALMD regulates aortic valve calcification via altered glycolysis
            and NF-kappaB-mediated inflammation
  JOURNAL   J Biol Chem 298 (5), 101887 (2022)
   PUBMED   35367413
  REMARK    GeneRIF: PALMD regulates aortic valve calcification via altered
            glycolysis and NF-kappaB-mediated inflammation.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Sainz-Jaspeado,M., Smith,R.O., Plunde,O., Pawelzik,S.C., Jin,Y.,
            Nordling,S., Ding,Y., Aspenstrom,P., Hedlund,M., Bastianello,G.,
            Ascione,F., Li,Q., Demir,C.S., Fernando,D., Daniel,G.,
            Franco-Cereceda,A., Kroon,J., Foiani,M., Petrova,T.V.,
            Kilimann,M.W., Back,M. and Claesson-Welsh,L.
  TITLE     Palmdelphin Regulates Nuclear Resilience to Mechanical Stress in
            the Endothelium
  JOURNAL   Circulation 144 (20), 1629-1645 (2021)
   PUBMED   34636652
  REMARK    GeneRIF: Palmdelphin Regulates Nuclear Resilience to Mechanical
            Stress in the Endothelium.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Li,Z., Gaudreault,N., Arsenault,B.J., Mathieu,P., Bosse,Y. and
            Theriault,S.
  TITLE     Phenome-wide analyses establish a specific association between
            aortic valve PALMD expression and calcific aortic valve stenosis
  JOURNAL   Commun Biol 3 (1), 477 (2020)
   PUBMED   32859967
  REMARK    GeneRIF: Phenome-wide analyses establish a specific association
            between aortic valve PALMD expression and calcific aortic valve
            stenosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Dashzeveg,N., Taira,N., Lu,Z.G., Kimura,J. and Yoshida,K.
  TITLE     Palmdelphin, a novel target of p53 with Ser46 phosphorylation,
            controls cell death in response to DNA damage
  JOURNAL   Cell Death Dis 5 (5), e1221 (2014)
   PUBMED   24810057
  REMARK    GeneRIF: findings define palmdelphin as a target of
            serine-46-phosphorylated p53 that controls cell death in response
            to DNA damage.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Vasan,R.S., Glazer,N.L., Felix,J.F., Lieb,W., Wild,P.S.,
            Felix,S.B., Watzinger,N., Larson,M.G., Smith,N.L., Dehghan,A.,
            Grosshennig,A., Schillert,A., Teumer,A., Schmidt,R., Kathiresan,S.,
            Lumley,T., Aulchenko,Y.S., Konig,I.R., Zeller,T., Homuth,G.,
            Struchalin,M., Aragam,J., Bis,J.C., Rivadeneira,F., Erdmann,J.,
            Schnabel,R.B., Dorr,M., Zweiker,R., Lind,L., Rodeheffer,R.J.,
            Greiser,K.H., Levy,D., Haritunians,T., Deckers,J.W., Stritzke,J.,
            Lackner,K.J., Volker,U., Ingelsson,E., Kullo,I., Haerting,J.,
            O'Donnell,C.J., Heckbert,S.R., Stricker,B.H., Ziegler,A.,
            Reffelmann,T., Redfield,M.M., Werdan,K., Mitchell,G.F., Rice,K.,
            Arnett,D.K., Hofman,A., Gottdiener,J.S., Uitterlinden,A.G.,
            Meitinger,T., Blettner,M., Friedrich,N., Wang,T.J., Psaty,B.M., van
            Duijn,C.M., Wichmann,H.E., Munzel,T.F., Kroemer,H.K.,
            Benjamin,E.J., Rotter,J.I., Witteman,J.C., Schunkert,H.,
            Schmidt,H., Volzke,H. and Blankenberg,S.
  TITLE     Genetic variants associated with cardiac structure and function: a
            meta-analysis and replication of genome-wide association data
  JOURNAL   JAMA 302 (2), 168-178 (2009)
   PUBMED   19584346
  REMARK    GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Andreu,N., Escarceller,M., Feather,S., Devriendt,K., Wolf,A.S.,
            Estivill,X. and Sumoy,L.
  TITLE     PALML, a novel paralemmin-related gene mapping on human chromosome
            1p21
  JOURNAL   Gene 278 (1-2), 33-40 (2001)
   PUBMED   11707320
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Hu,B., Copeland,N.G., Gilbert,D.J., Jenkins,N.A. and Kilimann,M.W.
  TITLE     The paralemmin protein family: identification of paralemmin-2, an
            isoform differentially spliced to AKAP2/AKAP-KL, and of
            palmdelphin, a more distant cytosolic relative
  JOURNAL   Biochem Biophys Res Commun 285 (5), 1369-1376 (2001)
   PUBMED   11478809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF262379.1 and AL390970.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000278.1, AF262379.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263174.9/ ENSP00000263174.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..551
                     /product="palmdelphin"
                     /note="paralemnin-like protein; paralemmin-like protein"
                     /calculated_mol_wt=62627
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          17..447
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cl46503"
                     /db_xref="CDD:480843"
     Region          78..>204
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          248..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHU2; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          342..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHU2; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHU2; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Region          449..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NP74.1)"
     CDS             1..551
                     /gene="PALMD"
                     /gene_synonym="C1orf11; PALML"
                     /coded_by="NM_017734.5:206..1861"
                     /db_xref="CCDS:CCDS758.1"
                     /db_xref="GeneID:54873"
                     /db_xref="HGNC:HGNC:15846"
                     /db_xref="MIM:610182"
ORIGIN      
        1 meeaelvkgr lqaitdkrki qeeisqkrlk ieedklkhqh lkkkalrekw lldgissgke
       61 qeemkkqnqq dqhqiqvleq silrlekeiq dlekaelqis tkeeailkkl ksierttedi
      121 irsvkveree raeesiediy anipdlpksy ipsrlrkein eekeddeqnr kalyameikv
      181 ekdlktgest vlssiplpsd dfkgtgikvy ddgqksvyav ssnhsaayng tdglapveve
      241 ellrqasern skspteyhep vyanpfyrpt tpqretvtpg pnfqerikik tnglgigvne
      301 sihnmgngls eergnnfnhi spippvphpr sviqqaeekl htpqkrlmtp weesnvmqdk
      361 dapspkprls pretifgkse hqnssptcqe deedvryniv hslppdindt epvtmifmgy
      421 qqaedseedk kfltgydgii haelvvidde eeedegeaek psyhpiaphs qvyqpakptp
      481 lprkrseasp hentnhksph knsislkeqe eslgspvhhs pfdaqttgdg tedpsltalr
      541 mrmaklgkkv i
//
