HEH2_YEAST
ID HEH2_YEAST Reviewed; 663 AA.
AC Q03281; D6VT82;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Inner nuclear membrane protein HEH2;
DE AltName: Full=Helix-extension-helix domain-containing protein 2;
GN Name=HEH2; OrderedLocusNames=YDR458C; ORFNames=D8035.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP GENE NAME, SUBCELLULAR LOCATION, INTERACTION WITH SRP1, AND MUTAGENESIS OF
RP 1-MET--PRO-52; 1-MET--SER-133; 124-PRO--LYS-137; LYS-126 AND
RP 309-ILE--GLU-663.
RX PubMed=16929305; DOI=10.1038/nature05075;
RA King M.C., Lusk C.P., Blobel G.;
RT "Karyopherin-mediated import of integral inner nuclear membrane proteins.";
RL Nature 442:1003-1007(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- SUBUNIT: Interacts with SRP1. {ECO:0000269|PubMed:16929305}.
CC -!- INTERACTION:
CC Q03281; P39929: SNF7; NbExp=3; IntAct=EBI-22131, EBI-17554;
CC Q03281; Q02821: SRP1; NbExp=7; IntAct=EBI-22131, EBI-1797;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16929305}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16929305}. Note=Targeting to the inner nuclear
CC membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
CC -!- MISCELLANEOUS: Present with 1250 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U33050; AAB64934.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12292.1; -; Genomic_DNA.
DR PIR; S69626; S69626.
DR RefSeq; NP_010746.1; NM_001180766.1.
DR PDB; 4PVZ; X-ray; 2.50 A; C/D=100-137.
DR PDBsum; 4PVZ; -.
DR AlphaFoldDB; Q03281; -.
DR SASBDB; Q03281; -.
DR SMR; Q03281; -.
DR BioGRID; 32512; 68.
DR DIP; DIP-7259N; -.
DR IntAct; Q03281; 6.
DR STRING; 4932.YDR458C; -.
DR iPTMnet; Q03281; -.
DR MaxQB; Q03281; -.
DR PaxDb; Q03281; -.
DR PRIDE; Q03281; -.
DR EnsemblFungi; YDR458C_mRNA; YDR458C; YDR458C.
DR GeneID; 852069; -.
DR KEGG; sce:YDR458C; -.
DR SGD; S000002866; HEH2.
DR VEuPathDB; FungiDB:YDR458C; -.
DR eggNOG; ENOG502QVG5; Eukaryota.
DR GeneTree; ENSGT00940000171142; -.
DR HOGENOM; CLU_010838_2_0_1; -.
DR InParanoid; Q03281; -.
DR OMA; HAFCYPN; -.
DR BioCyc; YEAST:G3O-29986-MON; -.
DR PRO; PR:Q03281; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03281; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR DisProt; DP02124; -.
DR Gene3D; 1.10.10.1180; -; 1.
DR Gene3D; 1.10.720.40; -; 1.
DR IDEAL; IID50288; -.
DR InterPro; IPR025856; HeH/LEM_domain.
DR InterPro; IPR044780; Heh2/Src1.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR041885; MAN1_winged_helix_dom.
DR InterPro; IPR018996; MSC.
DR PANTHER; PTHR47808; PTHR47808; 1.
DR Pfam; PF12949; HeH; 1.
DR Pfam; PF09402; MSC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..663
FT /note="Inner nuclear membrane protein HEH2"
FT /id="PRO_0000202596"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 46..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 124..137
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 1..133
FT /note="Missing: No interaction with SRP1; when associated
FT with missing 309-I--E-663."
FT /evidence="ECO:0000269|PubMed:16929305"
FT MUTAGEN 1..52
FT /note="Missing: Interaction with SRP1; when associated with
FT missing 309-I--E-663."
FT /evidence="ECO:0000269|PubMed:16929305"
FT MUTAGEN 124..137
FT /note="Missing: No interaction with SRP1; when associated
FT with missing 309-I--E-663. Mislocalized to the endoplasmic
FT reticulum."
FT /evidence="ECO:0000269|PubMed:16929305"
FT MUTAGEN 126
FT /note="K->T: Mislocalized to the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:16929305"
FT MUTAGEN 309..663
FT /note="Missing: Interaction with SRP1."
FT /evidence="ECO:0000269|PubMed:16929305"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:4PVZ"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:4PVZ"
SQ SEQUENCE 663 AA; 76377 MW; 1E11821F2542723E CRC64;
MDHRNLDPKT LKVSQLRRVL VENDVAFPAN ARKPVLVKLF EEKVRQRLQS SPEASKVRTS
IQKVVKSGAK NADRKKTLKS KKLESSSSES KTVKDENVET NKRKREQIST DNEAKMQIQE
EKSPKKKRKK RSSKANKPPE SPPQSKSDGK ATSADLTSEL ETVEELHKKD SSDDKPRVKE
LPKPELPNLK VSNEFLAQLN KELASAATEN YDHSIKSTDL SSIRIETEEP VGPSTGAETR
NESEVMENIN LEVQPEVKEA KEELTKISET FDNQDEEDTS RLSSKKNIRS PKGRTRHFIA
NKTKRGIDIM KPFIAHLFIW LWNGAIFLSI ICPILFGLWY REQRIQVGYC GHEKPLKSLA
ISAFPQTERV DSVLQAYRPN CLECPEHGIC SSFMNVECEP GYEPKSSILE TYGIIPFPKY
CAKDESKEKE VDELVWKVNE YLKKKNAQHE CGEGENLFES GETETKLYDI FSHSRPSWES
QREFNDHWKN VLEILKKKDD IIWLPLDFET NGKREKSKSN NTNYIYRSTS KKWVTLQCHL
EGDIQEYITK YGGSLFITLG VLFLIKKIQS TLDNYVQGEQ IIEKLVKEAI DKLKDVKKNK
GEEPFLTTVQ LRATLLSDIP NIKEQNNLWA QTKEKIMKEQ SENIELYLLE ENGEIMTCWE
WKE
