ID   SRC1_YEAST              Reviewed;         834 AA.
AC   Q03707; D6VZE1; Q03712;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Inner nuclear membrane protein SRC1;
DE   AltName: Full=Helix-extension-helix domain-containing protein 1;
GN   Name=SRC1; Synonyms=HEH1; OrderedLocusNames=YML034W; ORFNames=YML033W;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   FUNCTION, AND IDENTIFICATION OF INTRON.
RX   PubMed=11754482; DOI=10.1002/yea.803;
RA   Rodriguez-Navarro S., Igual J.C., Perez-Ortin J.E.;
RT   "SRC1: an intron-containing yeast gene involved in sister chromatid
RT   segregation.";
RL   Yeast 19:43-54(2002).
RN   [4]
RP   SUBCELLULAR LOCATION.
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-85; SER-204 AND
RP   SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; THR-394 AND SER-427, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80; SER-85; SER-181;
RP   SER-203; SER-204; SER-206 AND THR-394, AND IDENTIFICATION BY MASS
RP   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).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Plays a role in sister chromatid separation.
CC       {ECO:0000269|PubMed:11754482}.
CC   -!- INTERACTION:
CC       Q03707; Q02821: SRP1; NbExp=5; IntAct=EBI-18064, EBI-1797;
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000269|PubMed:16929305}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16929305}. Note=Targeting to the inner nuclear
CC       membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA86621.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA86622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z46659; CAA86621.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Z46659; CAA86622.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006946; DAA09865.1; -; Genomic_DNA.
DR   PIR; S49746; S49746.
DR   RefSeq; NP_013679.1; NM_001182391.1.
DR   PDB; 4XZR; X-ray; 2.25 A; A=170-223.
DR   PDBsum; 4XZR; -.
DR   AlphaFoldDB; Q03707; -.
DR   SMR; Q03707; -.
DR   BioGRID; 35136; 275.
DR   DIP; DIP-4546N; -.
DR   IntAct; Q03707; 11.
DR   MINT; Q03707; -.
DR   STRING; 4932.YML034W; -.
DR   iPTMnet; Q03707; -.
DR   MaxQB; Q03707; -.
DR   PaxDb; 4932-YML034W; -.
DR   PeptideAtlas; Q03707; -.
DR   EnsemblFungi; YML034W_mRNA; YML034W; YML034W.
DR   GeneID; 854974; -.
DR   KEGG; sce:YML034W; -.
DR   AGR; SGD:S000004497; -.
DR   SGD; S000004497; SRC1.
DR   VEuPathDB; FungiDB:YML034W; -.
DR   eggNOG; ENOG502QVG5; Eukaryota.
DR   GeneTree; ENSGT00940000171142; -.
DR   HOGENOM; CLU_010838_0_0_1; -.
DR   InParanoid; Q03707; -.
DR   OMA; FCEIPEE; -.
DR   OrthoDB; 1387791at2759; -.
DR   BioCyc; YEAST:G3O-32634-MONOMER; -.
DR   Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   BioGRID-ORCS; 854974; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q03707; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03707; Protein.
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   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IGI:SGD.
DR   GO; GO:0043007; P:maintenance of rDNA; IMP:SGD.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IGI:SGD.
DR   CDD; cd12935; LEM_like; 1.
DR   Gene3D; 1.10.10.1180; MAN1, winged-helix domain; 1.
DR   IDEAL; IID50325; -.
DR   InterPro; IPR025856; HeH/LEM_domain.
DR   InterPro; IPR044780; Heh2/Src1.
DR   InterPro; IPR018996; Man1/Src1-like_C.
DR   InterPro; IPR041885; MAN1_winged_helix_dom.
DR   PANTHER; PTHR47808; INNER NUCLEAR MEMBRANE PROTEIN HEH2-RELATED; 1.
DR   PANTHER; PTHR47808:SF2; LEM DOMAIN-CONTAINING PROTEIN 2; 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..834
FT                   /note="Inner nuclear membrane protein SRC1"
FT                   /id="PRO_0000072188"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        708..728
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          68..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..130
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         394
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   834 AA;  95498 MW;  214CA064ECE160F4 CRC64;
     MNSDLEYLED GFDPNSMKVA TLRRILVENN VDFPSNARKN ALVGLFDEKV KPQIPQLRKM
     YLNVRPSDEG IVKMDRPSSS PSIASPRRSR RARREKSASP MAKQFKKNRI LDDVSNDDDD
     DDDDDDDNDK KDDPLIVPSG TDTDEVDDEE DDVITSSSNK SDTNDFQQNS DTRKKRKDPD
     SDDWSESNSK ENKIDNKHLN LLSSDSEIEQ DYQKAKKRKT SDLNQEHGNG SAILGKLSVK
     TPIKNTNRKP VSMDNFNDSL TSSGTENDPF VPNIRHNPKE LGTANGTGHS TPLSKLKVSA
     SFADKLPQKE VPSTILVPEV EQQEPSQSER TPSLFSSEGS GSESEAPLLP EITTPGPHQP
     MGNTSNNVVE MIDTDSSNLV SDEDEVLVPT RIETPQLPTE KDVEKCEARV QELQEEVNEQ
     LEHENGSEFD VKQGSGKVGN RHKFKRALKF LSKSLLALFL FCIFIVIPLL FGLWYREQRL
     LIGYCGHEVP SHRVSGNSFE FIQKLDNLLQ DYRPKCIPCP PNGICYPYLK LKCKPDYKLA
     PSRLDFLEII PAQGKCVKDD KKQQLVSEVV EKSLEFLRAK NAQISCGDGK DDIESGMTED
     ALYQIFNEAR APWIRDDEFE DLWIQVIKDL TEEPEILWRQ LSPTDNNIGG NSNNIIKTND
     VPRQKRHLPE KFISKTRNFR STSKKYIGMK CRFEREIYQT YKKFQRPIWL MFLLIVISKV
     IEIKLKNYYR KKARIEELVT QTMEKLKFQK IKSMSDPKEN AYLSIVQLRD IFLSDIVDLK
     YKNQLWSEVV KYLEHNNSNI KSNLTEIRGE IMKCWEWIGP MELNEPKDSA ENKI
//