SRC1_YEAST
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 03-AUG-2022, entry version 169.
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; 267.
DR DIP; DIP-4546N; -.
DR IntAct; Q03707; 11.
DR MINT; Q03707; -.
DR STRING; 4932.YML034W; -.
DR iPTMnet; Q03707; -.
DR MaxQB; Q03707; -.
DR PaxDb; Q03707; -.
DR PRIDE; Q03707; -.
DR EnsemblFungi; YML034W_mRNA; YML034W; YML034W.
DR GeneID; 854974; -.
DR KEGG; sce:YML034W; -.
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; WIGPLED; -.
DR BioCyc; YEAST:G3O-32634-MON; -.
DR PRO; PR:Q03707; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03707; 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 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 Gene3D; 1.10.10.1180; -; 1.
DR InterPro; IPR025856; HeH/LEM_domain.
DR InterPro; IPR044780; Heh2/Src1.
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..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
