KRR1_HUMAN
ID KRR1_HUMAN Reviewed; 381 AA.
AC Q13601; A0FIK6; A0JLP0; B2R989; E7EUQ0; Q8NEA8; Q8TC37; Q96AT5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=KRR1 small subunit processome component homolog;
DE AltName: Full=HIV-1 Rev-binding protein 2;
DE AltName: Full=KRR-R motif-containing protein 1;
DE AltName: Full=Rev-interacting protein 1;
DE Short=Rip-1;
GN Name=KRR1; Synonyms=HRB2;
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] (ISOFORM 2).
RC TISSUE=Testis;
RA Ma Z.F., Chen J., Li J.M.;
RT "A novel splicing of the HRB2 gene.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Testis, and Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-377 (ISOFORM 1).
RA D'Sa-Eipper C., Venkatesh L.K., Chinnadurai G.;
RT "HIV Rev interacting protein-1.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-11; 53-66; 107-115 AND 358-369, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V.;
RL Submitted (AUG-2005) to UniProtKB.
RN [7]
RP INTERACTION WITH HIV-1 VPR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=7724608; DOI=10.1073/pnas.92.8.3621;
RA Refaeli Y., Levy D.N., Weiner D.B.;
RT "The glucocorticoid receptor type II complex is a target of the HIV-1 vpr
RT gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3621-3625(1995).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-5, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-340 AND LYS-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome (By
CC similarity). Directly interacts with HIV-1 protein VPR. Also identified
CC in a complex with NR3C1 and HIV-1 protein VPR. {ECO:0000250,
CC ECO:0000269|PubMed:7724608}.
CC -!- INTERACTION:
CC Q13601; P62263: RPS14; NbExp=4; IntAct=EBI-744525, EBI-352783;
CC Q13601; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-744525, EBI-539478;
CC Q13601; Q9H171: ZBP1; NbExp=3; IntAct=EBI-744525, EBI-6264672;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.6}. Nucleus
CC {ECO:0000269|Ref.6}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC Note=Translocates from cytoplasm to nucleus after exposure to HIV-1
CC virus or HIV-1 protein VPR or induction by hydrocortisone and
CC dexamethasone in the absence of HIV-1 protein VPR (Ref.6).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13601-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13601-2; Sequence=VSP_042223;
CC -!- SIMILARITY: Belongs to the KRR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB00557.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH05225.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; EF010919; ABJ97679.1; -; mRNA.
DR EMBL; AK313687; BAG36436.1; -; mRNA.
DR EMBL; AC022507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005225; AAH05225.1; ALT_SEQ; mRNA.
DR EMBL; BC016778; AAH16778.1; -; mRNA.
DR EMBL; BC026107; AAH26107.1; -; mRNA.
DR EMBL; BC033887; AAH33887.1; -; mRNA.
DR EMBL; U55766; AAB00557.1; ALT_FRAME; mRNA.
DR CCDS; CCDS9012.1; -. [Q13601-1]
DR PIR; G02629; G02629.
DR RefSeq; NP_008974.5; NM_007043.6. [Q13601-1]
DR PDB; 7MQ8; EM; 3.60 A; NY=1-381.
DR PDB; 7MQ9; EM; 3.87 A; NY=1-381.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR AlphaFoldDB; Q13601; -.
DR SMR; Q13601; -.
DR BioGRID; 116284; 352.
DR IntAct; Q13601; 67.
DR MINT; Q13601; -.
DR STRING; 9606.ENSP00000229214; -.
DR iPTMnet; Q13601; -.
DR PhosphoSitePlus; Q13601; -.
DR SwissPalm; Q13601; -.
DR BioMuta; KRR1; -.
DR DMDM; 50400303; -.
DR SWISS-2DPAGE; Q13601; -.
DR EPD; Q13601; -.
DR jPOST; Q13601; -.
DR MassIVE; Q13601; -.
DR MaxQB; Q13601; -.
DR PaxDb; Q13601; -.
DR PeptideAtlas; Q13601; -.
DR PRIDE; Q13601; -.
DR ProteomicsDB; 59591; -. [Q13601-1]
DR ProteomicsDB; 59592; -. [Q13601-2]
DR Antibodypedia; 29617; 181 antibodies from 28 providers.
DR DNASU; 11103; -.
DR Ensembl; ENST00000229214.9; ENSP00000229214.4; ENSG00000111615.14. [Q13601-1]
DR Ensembl; ENST00000438169.6; ENSP00000411740.2; ENSG00000111615.14. [Q13601-2]
DR GeneID; 11103; -.
DR KEGG; hsa:11103; -.
DR MANE-Select; ENST00000229214.9; ENSP00000229214.4; NM_007043.7; NP_008974.5.
DR UCSC; uc001sxt.4; human. [Q13601-1]
DR CTD; 11103; -.
DR DisGeNET; 11103; -.
DR GeneCards; KRR1; -.
DR HGNC; HGNC:5176; KRR1.
DR HPA; ENSG00000111615; Low tissue specificity.
DR MIM; 612817; gene.
DR neXtProt; NX_Q13601; -.
DR OpenTargets; ENSG00000111615; -.
DR PharmGKB; PA29450; -.
DR VEuPathDB; HostDB:ENSG00000111615; -.
DR eggNOG; KOG2874; Eukaryota.
DR GeneTree; ENSGT00390000018775; -.
DR HOGENOM; CLU_040185_0_0_1; -.
DR InParanoid; Q13601; -.
DR OMA; HKKEKFV; -.
DR OrthoDB; 944899at2759; -.
DR PhylomeDB; Q13601; -.
DR TreeFam; TF105745; -.
DR PathwayCommons; Q13601; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q13601; -.
DR BioGRID-ORCS; 11103; 718 hits in 1084 CRISPR screens.
DR ChiTaRS; KRR1; human.
DR GeneWiki; KRR1; -.
DR GenomeRNAi; 11103; -.
DR Pharos; Q13601; Tbio.
DR PRO; PR:Q13601; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13601; protein.
DR Bgee; ENSG00000111615; Expressed in calcaneal tendon and 201 other tissues.
DR Genevisible; Q13601; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR041174; KH_8.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR024166; rRNA_assembly_KRR1.
DR PANTHER; PTHR12581; PTHR12581; 1.
DR Pfam; PF17903; KH_8; 1.
DR PIRSF; PIRSF006515; KRR1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA processing; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..381
FT /note="KRR1 small subunit processome component homolog"
FT /id="PRO_0000050114"
FT DOMAIN 154..206
FT /note="KH"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 221..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_042223"
FT VARIANT 134
FT /note="R -> Q (in dbSNP:rs11540407)"
FT /id="VAR_049680"
FT CONFLICT 13
FT /note="A -> V (in Ref. 1; ABJ97679)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="E -> K (in Ref. 2; BAG36436)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="E -> G (in Ref. 4; AAH16778)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="R -> G (in Ref. 1; ABJ97679)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> V (in Ref. 1; ABJ97679)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="V -> A (in Ref. 4; AAH26107)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="E -> G (in Ref. 4; AAH33887)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="T -> A (in Ref. 1; ABJ97679 and 4; AAH33887)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="A -> G (in Ref. 4; AAH05225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43665 MW; 8F242FCC36BF079B CRC64;
MASPSLERPE KGAGKSEFRN QKPKPENQDE SELLTVPDGW KEPAFSKEDN PRGLLEESSF
ATLFPKYREA YLKECWPLVQ KALNEHHVNA TLDLIEGSMT VCTTKKTFDP YIIIRARDLI
KLLARSVSFE QAVRILQDDV ACDIIKIGSL VRNKERFVKR RQRLIGPKGS TLKALELLTN
CYIMVQGNTV SAIGPFSGLK EVRKVVLDTM KNIHPIYNIK SLMIKRELAK DSELRSQSWE
RFLPQFKHKN VNKRKEPKKK TVKKEYTPFP PPQPESQIDK ELASGEYFLK ANQKKRQKME
AIKAKQAEAI SKRQEERNKA FIPPKEKPIV KPKEASTETK IDVASIKEKV KKAKNKKLGA
LTAEEIALKM EADEKKKKKK K
