LOCUS       NP_002874                587 aa            linear   PRI 28-APR-2025
DEFINITION  ran GTPase-activating protein 1 [Homo sapiens].
ACCESSION   NP_002874
VERSION     NP_002874.1
DBSOURCE    REFSEQ: accession NM_002883.4
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 587)
  AUTHORS   Zhang,F., Yang,J. and Cheng,Y.
  TITLE     Impact of RANGAP1 SUMOylation on Smad4 nuclear export by
            bioinformatic analysis and cell assays
  JOURNAL   Biomol Biomed 24 (6), 1620-1636 (2024)
   PUBMED   38801243
  REMARK    GeneRIF: Impact of RANGAP1 SUMOylation on Smad4 nuclear export by
            bioinformatic analysis and cell assays.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 587)
  AUTHORS   You,H.J., Ma,L.H., Wang,X., Wang,Y.X., Zhang,H.Y., Bao,E.S.,
            Zhong,Y.J., Liu,X.Y., Kong,D.L., Zheng,K.Y., Kong,F.Y. and
            Tang,R.X.
  TITLE     Hepatitis B virus core protein stabilizes RANGAP1 to upregulate
            KDM2A and facilitate hepatocarcinogenesis
  JOURNAL   Cell Oncol (Dordr) 47 (2), 639-655 (2024)
   PUBMED   37845585
  REMARK    GeneRIF: Hepatitis B virus core protein stabilizes RANGAP1 to
            upregulate KDM2A and facilitate hepatocarcinogenesis.
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Lin,X., Pang,Q., Hu,J., Sun,J., Dai,S., Yu,Y. and Xu,J.
  TITLE     SUMOylation mediates the disassembly of the Smad4 nuclear export
            complex via RanGAP1 in KELOIDS
  JOURNAL   J Cell Mol Med 27 (8), 1045-1055 (2023)
   PUBMED   36916534
  REMARK    GeneRIF: SUMOylation mediates the disassembly of the Smad4 nuclear
            export complex via RanGAP1 in KELOIDS.
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Gong,Y., Zou,S., Deng,D., Wang,L., Hu,H., Qiu,Z., Wei,T., Yang,P.,
            Zhou,J., Zhang,Y., Zhu,W., Xie,X., Liao,Z., Yang,J., Zhang,S.,
            Liu,A., Jiang,Y., Zou,Z. and Bai,X.
  TITLE     Loss of RanGAP1 drives chromosome instability and rapid
            tumorigenesis of osteosarcoma
  JOURNAL   Dev Cell 58 (3), 192-210 (2023)
   PUBMED   36696903
  REMARK    GeneRIF: Loss of RanGAP1 drives chromosome instability and rapid
            tumorigenesis of osteosarcoma.
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Krebber,H. and Ponstingl,H.
  TITLE     Ubiquitous expression and testis-specific alternative
            polyadenylation of mRNA for the human Ran GTPase activator RanGAP1
  JOURNAL   Gene 180 (1-2), 7-11 (1996)
   PUBMED   8973340
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Gorlich,D., Pante,N., Kutay,U., Aebi,U. and Bischoff,F.R.
  TITLE     Identification of different roles for RanGDP and RanGTP in nuclear
            protein import
  JOURNAL   EMBO J 15 (20), 5584-5594 (1996)
   PUBMED   8896452
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Becker,J., Melchior,F., Gerke,V., Bischoff,F.R., Ponstingl,H. and
            Wittinghofer,A.
  TITLE     RNA1 encodes a GTPase-activating protein specific for Gsp1p, the
            Ran/TC4 homologue of Saccharomyces cerevisiae
  JOURNAL   J Biol Chem 270 (20), 11860-11865 (1995)
   PUBMED   7744835
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Bischoff,F.R., Krebber,H., Kempf,T., Hermes,I. and Ponstingl,H.
  TITLE     Human RanGTPase-activating protein RanGAP1 is a homologue of yeast
            Rna1p involved in mRNA processing and transport
  JOURNAL   Proc Natl Acad Sci U S A 92 (5), 1749-1753 (1995)
   PUBMED   7878053
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Bischoff,F.R., Krebber,H., Smirnova,E., Dong,W. and Ponstingl,H.
  TITLE     Co-activation of RanGTPase and inhibition of GTP dissociation by
            Ran-GTP binding protein RanBP1
  JOURNAL   EMBO J 14 (4), 705-715 (1995)
   PUBMED   7882974
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Bischoff,F.R., Klebe,C., Kretschmer,J., Wittinghofer,A. and
            Ponstingl,H.
  TITLE     RanGAP1 induces GTPase activity of nuclear Ras-related Ran
  JOURNAL   Proc Natl Acad Sci U S A 91 (7), 2587-2591 (1994)
   PUBMED   8146159
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA269460.1, BC014044.2,
            BC004990.1, HY062550.1 and HY251691.1.
            
            Summary: This gene encodes a protein that associates with the
            nuclear pore complex and participates in the regulation of nuclear
            transport. The encoded protein interacts with Ras-related nuclear
            protein 1 (RAN) and regulates guanosine triphosphate (GTP)-binding
            and exchange. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            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 :: SRR7346977.1799467.1, BC014044.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356244.8/ ENSP00000348577.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..587
                     /product="ran GTPase-activating protein 1"
                     /note="segregation distorter homolog"
                     /calculated_mol_wt=63411
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:20388717; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Region          21..358
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     Site            order(23,25,28,30,51,54,56,59,61,79,82,84,87,89,114,117,
                     119,122,124,144,147,149,152,154,182,185,187,190,192,210,
                     213,215,218,220,238,241,243,246,248,266,269,271,274,276,
                     295,298,300,303,305,323,326,328,331,333,351,354,356)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Region          48..71
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Region          51..81
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(57..58,121,189,217,273,299,301,327,355)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          82..113
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          111..134
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Region          114..143
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          144..171
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          182..209
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          207..230
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Region          210..237
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          235..258
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Region          238..265
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          266..294
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          292..319
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Region          320..343
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Region          357..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16428860,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Region          409..585
                     /region_name="RanGAP1_C"
                     /note="RanGAP1 C-terminal domain; pfam07834"
                     /db_xref="CDD:462282"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:15037602; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15037602,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15037602,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Region          523..526
                     /region_name="SUMO conjugation"
                     /note="propagated from UniProtKB/Swiss-Prot (P46060.1)"
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Site            562
                     /site_type="other"
                     /note="Hydrophobic interaction with UBE2I.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     Site            565
                     /site_type="other"
                     /note="Hydrophobic interaction with UBE2I.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P46060.1)"
     CDS             1..587
                     /gene="RANGAP1"
                     /gene_synonym="Fug1; RANGAP; SD"
                     /coded_by="NM_002883.4:241..2004"
                     /db_xref="CCDS:CCDS14012.1"
                     /db_xref="GeneID:5905"
                     /db_xref="HGNC:HGNC:9854"
                     /db_xref="MIM:602362"
ORIGIN      
        1 masediakla etlaktqvag gqlsfkgksl klntaedakd vikeiedfds lealrlegnt
       61 vgveaarvia kalekkselk rchwsdmftg rlrteippal islgeglita gaqlveldls
      121 dnafgpdgvq gfeallkssa cftlqelkln ncgmgigggk ilaaaltech rkssaqgkpl
      181 alkvfvagrn rlendgatal aeafrvigtl eevhmpqngi nhpgitalaq afavnpllrv
      241 inlndntfte kgavamaetl ktlrqvevin fgdclvrskg avaiadairg glpklkelnl
      301 sfceikrdaa lavaeamadk aelekldlng ntlgeegceq lqevlegfnm akvlaslsdd
      361 edeeeeeege eeeeeaeeee eedeeeeeee eeeeeeepqq rgqgeksatp srkildpntg
      421 epapvlsspp padvstflaf pspekllrlg pkssvliaqq tdtsdpekvv saflkvssvf
      481 kdeatvrmav qdavdalmqk afnsssfnsn tfltrllvhm gllksedkvk aianlygplm
      541 alnhmvqqdy fpkalaplll afvtkpnsal escsfarhsl lqtlykv
//
