UBXN7_PONAB
ID UBXN7_PONAB Reviewed; 489 AA.
AC Q5REY7; Q5RBE2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=UBX domain-containing protein 7;
GN Name=UBXN7; Synonyms=UBXD7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8-
CC associated cullin ring ligases (CRLs) to the segregase VCP/p97, to
CC regulate turnover of their ubiquitination substrates (By similarity).
CC {ECO:0000250|UniProtKB:O94888}.
CC -!- SUBUNIT: Interacts with neddylated CUL2, ubiquitinated HIF1A, and
CC VCP/p97. {ECO:0000250|UniProtKB:O94888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94888}.
CC -!- DOMAIN: The UIM (ubiquitin-interacting motif) is required to engage the
CC NEDD8 modification on cullins. {ECO:0000250|UniProtKB:O94888}.
CC -!- DOMAIN: The UBX domain mediates interaction with VCP/p97.
CC {ECO:0000250|UniProtKB:O94888}.
CC -!- DOMAIN: The UBA domain is required for binding ubiquitinated-protein
CC substrates. {ECO:0000250|UniProtKB:O94888}.
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DR EMBL; CR857376; CAH89670.1; -; mRNA.
DR EMBL; CR858709; CAH90918.1; -; mRNA.
DR RefSeq; NP_001125524.1; NM_001132052.1.
DR AlphaFoldDB; Q5REY7; -.
DR SMR; Q5REY7; -.
DR STRING; 9601.ENSPPYP00000016149; -.
DR Ensembl; ENSPPYT00000046529; ENSPPYP00000028144; ENSPPYG00000038112.
DR GeneID; 100172436; -.
DR KEGG; pon:100172436; -.
DR CTD; 26043; -.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG1364; Eukaryota.
DR GeneTree; ENSGT00390000018687; -.
DR HOGENOM; CLU_021255_3_0_1; -.
DR InParanoid; Q5REY7; -.
DR OMA; ICAFPRK; -.
DR OrthoDB; 1130151at2759; -.
DR TreeFam; TF323635; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR017346; UBX_7/2.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CHAIN 2..489
FT /note="UBX domain-containing protein 7"
FT /id="PRO_0000211037"
FT DOMAIN 2..54
FT /note="UBA"
FT REPEAT 285..304
FT /note="ubiquitin-interacting motif (UIM)"
FT DOMAIN 408..485
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 56..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CONFLICT 211
FT /note="E -> V (in Ref. 1; CAH90918)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="D -> G (in Ref. 1; CAH89670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54862 MW; 3C894533B1A2C41A CRC64;
MAAHGGSAAS SALKGLIQQF TTITGASESV GKHMLEACNN NLEMAVTMFL DGGGIAEEPS
TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGAPKR RRPARSIFDG FRDFQTETIR
QEQELRNGGA IDKKLTTLAD LFRPPIDLMH KGSFETAKEC GQMQNKWLMI NIQNVQDFAC
QCLNRDVWSN EAVKNIIREH FIFWQVYHDS EEGQRYIQFY KLGDFPYVSI LDPRTGQKLV
EWHQLDVSSF LDQVTGFLGE HGQLDGLSSS PPKKCARSES LIDASEDSQL EAAIRASLQE
THFDSTQTKQ DSRSDEESES ELFSGSEEFI SVCGSDEEEE VENLAKSRKS PHKDLGHRKE
ENRRPLTEPP VRTDPGTATN HQGLPAVDSE ILEMPPEKAD GVVEGIDVNG PKAQLMLRYP
DGKREQITLP EQAKLLALVK HVQSKGYPNE RFELLTNFPR RKLSHLDYDI TLQEAGLCPQ
ETVFVQERN
