ID H2N962_PONAB Unreviewed; 1173 AA.
AC H2N962; A0A2J8USD7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Ubiquitin conjugation factor E4 {ECO:0000256|RuleBase:RU369083};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369083};
DE AltName: Full=RING-type E3 ubiquitin transferase E4 {ECO:0000256|RuleBase:RU369083};
GN Name=UBE4B {ECO:0000313|Ensembl:ENSPPYP00000002206.3};
GN ORFNames=CR201_G0025768 {ECO:0000313|EMBL:PNJ48170.1};
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 {ECO:0000313|Ensembl:ENSPPYP00000002206.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000002206.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ48170.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ48170.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000002206.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC ligase in conjunction with specific E1 and E2 ligases. Also functions
CC as an E4 ligase mediating the assembly of polyubiquitin chains on
CC substrates ubiquitinated by another E3 ubiquitin ligase. Mediates 'Lys-
CC 48'-linked polyubiquitination of substrates.
CC {ECO:0000256|RuleBase:RU369083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU369083};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU369083}.
CC -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC activity. {ECO:0000256|RuleBase:RU369083}.
CC -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC {ECO:0000256|ARBA:ARBA00007434, ECO:0000256|RuleBase:RU369083}.
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DR EMBL; NDHI03003447; PNJ48170.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000002206; -.
DR Ensembl; ENSPPYT00000002273.3; ENSPPYP00000002206.3; ENSPPYG00000001903.3.
DR eggNOG; KOG2042; Eukaryota.
DR GeneTree; ENSGT00390000009300; -.
DR HOGENOM; CLU_003224_2_0_1; -.
DR TreeFam; TF300802; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR CDD; cd16658; RING-Ubox_UBE4B; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR InterPro; IPR045132; UBE4.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13931:SF2; UBIQUITIN CONJUGATION FACTOR E4 B; 1.
DR PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF10408; Ufd2P_core; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369083};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Transferase {ECO:0000256|RuleBase:RU369083};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369083}.
FT DOMAIN 1098..1171
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 133202 MW; D8ED50E15B3BCE39 CRC64;
MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS QSLGLSVHNM
TPATSPIGAS GVAHRSQSSE GVSSLSSSPS NSLETQSQSL SRSQSMDIDG VSCEKSMSQV
DVDSGIENME VDENDRREKR SLSDKEPSSG PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL
SSLSAQFKQN PKEVFSDFKD LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIAAAARSPD
RNLLLNTGSN PGTSPMFCNV GSFGASSLSS LGASGGASNW DSYSDHFTIE TCKETDMLNY
LIECFDRVGI EEKKAPKMCS QPAVSQLLSN IRSQCISHTA LVLQGSLTQP RSLQQPSFLV
PYMLCRNLPY GFIQELVRTT HQDEEVFKQI FIPILQGLAL AAKECSLDSD YFKYPLMALG
ELCETKFGKT HPVCNLVASL PLWLPKSLSP GCGRELQRLS YLGAFFSFSV FAEDDVKVVE
KYFSGPAITL ENTRVVSQSL QHYLELGRQE LFKILHSILL NGETREAALS YMAAVVNANM
KKAQMQTDDR LVSTDGFMLN FLWVLQQLST KIKLETVDPT YIFHPRCRIT LPNDETRVNA
TMEDVNDWLT ELYGDQPPFS EPKFPTECFF LTLHAHHLSI LPSCRRYIRR LRAIRELNRT
VEDLKNNESQ WKDSPLATRH REMLKRCKTQ LKKLVRCKAC ADAGLLDESF LRRCLNFYGL
LIQLLLRILD PAYPDITLPL NSDVPKVFAA LPEFYVEDVA EFLFFIVQYS PQALYEPCTQ
DIVMFLVVML CNQNYIRNPY LVAKLVEVMF MTNPAVQPRT QKFFEMIENH PLSTKLLVPS
LMKFYTDVEH TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM
LINDTTFLLD ESLESLKRIH EVQEEMKNKE QWDQLPRDQQ QARQSQLAQD ERVSRSYLAL
ATETVDMFHI LTKQVQKPFL RPELGPRLAA MLNFNLQQLC GPKCRDLKVE NPEKYGFEPK
KLLDQLTDIY LQLDCARFAK AIADDQRSYS KELFEEVISK MRKAGIKSTI AIEKFKLLAE
KVEEIVAKNA RAEIDYSDAP DEFRDPLMDT LMTDPVRLPS GTIMDRSIIL RHLLNSPTDP
FNRQTLTESM LEPVPELKEQ IQAWMREKQN SDH
//
