ID   MKRN4_HUMAN             Reviewed;         485 AA.
AC   Q13434;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase makorin-4;
DE            EC=2.3.2.27;
DE   AltName: Full=Makorin RING finger protein pseudogene 4;
DE   AltName: Full=Makorin RING finger protein pseudogene 5;
DE   AltName: Full=RING finger protein 64;
DE   AltName: Full=RING-type E3 ubiquitin transferase makorin-4 {ECO:0000305};
DE   AltName: Full=Zinc finger protein 127-Xp;
DE            Short=ZNF127-Xp;
DE   AltName: Full=Zinc finger protein 127-like 1;
GN   Name=MKRN4P; Synonyms=MKRN4, MKRNP5, RNF64, ZNF127L1;
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 [GENOMIC DNA].
RA   Hendrich B.D., Longstreet M., Gustashaw K., Nicholls R.D., Willard H.F.;
RT   "An X-linked homologue of the autosomal imprinted gene ZNF127 escapes X
RT   chromosome inactivation.";
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a E3 ubiquitin ligase catalyzing the covalent
CC       attachment of ubiquitin moieties onto substrate proteins.
CC       {ECO:0000250}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; U41315; AAA99070.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q13434; -.
DR   IntAct; Q13434; 3.
DR   iPTMnet; Q13434; -.
DR   PhosphoSitePlus; Q13434; -.
DR   BioMuta; HGNC:7115; -.
DR   DMDM; 17368441; -.
DR   jPOST; Q13434; -.
DR   MassIVE; Q13434; -.
DR   MaxQB; Q13434; -.
DR   PeptideAtlas; Q13434; -.
DR   PRIDE; Q13434; -.
DR   ProteomicsDB; 59430; -.
DR   GeneCards; MKRN4P; -.
DR   HGNC; HGNC:7115; MKRN4P.
DR   neXtProt; NX_Q13434; -.
DR   PharmGKB; PA30834; -.
DR   InParanoid; Q13434; -.
DR   PhylomeDB; Q13434; -.
DR   PathwayCommons; Q13434; -.
DR   SignaLink; Q13434; -.
DR   UniPathway; UPA00143; -.
DR   Pharos; Q13434; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q13434; protein.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR045072; MKRN-like.
DR   InterPro; IPR031644; MKRN1_C.
DR   InterPro; IPR041367; Znf-CCCH_4.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11224; PTHR11224; 1.
DR   Pfam; PF15815; MKRN1_C; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF18044; zf-CCCH_4; 2.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   SUPFAM; SSF90229; SSF90229; 2.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   5: Uncertain;
KW   Metal-binding; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..485
FT                   /note="Putative E3 ubiquitin-protein ligase makorin-4"
FT                   /id="PRO_0000055961"
FT   ZN_FING         90..117
FT                   /note="C3H1-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         124..146
FT                   /note="C3H1-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         243..270
FT                   /note="C3H1-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   ZN_FING         316..370
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         399..428
FT                   /note="C3H1-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..298
FT                   /note="Makorin-type Cys-His"
SQ   SEQUENCE   485 AA;  52910 MW;  AE28B962544CEFFE CRC64;
     MAEAAAPGTT VTTSGAGAAA AEAAETAEAV SPTPIPTVTA PSPRAGGGVG GSDGSDGSGG
     RGDSGAYDGS GACGGSDACD GSGDSSGDSW TKQVTCRYFK YGICKEGDNC RYSHDLSDRL
     CGVVCKYFQR GCCVYGDRCR CEHSKPLKQE EATATELTTK SSLAASSSLS SIVGPLVEMN
     TNEAESRNSN FATVVAGSED WANAIEFVPG QPYCGRTVPS CTEAPLQGSV TKEESEEEQT
     AVETKKQLCP YAAVGQCRYG ENCVYLHGDL CDMCGLQVLH PMDAAQRSQH IQACIEAHEK
     DMEFSFAVQR SKDKVCGICM EVVYEKANPN EHRFGILSNC NHTFCLKCIR KWRSAKEFES
     RIVKSCPQCR ITSNFVIPSE YWVEEKEEKQ KLIQKYKEAM SNKACKYFDE GRGSCPFGEN
     CFYKHMYPDG RREEPQRQQV GTSSRNPGQQ RNHFWEFFEE GANSNPFDDE EEAVTFELGE
     MLLML