ID   UE2NL_HUMAN             Reviewed;         153 AA.
AC   Q5JXB2; E9KL27;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative ubiquitin-conjugating enzyme E2 N-like;
DE   AltName: Full=Epididymis tissue protein Li 174;
GN   Name=UBE2NL;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA   Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA   Jin S., Liu J., Zhu P., Liu Y.;
RT   "Systematic mapping and functional analysis of a family of human epididymal
RT   secretory sperm-located proteins.";
RL   Mol. Cell. Proteomics 9:2517-2528(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
CC   -!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level).
CC       {ECO:0000269|PubMed:20736409}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- CAUTION: Could be inactive as a ligase. The potential active site Cys
CC       residue in position 88 is replaced by a Ser. {ECO:0000305}.
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DR   EMBL; GU727624; ADU87626.1; -; mRNA.
DR   EMBL; AL109622; CAB72341.1; -; Genomic_DNA.
DR   RefSeq; NP_001013007.1; NM_001012989.2.
DR   AlphaFoldDB; Q5JXB2; -.
DR   SMR; Q5JXB2; -.
DR   BioGRID; 133317; 9.
DR   IntAct; Q5JXB2; 3.
DR   iPTMnet; Q5JXB2; -.
DR   PhosphoSitePlus; Q5JXB2; -.
DR   SwissPalm; Q5JXB2; -.
DR   BioMuta; UBE2NL; -.
DR   DMDM; 74742728; -.
DR   EPD; Q5JXB2; -.
DR   jPOST; Q5JXB2; -.
DR   MassIVE; Q5JXB2; -.
DR   MaxQB; Q5JXB2; -.
DR   PaxDb; Q5JXB2; -.
DR   PeptideAtlas; Q5JXB2; -.
DR   PRIDE; Q5JXB2; -.
DR   ProteomicsDB; 63439; -.
DR   DNASU; 389898; -.
DR   GeneID; 389898; -.
DR   KEGG; hsa:389898; -.
DR   CTD; 389898; -.
DR   DisGeNET; 389898; -.
DR   GeneCards; UBE2NL; -.
DR   HGNC; HGNC:31710; UBE2NL.
DR   neXtProt; NX_Q5JXB2; -.
DR   PharmGKB; PA134943659; -.
DR   InParanoid; Q5JXB2; -.
DR   PhylomeDB; Q5JXB2; -.
DR   TreeFam; TF101126; -.
DR   BRENDA; 2.3.2.23; 2681.
DR   PathwayCommons; Q5JXB2; -.
DR   SignaLink; Q5JXB2; -.
DR   BioGRID-ORCS; 389898; 181 hits in 563 CRISPR screens.
DR   GenomeRNAi; 389898; -.
DR   Pharos; Q5JXB2; Tdark.
DR   PRO; PR:Q5JXB2; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q5JXB2; protein.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Reference proteome.
FT   CHAIN           1..153
FT                   /note="Putative ubiquitin-conjugating enzyme E2 N-like"
FT                   /id="PRO_0000271087"
FT   DOMAIN          3..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         83
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61088"
SQ   SEQUENCE   153 AA;  17377 MW;  462536F5533F2230 CRC64;
     MAELPHRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GESKDSPFEG GTFKRELLLA
     EEYPMAAPKV RFMTKIYHPN VDKLERISLD ILKDKWSPAL QIRTVLLSIQ ALLNAPNPDD
     PLANDVVEQW KTNEAQAIET ARAWTRLYAM NSI