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Protein

Putative ubiquitin-conjugating enzyme E2 N-like

Gene

UBE2NL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ5JXB2.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative ubiquitin-conjugating enzyme E2 N-like
Alternative name(s):
Epididymis tissue protein Li 174
Gene namesi
Name:UBE2NL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:31710. UBE2NL.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • nucleus Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134943659.

Polymorphism and mutation databases

DMDMi74742728.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 153153Putative ubiquitin-conjugating enzyme E2 N-likePRO_0000271087Add
BLAST

Proteomic databases

EPDiQ5JXB2.
PaxDbiQ5JXB2.
PeptideAtlasiQ5JXB2.
PRIDEiQ5JXB2.

PTM databases

iPTMnetiQ5JXB2.
PhosphoSiteiQ5JXB2.
SwissPalmiQ5JXB2.

Expressioni

Tissue specificityi

Expressed in epididymis (at protein level).1 Publication

Gene expression databases

BgeeiQ5JXB2.
CleanExiHS_UBE2NL.

Organism-specific databases

HPAiHPA003962.
HPA044976.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi133317. 3 interactions.
IntActiQ5JXB2. 2 interactions.
STRINGi9606.ENSP00000359525.

Structurei

3D structure databases

ProteinModelPortaliQ5JXB2.
SMRiQ5JXB2. Positions 4-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0417. Eukaryota.
COG5078. LUCA.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ5JXB2.
KOiK10580.
OrthoDBiEOG7XWPQB.
PhylomeDBiQ5JXB2.
TreeFamiTF101126.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5JXB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELPHRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GESKDSPFEG
60 70 80 90 100
GTFKRELLLA EEYPMAAPKV RFMTKIYHPN VDKLERISLD ILKDKWSPAL
110 120 130 140 150
QIRTVLLSIQ ALLNAPNPDD PLANDVVEQW KTNEAQAIET ARAWTRLYAM

NSI
Length:153
Mass (Da):17,377
Last modified:February 15, 2005 - v1
Checksum:i462536F5533F2230
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU727624 mRNA. Translation: ADU87626.1.
AL109622 Genomic DNA. Translation: CAB72341.1.
RefSeqiNP_001013007.1. NM_001012989.2.
UniGeneiHs.585177.

Genome annotation databases

GeneIDi389898.
KEGGihsa:389898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU727624 mRNA. Translation: ADU87626.1.
AL109622 Genomic DNA. Translation: CAB72341.1.
RefSeqiNP_001013007.1. NM_001012989.2.
UniGeneiHs.585177.

3D structure databases

ProteinModelPortaliQ5JXB2.
SMRiQ5JXB2. Positions 4-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi133317. 3 interactions.
IntActiQ5JXB2. 2 interactions.
STRINGi9606.ENSP00000359525.

PTM databases

iPTMnetiQ5JXB2.
PhosphoSiteiQ5JXB2.
SwissPalmiQ5JXB2.

Polymorphism and mutation databases

DMDMi74742728.

Proteomic databases

EPDiQ5JXB2.
PaxDbiQ5JXB2.
PeptideAtlasiQ5JXB2.
PRIDEiQ5JXB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi389898.
KEGGihsa:389898.

Organism-specific databases

CTDi389898.
GeneCardsiUBE2NL.
HGNCiHGNC:31710. UBE2NL.
HPAiHPA003962.
HPA044976.
neXtProtiNX_Q5JXB2.
PharmGKBiPA134943659.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0417. Eukaryota.
COG5078. LUCA.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiQ5JXB2.
KOiK10580.
OrthoDBiEOG7XWPQB.
PhylomeDBiQ5JXB2.
TreeFamiTF101126.

Enzyme and pathway databases

SignaLinkiQ5JXB2.

Miscellaneous databases

GenomeRNAii389898.
PROiQ5JXB2.

Gene expression databases

BgeeiQ5JXB2.
CleanExiHS_UBE2NL.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
    Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
    Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Epididymis.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiUE2NL_HUMAN
AccessioniPrimary (citable) accession number: Q5JXB2
Secondary accession number(s): E9KL27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: February 15, 2005
Last modified: July 6, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Could be inactive as a ligase. The potential active site Cys residue in position 88 is replaced by a Ser.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.