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Q9Y3C8 (UFC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-fold modifier-conjugating enzyme 1

Short name=Ufm1-conjugating enzyme 1
Gene names
Name:UFC1
ORF Names:CGI-126, HSPC155
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E2-like enzyme which forms an intermediate with UFM1 via a thioester linkage. Ref.1

Subunit structure

Interacts with UBA5. Interacts with UFL1. Ref.8 Ref.11

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family. UFC1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 167167Ubiquitin-fold modifier-conjugating enzyme 1
PRO_0000082613

Sites

Active site1161Glycyl thioester intermediate

Natural variations

Natural variant901Y → C. Ref.7
Corresponds to variant rs17849932 [ dbSNP | Ensembl ].
VAR_028312

Experimental info

Mutagenesis301Q → A: Does not affect neither UBA5-binding nor thioester formation with UFM1. Ref.11
Mutagenesis331K → A: Impairs binding to UBA5 and thioester formation with UFM1. Ref.11
Mutagenesis1161C → S: Instead of the formation of an intermediate complex with a thiol ester bond between UFC1 (E2-like enzyme) and UFM1 (substrate), a stable complex with an O-ester bond is formed. Ref.1
Sequence conflict1591I → N in BAF85465. Ref.4
Sequence conflict1601Q → H in BAD15374. Ref.1
Sequence conflict1601Q → H in AAF29119. Ref.3

Secondary structure

............................ 167
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y3C8 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 1675D9187DC43E14

FASTA16719,458
        10         20         30         40         50         60 
MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK 

        70         80         90        100        110        120 
EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH 

       130        140        150        160 
FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ 

« Hide

References

« Hide 'large scale' references
[1]"A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier."
Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N., Ueno T., Kominami E., Natsume T., Tanaka K.
EMBO J. 23:1977-1986(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-116.
[2]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Trachea.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-90.
Tissue: Urinary bladder.
[8]"A novel type of E3 ligase for the Ufm1 conjugation system."
Tatsumi K., Sou Y.S., Tada N., Nakamura E., Iemura S., Natsume T., Kang S.H., Chung C.H., Kasahara M., Kominami E., Yamamoto M., Tanaka K., Komatsu M.
J. Biol. Chem. 285:5417-5427(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UFL1.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"GFT NMR based resonance assignment for the 21 kDa human protein UFC1."
Liu G., Aramini J., Atreya H.S., Eletsky A., Xiao R., Acton T., Ma L., Montelione G.T., Szyperski T.
J. Biomol. NMR 32:261-261(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY STRUCTURE BY NMR.
[11]"Crystal structure of Ufc1, the Ufm1-conjugating enzyme."
Mizushima T., Tatsumi K., Ozaki Y., Kawakami T., Suzuki A., Ogasahara K., Komatsu M., Kominami E., Tanaka K., Yamane T.
Biochem. Biophys. Res. Commun. 362:1079-1084(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), INTERACTION WITH UBA5, MUTAGENESIS OF GLN-30 AND LYS-33.
[12]"NMR and X-RAY structures of human E2-like ubiquitin-fold modifier conjugating enzyme 1 (UFC1) reveal structural and functional conservation in the metazoan UFM1-UBA5-UFC1 ubiquination pathway."
Liu G., Forouhar F., Eletsky A., Atreya H.S., Aramini J.M., Xiao R., Huang Y.J., Abashidze M., Seetharaman J., Liu J., Rost B., Acton T., Montelione G.T., Hunt J.F., Szyperski T.
J. Struct. Funct. Genomics 10:127-136(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS), STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB154405 mRNA. Translation: BAD15374.1.
AF151884 mRNA. Translation: AAD34121.1.
AF161504 mRNA. Translation: AAF29119.1.
AK292776 mRNA. Translation: BAF85465.1.
AL590714 Genomic DNA. Translation: CAH72141.1.
CH471121 Genomic DNA. Translation: EAW52646.1.
CH471121 Genomic DNA. Translation: EAW52647.1.
BC005187 mRNA. Translation: AAH05187.1.
CCDSCCDS1220.1.
RefSeqNP_057490.2. NM_016406.3.
UniGeneHs.301412.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K07NMR-A1-167[»]
2Z6OX-ray1.60A1-167[»]
2Z6PX-ray1.80A1-167[»]
3EVXX-ray2.54A/B/C/D1-167[»]
ProteinModelPortalQ9Y3C8.
SMRQ9Y3C8. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119577. 26 interactions.
IntActQ9Y3C8. 1 interaction.
STRING9606.ENSP00000356982.

PTM databases

PhosphoSiteQ9Y3C8.

Polymorphism databases

DMDM116242840.

Proteomic databases

MaxQBQ9Y3C8.
PaxDbQ9Y3C8.
PeptideAtlasQ9Y3C8.
PRIDEQ9Y3C8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368003; ENSP00000356982; ENSG00000143222.
GeneID51506.
KEGGhsa:51506.
UCSCuc001fyd.4. human.

Organism-specific databases

CTD51506.
GeneCardsGC01P161122.
HGNCHGNC:26941. UFC1.
HPAHPA027481.
HPA028722.
MIM610554. gene.
neXtProtNX_Q9Y3C8.
PharmGKBPA142670644.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318908.
HOVERGENHBG054254.
InParanoidQ9Y3C8.
KOK12165.
OMAGTKWFGK.
OrthoDBEOG7JMGFR.
PhylomeDBQ9Y3C8.
TreeFamTF313587.

Gene expression databases

BgeeQ9Y3C8.
CleanExHS_UFC1.
GenevestigatorQ9Y3C8.

Family and domain databases

InterProIPR016135. UBQ-conjugating_enzyme/RWD.
IPR014806. Ufc1.
[Graphical view]
PANTHERPTHR12921. PTHR12921. 1 hit.
PfamPF08694. UFC1. 1 hit.
[Graphical view]
PIRSFPIRSF008716. DUF1782. 1 hit.
SUPFAMSSF54495. SSF54495. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUFC1. human.
EvolutionaryTraceQ9Y3C8.
GenomeRNAi51506.
NextBio55190.
PROQ9Y3C8.
SOURCESearch...

Entry information

Entry nameUFC1_HUMAN
AccessionPrimary (citable) accession number: Q9Y3C8
Secondary accession number(s): A8K9R1 expand/collapse secondary AC list , D3DVF9, Q549X0, Q5VTX1, Q9BS96, Q9P009
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM