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Protein

E3 UFM1-protein ligase 1

Gene

Ufl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins, a post-translational modification on lysine residues of proteins that may play a crucial role in a number of cellular processes. Mediates DDRGK1 ufmylation and may regulate the proteasomal degradation of DDRGK1 and CDK5RAP3 thereby modulating NF-kappa-B signaling. May also through TRIP4 ufmylation play a role in nuclear receptors-mediated transcription. May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
E3 UFM1-protein ligase 1Curated (EC:6.3.2.-By similarity)
Gene namesi
Name:Ufl1Imported
Synonyms:Kiaa0776Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914740. Ufl1.

Subcellular locationi

  • Endoplasmic reticulum By similarity
  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 793792E3 UFM1-protein ligase 1PRO_0000050772Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei458 – 4581PhosphoserineCombined sources
Modified residuei752 – 7521PhosphoserineCombined sources
Modified residuei753 – 7531PhosphoserineCombined sources

Post-translational modificationi

Ubiquitinated, leading to its degradation by the proteasome. Interaction with CDK5RAP3 protects each other against ubiquitination and degradation via the proteasome.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8CCJ3.
MaxQBiQ8CCJ3.
PaxDbiQ8CCJ3.
PeptideAtlasiQ8CCJ3.
PRIDEiQ8CCJ3.

PTM databases

iPTMnetiQ8CCJ3.
PhosphoSiteiQ8CCJ3.

Expressioni

Tissue specificityi

Ubiquitously expressed with higher expression in pancreatic islets and other secretory tissues.2 Publications

Gene expression databases

BgeeiQ8CCJ3.
CleanExiMM_1810074P20RIK.
GenevisibleiQ8CCJ3. MM.

Interactioni

Subunit structurei

Interacts with DDRGK1 (By similarity). Interacts with UFC1 (By similarity). Interacts with RELA (By similarity). Interacts with TRIP4 (By similarity). Interacts with CDK5RAP3; the interaction is direct (PubMed:21494687).By similarity

Protein-protein interaction databases

BioGridi212226. 59 interactions.
IntActiQ8CCJ3. 59 interactions.
STRINGi10090.ENSMUSP00000100059.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 212211Required for E3 UFM1-protein ligase activityBy similarityAdd
BLAST
Regioni2 – 200199Mediates interaction with DDRGK1By similarityAdd
BLAST
Regioni121 – 250130Involved in CDK5RAP3-bindingBy similarityAdd
BLAST
Regioni200 – 400201Mediates interaction with TRIP4By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the UFL1 family.Curated

Phylogenomic databases

eggNOGiKOG2235. Eukaryota.
ENOG410XSRX. LUCA.
GeneTreeiENSGT00390000002112.
HOVERGENiHBG060009.
InParanoidiQ8CCJ3.
OMAiIVDLQQV.
OrthoDBiEOG78WKR3.
PhylomeDBiQ8CCJ3.
TreeFamiTF319116.

Family and domain databases

InterProiIPR018611. E3_UFM1_ligase_1.
[Graphical view]
PfamiPF09743. DUF2042. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CCJ3-3) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADAWEEIRR LAADFQRAQF AESTQRLSER NCIEIVNKLI SQKQLEVVHT
60 70 80 90 100
LDGKEYITPA QISKEMRDEL HVRGGRVNIV DLQQVINVDL THIESRVSDI
110 120 130 140 150
IKSEKHVQMV LGQLIDENYL DQLSEEVNDK LQESGQVTVS ELCKAYDLPG
160 170 180 190 200
DFLTQALTQR LGRIINGHLD LDNRGVIFTE AFVARHKARI RGLFSAITRP
210 220 230 240 250
TPVNSLVSKY GFQEQLLYSV LEDLVSTGRL RGTVVGGRQD KAVFVPDIYS
260 270 280 290 300
RTQSTWVDSF FRQNGYLEFD ALSRLGIPDA VNYIKKRYKN TQLLFLKATC
310 320 330 340 350
VGQGLVDQVE ASVEEAISSG TWVDISPLLP SSLSVEDAAM LLQQVMRPFG
360 370 380 390 400
KLASAIVFSD TVVVSEKFIT DCTGLFSERM HQKAEKEMKN NPVHLITEED
410 420 430 440 450
LKQISILESV NTSKKDKKDE RRKKATEGSG SVRGGGGGNA REYKIKKTKK
460 470 480 490 500
KGRKDEDSDD ESQSSHGGKK KPDITFMFQD EIEDCLRKHI QDAPEEFISE
510 520 530 540 550
LAEYLIKPLN KMYLEVVRSV FMSSTSASGT GRKRTIKDLQ EEVSNLYNNI
560 570 580 590 600
RLFEKGMKYF ADDTQTALTK HLLKTVCTDI TNLMFNFLAS DFLMAVEEPA
610 620 630 640 650
AITSDIRKKI LSKLTEETKV ALTKLHNSLN EKSIEDFLSC LDSATEACDI
660 670 680 690 700
MVKKGDKKRE RQILFQHRQA LCEQLKVTED PALILHLTAV LLFQLSTHSM
710 720 730 740 750
LHAPGRCVPQ IIAFLHSKIP EDQHTLLVKY QGLVVKQLVS QNKKTGQGED
760 770 780 790
PSSDELDKEQ HDVTNATRKE LQELSLSIKD LVLKSRKSSV TEE
Length:793
Mass (Da):89,520
Last modified:June 21, 2005 - v2
Checksum:i182930A83D1F7155
GO
Isoform 2 (identifier: Q8CCJ3-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.
     81-84: DLQQ → MSEV

Show »
Length:713
Mass (Da):80,220
Checksum:i62216D414C1E4227
GO
Isoform 3 (identifier: Q8CCJ3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-476: Missing.

Show »
Length:317
Mass (Da):36,084
Checksum:i530E7B2123DE1A2A
GO

Sequence cautioni

The sequence BAC98021.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221Q → R in BAC98021 (PubMed:14621295).Curated
Sequence conflicti122 – 1221Q → R in AAI38154 (PubMed:15489334).Curated
Sequence conflicti122 – 1221Q → R in AAI32196 (PubMed:15489334).Curated
Sequence conflicti389 – 3891K → N in BAC27976 (PubMed:16141072).Curated
Sequence conflicti408 – 4081E → G in BAB25395 (PubMed:16141072).Curated
Sequence conflicti409 – 4091S → C in BAC38618 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 476476Missing in isoform 3. 1 PublicationVSP_014249Add
BLAST
Alternative sequencei1 – 8080Missing in isoform 2. 1 PublicationVSP_014250Add
BLAST
Alternative sequencei81 – 844DLQQ → MSEV in isoform 2. 1 PublicationVSP_014251

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007993 mRNA. Translation: BAB25395.1.
AK013382 mRNA. Translation: BAC25404.1.
AK032663 mRNA. Translation: BAC27976.1.
AK082785 mRNA. Translation: BAC38618.1.
AK129211 mRNA. Translation: BAC98021.1. Different initiation.
AK132697 mRNA. Translation: BAE21308.1.
AL831754, AL935267 Genomic DNA. Translation: CAM19990.1.
AL935267, AL831754 Genomic DNA. Translation: CAM22171.1.
AL831754, AL935267 Genomic DNA. Translation: CAM19989.1.
AL935267, AL831754 Genomic DNA. Translation: CAM22170.1.
CH466538 Genomic DNA. Translation: EDL05527.1.
BC138153 mRNA. Translation: AAI38154.1.
BC132195 mRNA. Translation: AAI32196.1.
CCDSiCCDS18010.1. [Q8CCJ3-3]
RefSeqiNP_080470.2. NM_026194.4. [Q8CCJ3-3]
XP_006538266.1. XM_006538203.2. [Q8CCJ3-3]
UniGeneiMm.226295.

Genome annotation databases

EnsembliENSMUST00000038705; ENSMUSP00000042118; ENSMUSG00000040359. [Q8CCJ3-1]
ENSMUST00000102994; ENSMUSP00000100059; ENSMUSG00000040359. [Q8CCJ3-3]
GeneIDi67490.
KEGGimmu:67490.
UCSCiuc008seg.2. mouse. [Q8CCJ3-3]
uc012dbb.1. mouse. [Q8CCJ3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007993 mRNA. Translation: BAB25395.1.
AK013382 mRNA. Translation: BAC25404.1.
AK032663 mRNA. Translation: BAC27976.1.
AK082785 mRNA. Translation: BAC38618.1.
AK129211 mRNA. Translation: BAC98021.1. Different initiation.
AK132697 mRNA. Translation: BAE21308.1.
AL831754, AL935267 Genomic DNA. Translation: CAM19990.1.
AL935267, AL831754 Genomic DNA. Translation: CAM22171.1.
AL831754, AL935267 Genomic DNA. Translation: CAM19989.1.
AL935267, AL831754 Genomic DNA. Translation: CAM22170.1.
CH466538 Genomic DNA. Translation: EDL05527.1.
BC138153 mRNA. Translation: AAI38154.1.
BC132195 mRNA. Translation: AAI32196.1.
CCDSiCCDS18010.1. [Q8CCJ3-3]
RefSeqiNP_080470.2. NM_026194.4. [Q8CCJ3-3]
XP_006538266.1. XM_006538203.2. [Q8CCJ3-3]
UniGeneiMm.226295.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212226. 59 interactions.
IntActiQ8CCJ3. 59 interactions.
STRINGi10090.ENSMUSP00000100059.

PTM databases

iPTMnetiQ8CCJ3.
PhosphoSiteiQ8CCJ3.

Proteomic databases

EPDiQ8CCJ3.
MaxQBiQ8CCJ3.
PaxDbiQ8CCJ3.
PeptideAtlasiQ8CCJ3.
PRIDEiQ8CCJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038705; ENSMUSP00000042118; ENSMUSG00000040359. [Q8CCJ3-1]
ENSMUST00000102994; ENSMUSP00000100059; ENSMUSG00000040359. [Q8CCJ3-3]
GeneIDi67490.
KEGGimmu:67490.
UCSCiuc008seg.2. mouse. [Q8CCJ3-3]
uc012dbb.1. mouse. [Q8CCJ3-1]

Organism-specific databases

CTDi23376.
MGIiMGI:1914740. Ufl1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG2235. Eukaryota.
ENOG410XSRX. LUCA.
GeneTreeiENSGT00390000002112.
HOVERGENiHBG060009.
InParanoidiQ8CCJ3.
OMAiIVDLQQV.
OrthoDBiEOG78WKR3.
PhylomeDBiQ8CCJ3.
TreeFamiTF319116.

Miscellaneous databases

PROiQ8CCJ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CCJ3.
CleanExiMM_1810074P20RIK.
GenevisibleiQ8CCJ3. MM.

Family and domain databases

InterProiIPR018611. E3_UFM1_ligase_1.
[Graphical view]
PfamiPF09743. DUF2042. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo, Pancreas and Testis.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Embryonic tail.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain.
  6. "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
    Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
    Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752 AND SER-753, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "A novel C53/LZAP-interacting protein regulates stability of C53/LZAP and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB signaling."
    Wu J., Lei G., Mei M., Tang Y., Li H.
    J. Biol. Chem. 285:15126-15136(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  10. "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis."
    Lemaire K., Moura R.F., Granvik M., Igoillo-Esteve M., Hohmeier H.E., Hendrickx N., Newgard C.B., Waelkens E., Cnop M., Schuit F.
    PLoS ONE 6:E18517-E18517(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK5RAP3, TISSUE SPECIFICITY.

Entry informationi

Entry nameiUFL1_MOUSE
AccessioniPrimary (citable) accession number: Q8CCJ3
Secondary accession number(s): A2RSP7
, B1AXU5, B1AXU6, Q3V145, Q6ZQ50, Q8BT70, Q8C484, Q9D8I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: July 6, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.