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Protein

Ubiquitin-fold modifier 1

Gene

Ufm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer (PubMed:21494687). The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes. TRIP4 ufmylation may for instance play a role in nuclear receptors-mediated transcription (By similarity). Other substrates may include DDRGK1 with which it may play a role in the cellular response to endoplasmic reticulum stress(PubMed:21494687).By similarity1 Publication

GO - Biological processi

  • protein K69-linked ufmylation Source: UniProtKB
  • protein polyufmylation Source: MGI
  • protein ufmylation Source: UniProtKB
  • regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
  • response to endoplasmic reticulum stress Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-fold modifier 1
Gene namesi
Name:Ufm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1915140. Ufm1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8383Ubiquitin-fold modifier 1PRO_0000042126Add
BLAST
Propeptidei84 – 852Removed in mature formBy similarityPRO_0000042127

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki69 – 69Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)By similarity
Cross-linki83 – 83Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP61961.
PaxDbiP61961.
PRIDEiP61961.

PTM databases

PhosphoSiteiP61961.

Expressioni

Tissue specificityi

Widely expressed with higher expression in secretory tissues (at protein level).1 Publication

Gene expression databases

BgeeiP61961.
CleanExiMM_UFM1.
ExpressionAtlasiP61961. baseline and differential.
GenevisibleiP61961. MM.

Interactioni

Protein-protein interaction databases

BioGridi212514. 10 interactions.
STRINGi10090.ENSMUSP00000118478.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Beta strandi18 – 247Combined sources
Helixi29 – 3911Combined sources
Beta strandi44 – 507Combined sources
Beta strandi60 – 623Combined sources
Helixi63 – 697Combined sources
Beta strandi72 – 787Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J0GNMR-A1-85[»]
ProteinModelPortaliP61961.
SMRiP61961. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61961.

Family & Domainsi

Sequence similaritiesi

Belongs to the UFM1 family.Curated

Phylogenomic databases

eggNOGiNOG249065.
GeneTreeiENSGT00390000010391.
HOGENOMiHOG000185753.
HOVERGENiHBG094129.
InParanoidiP61961.
KOiK12162.
OMAiVTFKIIL.
OrthoDBiEOG7Q8CQW.
PhylomeDBiP61961.
TreeFamiTF312934.

Family and domain databases

InterProiIPR029071. Ubiquitin-rel_dom.
IPR005375. UFM1.
[Graphical view]
PfamiPF03671. Ufm1. 1 hit.
[Graphical view]
PIRSFiPIRSF038027. Ubiquitin-like_Ufm1. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P61961-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII
60 70 80
TNDGIGINPA QTAGNVFLKH GSELRIIPRD RVGSC
Length:85
Mass (Da):9,118
Last modified:June 7, 2004 - v1
Checksum:iEDB2412E5E5836D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007788 mRNA. Translation: BAB25255.1.
AK008280 mRNA. Translation: BAB25572.1.
AK089948 mRNA. Translation: BAC41011.1.
AK148146 mRNA. Translation: BAE28374.1.
AK166332 mRNA. Translation: BAE38712.1.
AK167301 mRNA. Translation: BAE39406.1.
AK167321 mRNA. Translation: BAE39423.1.
BC061065 mRNA. Translation: AAH61065.1.
CCDSiCCDS38430.1.
RefSeqiNP_080711.1. NM_026435.5.
UniGeneiMm.23067.

Genome annotation databases

EnsembliENSMUST00000146598; ENSMUSP00000118478; ENSMUSG00000027746.
GeneIDi67890.
KEGGimmu:67890.
UCSCiuc008pfa.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007788 mRNA. Translation: BAB25255.1.
AK008280 mRNA. Translation: BAB25572.1.
AK089948 mRNA. Translation: BAC41011.1.
AK148146 mRNA. Translation: BAE28374.1.
AK166332 mRNA. Translation: BAE38712.1.
AK167301 mRNA. Translation: BAE39406.1.
AK167321 mRNA. Translation: BAE39423.1.
BC061065 mRNA. Translation: AAH61065.1.
CCDSiCCDS38430.1.
RefSeqiNP_080711.1. NM_026435.5.
UniGeneiMm.23067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J0GNMR-A1-85[»]
ProteinModelPortaliP61961.
SMRiP61961. Positions 1-85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212514. 10 interactions.
STRINGi10090.ENSMUSP00000118478.

PTM databases

PhosphoSiteiP61961.

Proteomic databases

MaxQBiP61961.
PaxDbiP61961.
PRIDEiP61961.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000146598; ENSMUSP00000118478; ENSMUSG00000027746.
GeneIDi67890.
KEGGimmu:67890.
UCSCiuc008pfa.2. mouse.

Organism-specific databases

CTDi51569.
MGIiMGI:1915140. Ufm1.

Phylogenomic databases

eggNOGiNOG249065.
GeneTreeiENSGT00390000010391.
HOGENOMiHOG000185753.
HOVERGENiHBG094129.
InParanoidiP61961.
KOiK12162.
OMAiVTFKIIL.
OrthoDBiEOG7Q8CQW.
PhylomeDBiP61961.
TreeFamiTF312934.

Miscellaneous databases

EvolutionaryTraceiP61961.
NextBioi325858.
PROiP61961.
SOURCEiSearch...

Gene expression databases

BgeeiP61961.
CleanExiMM_UFM1.
ExpressionAtlasiP61961. baseline and differential.
GenevisibleiP61961. MM.

Family and domain databases

InterProiIPR029071. Ubiquitin-rel_dom.
IPR005375. UFM1.
[Graphical view]
PfamiPF03671. Ufm1. 1 hit.
[Graphical view]
PIRSFiPIRSF038027. Ubiquitin-like_Ufm1. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.
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].
    Strain: BALB/c and C57BL/6J.
    Tissue: Mammary gland, Pancreas, Placenta and Small intestine.
  2. "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.
  3. "Solution structure of mouse hypothetical 9.1 kDa protein, a ubiquitin-like fold."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2002) to the PDB data bank
    Cited for: STRUCTURE BY NMR.
  4. "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: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiUFM1_MOUSE
AccessioniPrimary (citable) accession number: P61961
Secondary accession number(s): Q14346
, Q3TLT0, Q542A7, Q9CPX2, Q9NZF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 24, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.