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Protein

Transmembrane and ubiquitin-like domain-containing protein 1

Gene

TMUB1

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

Functioni

Involved in sterol-regulated ubiquitination and degradation of HMG-CoA reductase HMGCR (PubMed:21343306). Involved in positive regulation of AMPA-selective glutamate receptor GRIA2 recycling to the cell surface (By similarity). Acts as negative regulator of hepatocyte growth during regeneration (By similarity).By similarity1 Publication
iHOPS: May contribute to the regulation of translation during cell-cycle progression. May contribute to the regulation of cell proliferation (By similarity). May be involved in centrosome assembly. Modulates stabilization and nucleolar localization of tumor suppressor CDKN2A and enhances association between CDKN2A and NPM1 (By similarity).By similarity

GO - Biological processi

  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Protein family/group databases

TCDBi8.A.62.1.1. the transmembrane and ubiquitin-like domain-containing protein 1 (tmub1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane and ubiquitin-like domain-containing protein 1
Alternative name(s):
Dendritic cell-derived ubiquitin-like protein
Short name:
DULP
Hepatocyte odd protein shuttling protein
Ubiquitin-like protein SB144
Cleaved into the following chain:
Gene namesi
Name:TMUB1
Synonyms:C7orf21, DULP, HOPS
ORF Names:SB144, UNQ763/PRO1555
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21709. TMUB1.

Subcellular locationi

  • Membrane By similarity; Multi-pass membrane protein By similarity
  • Cell junctionsynapsepostsynaptic cell membrane By similarity
  • Recycling endosome By similarity
  • Cytoplasm By similarity
  • Nucleus By similarity
  • Nucleusnucleolus By similarity
iHOPS :
  • Cytoplasm By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Nucleusnucleolus By similarity
  • Nucleus By similarity

  • Note: iHOPS is proposed to be the shuttling form across different cellular compartments. XPO1-dependent exported from the nucleus in dividing cells. Predominantly nuclear during growth arrest.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence analysisAdd
BLAST
Transmembranei195 – 21521HelicalSequence analysisAdd
BLAST
Transmembranei221 – 24121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Endosome, Membrane, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134863959.

Polymorphism and mutation databases

BioMutaiTMUB1.
DMDMi34922062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 246iHOPSPRO_0000435488
Chaini1 – 246246Transmembrane and ubiquitin-like domain-containing protein 1PRO_0000114922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711PhosphothreonineCombined sources
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei92 – 921PhosphothreonineCombined sources
Modified residuei98 – 981PhosphoserineCombined sources
Modified residuei127 – 1271PhosphoserineCombined sources

Post-translational modificationi

iHOPS: Processed by regulated intramembrane proteolysis (RIP)in the N-terminus to release iHOPS from membranes (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BVT8.
MaxQBiQ9BVT8.
PaxDbiQ9BVT8.
PeptideAtlasiQ9BVT8.
PRIDEiQ9BVT8.
TopDownProteomicsiQ9BVT8.

PTM databases

iPTMnetiQ9BVT8.
PhosphoSiteiQ9BVT8.

Miscellaneous databases

PMAP-CutDBQ9BVT8.

Expressioni

Tissue specificityi

Ubiquitously expressed with highest levels in mammary and thyroid glands, bone marrow and spleen; limited expression in cardiac, pancreatic and ovarian tissues.1 Publication

Gene expression databases

BgeeiQ9BVT8.
CleanExiHS_TMUB1.
ExpressionAtlasiQ9BVT8. baseline and differential.
GenevisibleiQ9BVT8. HS.

Organism-specific databases

HPAiHPA029429.

Interactioni

Subunit structurei

Interacts with EEF1A1, GRIA2, GRIP1, CAMLG, TUBG1 (By similarity). Interacts with NPM1 and CDKN2A; TMUB1 can enhance interaction between NPM1 and CDKN2A and is proposed to bridge the proteins; proposed to be mediated by iHOPS (By similarity). Interacts with ERLIN2 and AMFR; TMUB1 promotes the interaction of ERLIN2 with AMFR (PubMed:21343306).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ERLIN2O949055EBI-11425701,EBI-4400770

Protein-protein interaction databases

BioGridi123686. 29 interactions.
IntActiQ9BVT8. 4 interactions.
STRINGi9606.ENSP00000297533.

Structurei

3D structure databases

ProteinModelPortaliQ9BVT8.
SMRiQ9BVT8. Positions 105-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 17674Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 3029Required to release iHOPS from membranesBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IG1T. Eukaryota.
ENOG4111WH7. LUCA.
GeneTreeiENSGT00390000014069.
HOGENOMiHOG000232067.
HOVERGENiHBG050920.
InParanoidiQ9BVT8.
OMAiHQVRLIY.
OrthoDBiEOG7TF7B5.
PhylomeDBiQ9BVT8.
TreeFamiTF329265.

Family and domain databases

InterProiIPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BVT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLIEGVGDE VTVLFSVLAC LLVLALAWVS THTAEGGDPL PQPSGTPTPS
60 70 80 90 100
QPSAAMAATD SMRGEAPGAE TPSLRHRGQA AQPEPSTGFT ATPPAPDSPQ
110 120 130 140 150
EPLVLRLKFL NDSEQVARAW PHDTIGSLKR TQFPGREQQV RLIYQGQLLG
160 170 180 190 200
DDTQTLGSLH LPPNCVLHCH VSTRVGPPNP PCPPGSEPGP SGLEIGSLLL
210 220 230 240
PLLLLLLLLL WYCQIQYRPF FPLTATLGLA GFTLLLSLLA FAMYRP
Length:246
Mass (Da):26,261
Last modified:June 1, 2001 - v1
Checksum:iE08E25A6B37665B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY603380 mRNA. Translation: AAU00156.1.
AY037155 mRNA. Translation: AAK67645.1.
AY358481 mRNA. Translation: AAQ88845.1.
AK314035 mRNA. Translation: BAG36745.1.
AC010973 Genomic DNA. No translation available.
CH471173 Genomic DNA. Translation: EAW54030.1.
CH471173 Genomic DNA. Translation: EAW54032.1.
BC000936 mRNA. Translation: AAH00936.1.
BC033182 mRNA. Translation: AAH33182.1.
CCDSiCCDS5920.1.
RefSeqiNP_001129516.1. NM_001136044.1.
NP_113622.1. NM_031434.3.
UniGeneiHs.726215.

Genome annotation databases

EnsembliENST00000297533; ENSP00000297533; ENSG00000164897.
ENST00000392818; ENSP00000376565; ENSG00000164897.
ENST00000462940; ENSP00000417519; ENSG00000164897.
ENST00000476627; ENSP00000419214; ENSG00000164897.
ENST00000482202; ENSP00000418709; ENSG00000164897.
GeneIDi83590.
KEGGihsa:83590.
UCSCiuc003wjb.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY603380 mRNA. Translation: AAU00156.1.
AY037155 mRNA. Translation: AAK67645.1.
AY358481 mRNA. Translation: AAQ88845.1.
AK314035 mRNA. Translation: BAG36745.1.
AC010973 Genomic DNA. No translation available.
CH471173 Genomic DNA. Translation: EAW54030.1.
CH471173 Genomic DNA. Translation: EAW54032.1.
BC000936 mRNA. Translation: AAH00936.1.
BC033182 mRNA. Translation: AAH33182.1.
CCDSiCCDS5920.1.
RefSeqiNP_001129516.1. NM_001136044.1.
NP_113622.1. NM_031434.3.
UniGeneiHs.726215.

3D structure databases

ProteinModelPortaliQ9BVT8.
SMRiQ9BVT8. Positions 105-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123686. 29 interactions.
IntActiQ9BVT8. 4 interactions.
STRINGi9606.ENSP00000297533.

Protein family/group databases

TCDBi8.A.62.1.1. the transmembrane and ubiquitin-like domain-containing protein 1 (tmub1) family.

PTM databases

iPTMnetiQ9BVT8.
PhosphoSiteiQ9BVT8.

Polymorphism and mutation databases

BioMutaiTMUB1.
DMDMi34922062.

Proteomic databases

EPDiQ9BVT8.
MaxQBiQ9BVT8.
PaxDbiQ9BVT8.
PeptideAtlasiQ9BVT8.
PRIDEiQ9BVT8.
TopDownProteomicsiQ9BVT8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297533; ENSP00000297533; ENSG00000164897.
ENST00000392818; ENSP00000376565; ENSG00000164897.
ENST00000462940; ENSP00000417519; ENSG00000164897.
ENST00000476627; ENSP00000419214; ENSG00000164897.
ENST00000482202; ENSP00000418709; ENSG00000164897.
GeneIDi83590.
KEGGihsa:83590.
UCSCiuc003wjb.4. human.

Organism-specific databases

CTDi83590.
GeneCardsiTMUB1.
HGNCiHGNC:21709. TMUB1.
HPAiHPA029429.
MIMi614792. gene.
neXtProtiNX_Q9BVT8.
PharmGKBiPA134863959.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG1T. Eukaryota.
ENOG4111WH7. LUCA.
GeneTreeiENSGT00390000014069.
HOGENOMiHOG000232067.
HOVERGENiHBG050920.
InParanoidiQ9BVT8.
OMAiHQVRLIY.
OrthoDBiEOG7TF7B5.
PhylomeDBiQ9BVT8.
TreeFamiTF329265.

Miscellaneous databases

ChiTaRSiTMUB1. human.
GenomeRNAii83590.
PMAP-CutDBQ9BVT8.
PROiQ9BVT8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BVT8.
CleanExiHS_TMUB1.
ExpressionAtlasiQ9BVT8. baseline and differential.
GenevisibleiQ9BVT8. HS.

Family and domain databases

InterProiIPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HOPS: a novel cAMP-dependent shuttling protein involved in protein synthesis regulation."
    Della Fazia M.A., Castelli M., Bartoli D., Pieroni S., Pettirossi V., Piobbico D., Viola-Magni M., Servillo G.
    J. Cell Sci. 118:3185-3194(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and characterization of DULP, a novel ubiquitin-like molecule from human dendritic cells."
    Liu G.Y., Liu S.X., Li P., Tang L., Han Y.M., An H.Z., Li J.Y., Dai X.K., Li N., Cao X.T., Yu Y.Z.
    Cell. Mol. Immunol. 6:27-33(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Tissue: Dendritic cell.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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.
    , 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].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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].
    Tissue: Kidney and Placenta.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; THR-92 AND SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase."
    Jo Y., Sguigna P.V., DeBose-Boyd R.A.
    J. Biol. Chem. 286:15022-15031(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERLIN2 AND AMFR.
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-73 AND SER-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  13. "Different functions of HOPS isoforms in the cell: HOPS shuttling isoform is determined by RIP cleavage system."
    Castelli M., Piobbico D., Bartoli D., Pieroni S., Brunacci C., Bellet M.M., Chiacchiaretta M., Della Fazia M.A., Servillo G.
    Cell Cycle 13:293-302(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiTMUB1_HUMAN
AccessioniPrimary (citable) accession number: Q9BVT8
Secondary accession number(s): D3DX06, Q53AQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 122 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.