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A0AVT1

- UBA6_HUMAN

UniProt

A0AVT1 - UBA6_HUMAN

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Protein

Ubiquitin-like modifier-activating enzyme 6

Gene

UBA6

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

Functioni

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its specificity for substrate E2 charging. Does not charge cell cycle E2s, such as CDC34. Essential for embryonic development. Required for UBD/FAT10 conjugation. Isoform 2 may play a key role in ubiquitin system and may influence spermatogenesis and male fertility.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei625 – 6251Glycyl thioester intermediateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi470 – 50031ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. FAT10 activating enzyme activity Source: UniProtKB
  3. ligase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein ubiquitination Source: UniProtKB
  2. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme 6
Short name:
Ubiquitin-activating enzyme 6
Alternative name(s):
Monocyte protein 4
Short name:
MOP-4
Ubiquitin-activating enzyme E1-like protein 2
Short name:
E1-L2
Gene namesi
Name:UBA6
Synonyms:MOP4, UBE1L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:25581. UBA6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi625 – 6251C → A or S: Impairs ubiquitin activation. 2 Publications

Organism-specific databases

PharmGKBiPA162407690.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10521052Ubiquitin-like modifier-activating enzyme 6PRO_0000277797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei544 – 5441N6-acetyllysine1 Publication
Modified residuei729 – 7291N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiA0AVT1.
PaxDbiA0AVT1.
PRIDEiA0AVT1.

PTM databases

PhosphoSiteiA0AVT1.

Expressioni

Tissue specificityi

Widely expressed. Isoform 2 is predominantly expressed in testis with higher expression in adult testis than in fetal testis.2 Publications

Gene expression databases

BgeeiA0AVT1.
ExpressionAtlasiA0AVT1. baseline and differential.
GenevestigatoriA0AVT1.

Organism-specific databases

HPAiHPA037001.
HPA044870.

Interactioni

Subunit structurei

Forms a thioester with UBD in cells stimulated with tumor necrosis factor-alpha (TNFa) and interferon-gamma (IFNg).

Protein-protein interaction databases

BioGridi120529. 45 interactions.
DIPiDIP-57633N.
IntActiA0AVT1. 1 interaction.
MINTiMINT-1195700.

Structurei

3D structure databases

ProteinModelPortaliA0AVT1.
SMRiA0AVT1. Positions 38-1019.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-activating E1 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000016689.
HOVERGENiHBG054199.
InParanoidiA0AVT1.
KOiK10699.
OMAiFSPLCQW.
OrthoDBiEOG74R1PV.
PhylomeDBiA0AVT1.
TreeFamiTF300586.

Family and domain databases

Gene3Di1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view]
PfamiPF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view]
PRINTSiPR01849. UBIQUITINACT.
SMARTiSM00985. UBA_e1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 2 hits.
TIGRFAMsiTIGR01408. Ube1. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Named isoforms=3.

Isoform 1 (identifier: A0AVT1-1) [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
MEGSEPVAAH QGEEASCSSW GTGSTNKNLP IMSTASVEID DALYSRQRYV
60 70 80 90 100
LGDTAMQKMA KSHVFLSGMG GLGLEIAKNL VLAGIKAVTI HDTEKCQAWD
110 120 130 140 150
LGTNFFLSED DVVNKRNRAE AVLKHIAELN PYVHVTSSSV PFNETTDLSF
160 170 180 190 200
LDKYQCVVLT EMKLPLQKKI NDFCRSQCPP IKFISADVHG IWSRLFCDFG
210 220 230 240 250
DEFEVLDTTG EEPKEIFISN ITQANPGIVT CLENHPHKLE TGQFLTFREI
260 270 280 290 300
NGMTGLNGSI QQITVISPFS FSIGDTTELE PYLHGGIAVQ VKTPKTVFFE
310 320 330 340 350
SLERQLKHPK CLIVDFSNPE APLEIHTAML ALDQFQEKYS RKPNVGCQQD
360 370 380 390 400
SEELLKLATS ISETLEEKPD VNADIVHWLS WTAQGFLSPL AAAVGGVASQ
410 420 430 440 450
EVLKAVTGKF SPLCQWLYLE AADIVESLGK PECEEFLPRG DRYDALRACI
460 470 480 490 500
GDTLCQKLQN LNIFLVGCGA IGCEMLKNFA LLGVGTSKEK GMITVTDPDL
510 520 530 540 550
IEKSNLNRQF LFRPHHIQKP KSYTAADATL KINSQIKIDA HLNKVCPTTE
560 570 580 590 600
TIYNDEFYTK QDVIITALDN VEARRYVDSR CLANLRPLLD SGTMGTKGHT
610 620 630 640 650
EVIVPHLTES YNSHRDPPEE EIPFCTLKSF PAAIEHTIQW ARDKFESSFS
660 670 680 690 700
HKPSLFNKFW QTYSSAEEVL QKIQSGHSLE GCFQVIKLLS RRPRNWSQCV
710 720 730 740 750
ELARLKFEKY FNHKALQLLH CFPLDIRLKD GSLFWQSPKR PPSPIKFDLN
760 770 780 790 800
EPLHLSFLQN AAKLYATVYC IPFAEEDLSA DALLNILSEV KIQEFKPSNK
810 820 830 840 850
VVQTDETARK PDHVPISSED ERNAIFQLEK AILSNEATKS DLQMAVLSFE
860 870 880 890 900
KDDDHNGHID FITAASNLRA KMYSIEPADR FKTKRIAGKI IPAIATTTAT
910 920 930 940 950
VSGLVALEMI KVTGGYPFEA YKNCFLNLAI PIVVFTETTE VRKTKIRNGI
960 970 980 990 1000
SFTIWDRWTV HGKEDFTLLD FINAVKEKYG IEPTMVVQGV KMLYVPVMPG
1010 1020 1030 1040 1050
HAKRLKLTMH KLVKPTTEKK YVDLTVSFAP DIDGDEDLPG PPVRYYFSHD

TD
Length:1,052
Mass (Da):117,970
Last modified:November 28, 2006 - v1
Checksum:i9F9C70EABA750A71
GO
Isoform 2 (identifier: A0AVT1-2) [UniParc]FASTAAdd to Basket

Also known as: nUBE1L

The sequence of this isoform differs from the canonical sequence as follows:
     1-474: Missing.

Show »
Length:578
Mass (Da):65,757
Checksum:i33FDBFF4EA8AADF0
GO
Isoform 3 (identifier: A0AVT1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     369-389: PDVNADIVHWLSWTAQGFLSP → VTIEIYGCPNICLLIHKCSVY
     390-1052: Missing.

Show »
Length:389
Mass (Da):43,216
Checksum:iE4534BE50710EF6C
GO
Isoform 4 (identifier: A0AVT1-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-340: APLEIHTAMLALDQFQEKYS → VNKHFAGLREAAESEMRISE
     341-1052: Missing.

Show »
Length:340
Mass (Da):37,693
Checksum:iB73DEE549B7E7143
GO

Sequence cautioni

The sequence BAA91824.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141E → K in CAD89908. (PubMed:17974005)Curated
Sequence conflicti140 – 1401V → A in CAD89908. (PubMed:17974005)Curated
Sequence conflicti197 – 1971C → Y in BAC04463. (PubMed:14702039)Curated
Sequence conflicti234 – 2341N → D in CAD89959. (PubMed:17974005)Curated
Sequence conflicti297 – 2971V → A in BAC04463. (PubMed:14702039)Curated
Sequence conflicti645 – 6451F → V in AAQ63403. (PubMed:15202508)Curated
Sequence conflicti803 – 8031Q → H in BAA91824. (PubMed:14702039)Curated
Sequence conflicti821 – 8211E → G in CAD89959. (PubMed:17974005)Curated
Sequence conflicti868 – 8681L → P in CAD89908. (PubMed:17974005)Curated
Sequence conflicti905 – 9051V → G in AAQ63403. (PubMed:15202508)Curated
Sequence conflicti909 – 9091M → K in CAD89959. (PubMed:17974005)Curated
Sequence conflicti920 – 9201A → V in BAB19785. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241A → T.3 Publications
Corresponds to variant rs10010188 [ dbSNP | Ensembl ].
VAR_030594

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 474474Missing in isoform 2. 1 PublicationVSP_023083Add
BLAST
Alternative sequencei321 – 34020APLEI…QEKYS → VNKHFAGLREAAESEMRISE in isoform 4. 1 PublicationVSP_023084Add
BLAST
Alternative sequencei341 – 1052712Missing in isoform 4. 1 PublicationVSP_023085Add
BLAST
Alternative sequencei369 – 38921PDVNA…GFLSP → VTIEIYGCPNICLLIHKCSV Y in isoform 3. 1 PublicationVSP_023086Add
BLAST
Alternative sequencei390 – 1052663Missing in isoform 3. 1 PublicationVSP_023087Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY359880 mRNA. Translation: AAQ63403.1.
EF623993 mRNA. Translation: ABR25253.1.
AB014773 mRNA. Translation: BAB19785.1.
AK001670 mRNA. Translation: BAA91824.1. Different initiation.
AK094969 mRNA. Translation: BAC04463.1.
AK314371 mRNA. Translation: BAG37000.1.
AL832015 mRNA. Translation: CAD89908.1.
AL832458 mRNA. Translation: CAD89959.1.
AC079880 Genomic DNA. No translation available.
AC096720 Genomic DNA. Translation: AAY40999.1.
BC031637 mRNA. Translation: AAH31637.1.
BC126484 mRNA. Translation: AAI26485.1.
BC126486 mRNA. Translation: AAI26487.1.
CCDSiCCDS3516.1. [A0AVT1-1]
RefSeqiNP_060697.4. NM_018227.5. [A0AVT1-1]
UniGeneiHs.212774.

Genome annotation databases

EnsembliENST00000322244; ENSP00000313454; ENSG00000033178. [A0AVT1-1]
ENST00000420827; ENSP00000399234; ENSG00000033178. [A0AVT1-3]
GeneIDi55236.
KEGGihsa:55236.
UCSCiuc003hdg.4. human. [A0AVT1-1]
uc003hdi.3. human. [A0AVT1-3]
uc003hdj.2. human. [A0AVT1-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY359880 mRNA. Translation: AAQ63403.1 .
EF623993 mRNA. Translation: ABR25253.1 .
AB014773 mRNA. Translation: BAB19785.1 .
AK001670 mRNA. Translation: BAA91824.1 . Different initiation.
AK094969 mRNA. Translation: BAC04463.1 .
AK314371 mRNA. Translation: BAG37000.1 .
AL832015 mRNA. Translation: CAD89908.1 .
AL832458 mRNA. Translation: CAD89959.1 .
AC079880 Genomic DNA. No translation available.
AC096720 Genomic DNA. Translation: AAY40999.1 .
BC031637 mRNA. Translation: AAH31637.1 .
BC126484 mRNA. Translation: AAI26485.1 .
BC126486 mRNA. Translation: AAI26487.1 .
CCDSi CCDS3516.1. [A0AVT1-1 ]
RefSeqi NP_060697.4. NM_018227.5. [A0AVT1-1 ]
UniGenei Hs.212774.

3D structure databases

ProteinModelPortali A0AVT1.
SMRi A0AVT1. Positions 38-1019.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120529. 45 interactions.
DIPi DIP-57633N.
IntActi A0AVT1. 1 interaction.
MINTi MINT-1195700.

Chemistry

BindingDBi A0AVT1.
ChEMBLi CHEMBL2321622.

PTM databases

PhosphoSitei A0AVT1.

Proteomic databases

MaxQBi A0AVT1.
PaxDbi A0AVT1.
PRIDEi A0AVT1.

Protocols and materials databases

DNASUi 55236.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322244 ; ENSP00000313454 ; ENSG00000033178 . [A0AVT1-1 ]
ENST00000420827 ; ENSP00000399234 ; ENSG00000033178 . [A0AVT1-3 ]
GeneIDi 55236.
KEGGi hsa:55236.
UCSCi uc003hdg.4. human. [A0AVT1-1 ]
uc003hdi.3. human. [A0AVT1-3 ]
uc003hdj.2. human. [A0AVT1-4 ]

Organism-specific databases

CTDi 55236.
GeneCardsi GC04M068481.
H-InvDB HIX0031574.
HIX0120163.
HGNCi HGNC:25581. UBA6.
HPAi HPA037001.
HPA044870.
MIMi 611361. gene.
neXtProti NX_A0AVT1.
PharmGKBi PA162407690.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00390000016689.
HOVERGENi HBG054199.
InParanoidi A0AVT1.
KOi K10699.
OMAi FSPLCQW.
OrthoDBi EOG74R1PV.
PhylomeDBi A0AVT1.
TreeFami TF300586.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi UBA6. human.
GeneWikii UBE1L2.
GenomeRNAii 55236.
NextBioi 59255.
PROi A0AVT1.
SOURCEi Search...

Gene expression databases

Bgeei A0AVT1.
ExpressionAtlasi A0AVT1. baseline and differential.
Genevestigatori A0AVT1.

Family and domain databases

Gene3Di 1.10.3240.10. 2 hits.
3.40.50.720. 4 hits.
InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
IPR018965. Ub-activating_enz_e1_C.
IPR023280. Ub-like_act_enz_cat_cys_dom.
IPR000127. UBact_repeat.
IPR019572. Ubiquitin-activating_enzyme.
IPR018075. UBQ-activ_enz_E1.
IPR000011. UBQ/SUMO-activ_enz_E1-like.
[Graphical view ]
Pfami PF00899. ThiF. 2 hits.
PF09358. UBA_e1_C. 1 hit.
PF10585. UBA_e1_thiolCys. 1 hit.
PF02134. UBACT. 1 hit.
[Graphical view ]
PRINTSi PR01849. UBIQUITINACT.
SMARTi SM00985. UBA_e1_C. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 2 hits.
TIGRFAMsi TIGR01408. Ube1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characteristics of a novel E1 like gene nUBE1L in human testis."
    Zhu H., Zhou Z.-M., Huo R., Huang X.-Y., Lu L., Lin M., Wang L.-R., Zhou Y.-D., Li J.-M., Sha J.-H.
    Acta Biochim. Biophys. Sin. 36:227-234(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
  2. "Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging."
    Jin J., Li X., Gygi S.P., Harper J.W.
    Nature 447:1135-1138(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-224, FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-625.
  3. "Molecular and biological characterization of a new ubiquitin-activating enzyme E1 like protein, MOP-4 which is highly expressed in human monocytes."
    Takayama K., Fujii Y., Ukai Y., Yoshimoto M.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: 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.
    , 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] (ISOFORMS 1 AND 4), VARIANT THR-224.
    Tissue: Hippocampus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-224.
    Tissue: Skeletal muscle.
  6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 1 AND 3).
    Tissue: Brain.
  8. "E1-L2 activates both ubiquitin and FAT10."
    Chiu Y.-H., Sun Q., Chen Z.J.
    Mol. Cell 27:1014-1023(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBD, THIOESTER FORMATION, MUTAGENESIS OF CYS-625.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBA6_HUMAN
AccessioniPrimary (citable) accession number: A0AVT1
Secondary accession number(s): A6N8M7
, B2RAV3, Q4W5K0, Q6UV21, Q86T78, Q86TC7, Q8N5T3, Q8N9E4, Q9H3T7, Q9NVC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: November 28, 2006
Last modified: November 26, 2014
This is version 86 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3