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Protein

Protein BUD31 homolog

Gene

BUD31

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

  • mRNA splicing, via spliceosome Source: GO_Central
  • positive regulation of androgen receptor activity Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BUD31 homolog
Alternative name(s):
Protein EDG-2
Protein G10 homolog
Gene namesi
Name:BUD31
Synonyms:EDG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:29629. BUD31.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: ProtInc
  • spliceosomal complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA144596513.

Polymorphism and mutation databases

BioMutaiBUD31.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 144144Protein BUD31 homologPRO_0000193897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP41223.
MaxQBiP41223.
PaxDbiP41223.
PeptideAtlasiP41223.
PRIDEiP41223.

PTM databases

iPTMnetiP41223.
PhosphoSiteiP41223.

Expressioni

Gene expression databases

BgeeiP41223.
CleanExiHS_BUD31.
ExpressionAtlasiP41223. baseline and differential.
GenevisibleiP41223. HS.

Organism-specific databases

HPAiHPA028943.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
BEND5Q7L4P63EBI-3904603,EBI-724373
KRTAP10-7P604093EBI-3904603,EBI-10172290

GO - Molecular functioni

  • nuclear hormone receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114413. 47 interactions.
IntActiP41223. 8 interactions.
MINTiMINT-3015365.
STRINGi9606.ENSP00000222969.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi60 – 656Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OEDX-ray2.79B56-70[»]
4OH6X-ray3.56B56-70[»]
4OKBX-ray2.95B56-70[»]
ProteinModelPortaliP41223.
SMRiP41223. Positions 2-143.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2 – 109Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the BUD31 (G10) family.Curated

Phylogenomic databases

eggNOGiKOG3404. Eukaryota.
COG5132. LUCA.
GeneTreeiENSGT00390000014300.
HOGENOMiHOG000235066.
HOVERGENiHBG080938.
InParanoidiP41223.
KOiK12873.
OMAiCRGCSSD.
OrthoDBiEOG72NRRM.
PhylomeDBiP41223.
TreeFamiTF105609.

Family and domain databases

InterProiIPR018230. BUD31/G10-rel_CS.
IPR001748. G10.
[Graphical view]
PANTHERiPTHR19411. PTHR19411. 1 hit.
PfamiPF01125. G10. 1 hit.
[Graphical view]
PRINTSiPR00322. G10.
PROSITEiPS00997. G10_1. 1 hit.
PS00998. G10_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P41223-1) [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
MPKVKRSRKA PPDGWELIEP TLDELDQKMR EAETEPHEGK RKVESLWPIF
60 70 80 90 100
RIHHQKTRYI FDLFYKRKAI SRELYEYCIK EGYADKNLIA KWKKQGYENL
110 120 130 140
CCLRCIQTRD TNFGTNCICR VPKSKLEVGR IIECTHCGCR GCSG
Length:144
Mass (Da):17,000
Last modified:October 10, 2002 - v2
Checksum:i520B8E74C97D0926
GO
Isoform 2 (identifier: P41223-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-144: GRIIECTHCGCRGCSG → VMSDTQAWCCFQLKILP

Note: No experimental confirmation available.
Show »
Length:145
Mass (Da):17,331
Checksum:i00598D743480CF95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → Q in AAA20008 (PubMed:7841202).Curated
Sequence conflicti12 – 121P → Q in AAB33291 (PubMed:7841202).Curated
Sequence conflicti24 – 241E → Q in AAA20008 (PubMed:7841202).Curated
Sequence conflicti24 – 241E → Q in AAB33291 (PubMed:7841202).Curated
Sequence conflicti70 – 701I → Y in AAA20008 (PubMed:7841202).Curated
Sequence conflicti70 – 701I → Y in AAB33291 (PubMed:7841202).Curated
Sequence conflicti75 – 795YEYCI → LDICY in AAA20008 (PubMed:7841202).Curated
Sequence conflicti83 – 831Y → L in AAA20008 (PubMed:7841202).Curated
Sequence conflicti83 – 831Y → L in AAB33291 (PubMed:7841202).Curated
Sequence conflicti89 – 891I → L in AAA20008 (PubMed:7841202).Curated
Sequence conflicti89 – 891I → L in AAB33291 (PubMed:7841202).Curated
Sequence conflicti97 – 982YE → IG in AAA20008 (PubMed:7841202).Curated
Sequence conflicti97 – 982YE → IG in AAB33291 (PubMed:7841202).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei129 – 14416GRIIE…RGCSG → VMSDTQAWCCFQLKILP in isoform 2. 1 PublicationVSP_055558Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11861 mRNA. Translation: AAA20008.1.
S77329 mRNA. Translation: AAB33291.1.
AK297784 mRNA. Translation: BAH12665.1.
AK316477 mRNA. Translation: BAH14848.1.
CR456951 mRNA. Translation: CAG33232.1.
AC004922 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23881.1.
CH471091 Genomic DNA. Translation: EAW76670.1.
CH471091 Genomic DNA. Translation: EAW76671.1.
CH471091 Genomic DNA. Translation: EAW76672.1.
CH471091 Genomic DNA. Translation: EAW76673.1.
BC022821 mRNA. Translation: AAH22821.1.
BC104670 mRNA. Translation: AAI04671.1.
CCDSiCCDS5663.1. [P41223-1]
PIRiS52131.
RefSeqiNP_003901.2. NM_003910.3. [P41223-1]
XP_005250727.1. XM_005250670.3. [P41223-2]
XP_005250728.1. XM_005250671.3. [P41223-2]
XP_005250731.1. XM_005250674.2. [P41223-1]
UniGeneiHs.380233.

Genome annotation databases

EnsembliENST00000222969; ENSP00000222969; ENSG00000106245. [P41223-1]
ENST00000403633; ENSP00000386023; ENSG00000106245. [P41223-1]
GeneIDi8896.
KEGGihsa:8896.
UCSCiuc003uqf.4. human. [P41223-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11861 mRNA. Translation: AAA20008.1.
S77329 mRNA. Translation: AAB33291.1.
AK297784 mRNA. Translation: BAH12665.1.
AK316477 mRNA. Translation: BAH14848.1.
CR456951 mRNA. Translation: CAG33232.1.
AC004922 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23881.1.
CH471091 Genomic DNA. Translation: EAW76670.1.
CH471091 Genomic DNA. Translation: EAW76671.1.
CH471091 Genomic DNA. Translation: EAW76672.1.
CH471091 Genomic DNA. Translation: EAW76673.1.
BC022821 mRNA. Translation: AAH22821.1.
BC104670 mRNA. Translation: AAI04671.1.
CCDSiCCDS5663.1. [P41223-1]
PIRiS52131.
RefSeqiNP_003901.2. NM_003910.3. [P41223-1]
XP_005250727.1. XM_005250670.3. [P41223-2]
XP_005250728.1. XM_005250671.3. [P41223-2]
XP_005250731.1. XM_005250674.2. [P41223-1]
UniGeneiHs.380233.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OEDX-ray2.79B56-70[»]
4OH6X-ray3.56B56-70[»]
4OKBX-ray2.95B56-70[»]
ProteinModelPortaliP41223.
SMRiP41223. Positions 2-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114413. 47 interactions.
IntActiP41223. 8 interactions.
MINTiMINT-3015365.
STRINGi9606.ENSP00000222969.

PTM databases

iPTMnetiP41223.
PhosphoSiteiP41223.

Polymorphism and mutation databases

BioMutaiBUD31.

Proteomic databases

EPDiP41223.
MaxQBiP41223.
PaxDbiP41223.
PeptideAtlasiP41223.
PRIDEiP41223.

Protocols and materials databases

DNASUi8896.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222969; ENSP00000222969; ENSG00000106245. [P41223-1]
ENST00000403633; ENSP00000386023; ENSG00000106245. [P41223-1]
GeneIDi8896.
KEGGihsa:8896.
UCSCiuc003uqf.4. human. [P41223-1]

Organism-specific databases

CTDi8896.
GeneCardsiBUD31.
HGNCiHGNC:29629. BUD31.
HPAiHPA028943.
MIMi603477. gene.
neXtProtiNX_P41223.
PharmGKBiPA144596513.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3404. Eukaryota.
COG5132. LUCA.
GeneTreeiENSGT00390000014300.
HOGENOMiHOG000235066.
HOVERGENiHBG080938.
InParanoidiP41223.
KOiK12873.
OMAiCRGCSSD.
OrthoDBiEOG72NRRM.
PhylomeDBiP41223.
TreeFamiTF105609.

Miscellaneous databases

ChiTaRSiBUD31. human.
GenomeRNAii8896.
NextBioi33411.
PROiP41223.
SOURCEiSearch...

Gene expression databases

BgeeiP41223.
CleanExiHS_BUD31.
ExpressionAtlasiP41223. baseline and differential.
GenevisibleiP41223. HS.

Family and domain databases

InterProiIPR018230. BUD31/G10-rel_CS.
IPR001748. G10.
[Graphical view]
PANTHERiPTHR19411. PTHR19411. 1 hit.
PfamiPF01125. G10. 1 hit.
[Graphical view]
PRINTSiPR00322. G10.
PROSITEiPS00997. G10_1. 1 hit.
PS00998. G10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of edg-2, a human homologue of the Xenopus maternal transcript G10 from endothelial cells."
    Hla T., Jackson A.Q., Appleby S.B., Maciag T.
    Biochim. Biophys. Acta 1260:227-229(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORM 2).
    Tissue: Thymus.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
  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] (ISOFORM 1).
    Tissue: Lymph.
  8. "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-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBUD31_HUMAN
AccessioniPrimary (citable) accession number: P41223
Secondary accession number(s): A4D274
, B7Z4S9, D6W5S6, Q6IB53, Q9UDV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 10, 2002
Last modified: April 13, 2016
This is version 134 of the entry and version 2 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.