Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

PAX3- and PAX7-binding protein 1

Gene

PAXBP1

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

Functioni

Adapter protein linking the transcription factors PAX3 and PAX7 to the histone methylation machinery and involved in myogenesis. Associates with a histone methyltransferase complex that specifically mediates dimethylation and trimethylation of 'Lys-4' of histone H3. Mediates the recruitment of that complex to the transcription factors PAX3 and PAX7 on chromatin to regulate the expression of genes involved in muscle progenitor cells proliferation including ID3 and CDC20 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
PAX3- and PAX7-binding protein 1
Alternative name(s):
GC-rich sequence DNA-binding factor 1
Gene namesi
Name:PAXBP1
Synonyms:C21orf66, GCFC, GCFC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:13579. PAXBP1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25861.

Polymorphism and mutation databases

BioMutaiPAXBP1.
DMDMi20141448.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 917917PAX3- and PAX7-binding protein 1PRO_0000087439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Cross-linki149 – 149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki149 – 149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei155 – 1551PhosphoserineCombined sources
Modified residuei158 – 1581PhosphoserineCombined sources
Modified residuei191 – 1911PhosphoserineCombined sources
Modified residuei262 – 2621PhosphoserineCombined sources
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei557 – 5571PhosphoserineCombined sources
Modified residuei558 – 5581PhosphoserineCombined sources
Modified residuei563 – 5631PhosphothreonineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y5B6.
MaxQBiQ9Y5B6.
PaxDbiQ9Y5B6.
PeptideAtlasiQ9Y5B6.
PRIDEiQ9Y5B6.

PTM databases

iPTMnetiQ9Y5B6.
PhosphoSiteiQ9Y5B6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9Y5B6.
CleanExiHS_C21orf66.
ExpressionAtlasiQ9Y5B6. baseline and differential.
GenevisibleiQ9Y5B6. HS.

Organism-specific databases

HPAiHPA003757.
HPA039984.

Interactioni

Subunit structurei

Interacts with PAX3 and PAX7. Interacts with WDR5; associates with a histone methyltransferase (HMT) complex composed at least of RBBP5, ASH2L, SET1, SET2 and KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4 through direct interaction with WDR5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi125115. 22 interactions.
IntActiQ9Y5B6. 6 interactions.
MINTiMINT-2823834.
STRINGi9606.ENSP00000328992.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5B6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni378 – 558181Necessary and sufficient for interaction with PAX7By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the GCF family.Curated

Phylogenomic databases

eggNOGiKOG2136. Eukaryota.
ENOG410YU43. LUCA.
GeneTreeiENSGT00390000000455.
HOGENOMiHOG000043757.
HOVERGENiHBG005817.
InParanoidiQ9Y5B6.
KOiK13211.
OMAiPMSQASI.
PhylomeDBiQ9Y5B6.
TreeFamiTF315109.

Family and domain databases

InterProiIPR012890. GCFC.
IPR022783. GCFC_dom.
[Graphical view]
PANTHERiPTHR12214. PTHR12214. 2 hits.
PfamiPF07842. GCFC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y5B6-1) [UniParc]FASTAAdd to basket

Also known as: A

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
MFRKARRVNV RKRNDSEEEE RERDEEQEPP PLLPPPGTGE EAGPGGGDRA
60 70 80 90 100
PGGESLLGPG PSPPSALTPG LGAEAGGGFP GGAEPGNGLK PRKRPRENKE
110 120 130 140 150
VPRASLLSFQ DEEEENEEVF KVKKSSYSKK IVKLLKKEYK EDLEKSKIKT
160 170 180 190 200
ELNSSAESEQ PLDKTGHVKD TNQEDGVIIS EHGEDEMDME SEKEEEKPKT
210 220 230 240 250
GGAFSNALSS LNVLRPGEIP DAAFIHAARK KRQMARELGD FTPHDNEPGK
260 270 280 290 300
GRLVREDEND ASDDEDDDEK RRIVFSVKEK SQRQKIAEEI GIEGSDDDAL
310 320 330 340 350
VTGEQDEELS RWEQEQIRKG INIPQVQASQ PAEVNMYYQN TYQTMPYGSS
360 370 380 390 400
YGIPYSYTAY GSSDAKSQKT DNTVPFKTPS NEMTPVTIDL VKKQLKDRLD
410 420 430 440 450
SMKELHKTNR QQHEKHLQSR VDSTRAIERL EGSSGGIGER YKFLQEMRGY
460 470 480 490 500
VQDLLECFSE KVPLINELES AIHQLYKQRA SRLVQRRQDD IKDESSEFSS
510 520 530 540 550
HSNKALMAPN LDSFGRDRAL YQEHAKRRIA EREARRTRRR QAREQTGKMA
560 570 580 590 600
DHLEGLSSDD EETSTDITNF NLEKDRISKE SGKVFEDVLE SFYSIDCIKS
610 620 630 640 650
QFEAWRSKYY TSYKDAYIGL CLPKLFNPLI RLQLLTWTPL EAKCRDFENM
660 670 680 690 700
LWFESLLFYG CEEREQEKDD VDVALLPTIV EKVILPKLTV IAENMWDPFS
710 720 730 740 750
TTQTSRMVGI TLKLINGYPS VVNAENKNTQ VYLKALLLRM RRTLDDDVFM
760 770 780 790 800
PLYPKNVLEN KNSGPYLFFQ RQFWSSVKLL GNFLQWYGIF SNKTLQELSI
810 820 830 840 850
DGLLNRYILM AFQNSEYGDD SIKKAQNVIN CFPKQWFMNL KGERTISQLE
860 870 880 890 900
NFCRYLVHLA DTIYRNSIGC SDVEKRNARE NIKQIVKLLA SVRALDHAMS
910
VASDHNVKEF KSLIEGK
Length:917
Mass (Da):104,804
Last modified:December 19, 2001 - v2
Checksum:i855960A1D50A7789
GO
Isoform 2 (identifier: Q9Y5B6-2) [UniParc]FASTAAdd to basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     779-917: LLGNFLQWYG...KEFKSLIEGK → VIKPPFQRGS...WTDRPCVVFS

Show »
Length:815
Mass (Da):93,170
Checksum:iA2843B97BBEA753E
GO
Isoform 3 (identifier: Q9Y5B6-3) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     462-469: VPLINELE → SVQFRKLL
     470-917: Missing.

Show »
Length:469
Mass (Da):52,611
Checksum:i96B04F480DFFAEDD
GO
Isoform 4 (identifier: Q9Y5B6-4) [UniParc]FASTAAdd to basket

Also known as: D

The sequence of this isoform differs from the canonical sequence as follows:
     503-511: NKALMAPNL → SQSILKTKL
     512-917: Missing.

Note: Most abundantly expressed isoform, at mRNA level according to PubMed:11707072, despite the presence of a premature stop codon in the mRNA that may lead to nonsense-mediated mRNA decay.
Show »
Length:511
Mass (Da):57,431
Checksum:i2D90273749BD50FE
GO

Sequence cautioni

The sequence AAD34617.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti692 – 71120Missing in AAD34617 (Ref. 5) CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei462 – 4698VPLINELE → SVQFRKLL in isoform 3. 1 PublicationVSP_004263
Alternative sequencei470 – 917448Missing in isoform 3. 1 PublicationVSP_004264Add
BLAST
Alternative sequencei503 – 5119NKALMAPNL → SQSILKTKL in isoform 4. 2 PublicationsVSP_004265
Alternative sequencei512 – 917406Missing in isoform 4. 2 PublicationsVSP_004266Add
BLAST
Alternative sequencei779 – 917139LLGNF…LIEGK → VIKPPFQRGSCPIPRRKECC SERPRRIWTDRPCVVFS in isoform 2. 2 PublicationsVSP_004267Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033903 mRNA. Translation: AAK68721.1.
AY033904 mRNA. Translation: AAK68722.1.
AY033905 mRNA. Translation: AAK68723.1.
AY033906 mRNA. Translation: AAK68724.1.
AJ279080 mRNA. Translation: CAC40813.1.
AJ279081 mRNA. Translation: CAC40814.1.
CH471079 Genomic DNA. Translation: EAX09859.1.
CH471079 Genomic DNA. Translation: EAX09861.1.
AF231920 mRNA. Translation: AAF72944.1.
AF153208 mRNA. Translation: AAD34617.1. Sequence problems.
CCDSiCCDS13619.1. [Q9Y5B6-1]
CCDS33541.1. [Q9Y5B6-2]
RefSeqiNP_037461.2. NM_013329.3. [Q9Y5B6-2]
NP_057715.2. NM_016631.3. [Q9Y5B6-1]
UniGeneiHs.644004.

Genome annotation databases

EnsembliENST00000290178; ENSP00000290178; ENSG00000159086. [Q9Y5B6-2]
ENST00000331923; ENSP00000328992; ENSG00000159086. [Q9Y5B6-1]
ENST00000443785; ENSP00000393038; ENSG00000159086. [Q9Y5B6-4]
ENST00000573680; ENSP00000458892; ENSG00000263141.
ENST00000574159; ENSP00000458262; ENSG00000263141.
GeneIDi94104.
KEGGihsa:94104.
UCSCiuc002yqn.3. human. [Q9Y5B6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033903 mRNA. Translation: AAK68721.1.
AY033904 mRNA. Translation: AAK68722.1.
AY033905 mRNA. Translation: AAK68723.1.
AY033906 mRNA. Translation: AAK68724.1.
AJ279080 mRNA. Translation: CAC40813.1.
AJ279081 mRNA. Translation: CAC40814.1.
CH471079 Genomic DNA. Translation: EAX09859.1.
CH471079 Genomic DNA. Translation: EAX09861.1.
AF231920 mRNA. Translation: AAF72944.1.
AF153208 mRNA. Translation: AAD34617.1. Sequence problems.
CCDSiCCDS13619.1. [Q9Y5B6-1]
CCDS33541.1. [Q9Y5B6-2]
RefSeqiNP_037461.2. NM_013329.3. [Q9Y5B6-2]
NP_057715.2. NM_016631.3. [Q9Y5B6-1]
UniGeneiHs.644004.

3D structure databases

ProteinModelPortaliQ9Y5B6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125115. 22 interactions.
IntActiQ9Y5B6. 6 interactions.
MINTiMINT-2823834.
STRINGi9606.ENSP00000328992.

PTM databases

iPTMnetiQ9Y5B6.
PhosphoSiteiQ9Y5B6.

Polymorphism and mutation databases

BioMutaiPAXBP1.
DMDMi20141448.

Proteomic databases

EPDiQ9Y5B6.
MaxQBiQ9Y5B6.
PaxDbiQ9Y5B6.
PeptideAtlasiQ9Y5B6.
PRIDEiQ9Y5B6.

Protocols and materials databases

DNASUi94104.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290178; ENSP00000290178; ENSG00000159086. [Q9Y5B6-2]
ENST00000331923; ENSP00000328992; ENSG00000159086. [Q9Y5B6-1]
ENST00000443785; ENSP00000393038; ENSG00000159086. [Q9Y5B6-4]
ENST00000573680; ENSP00000458892; ENSG00000263141.
ENST00000574159; ENSP00000458262; ENSG00000263141.
GeneIDi94104.
KEGGihsa:94104.
UCSCiuc002yqn.3. human. [Q9Y5B6-1]

Organism-specific databases

CTDi94104.
GeneCardsiPAXBP1.
HGNCiHGNC:13579. PAXBP1.
HPAiHPA003757.
HPA039984.
neXtProtiNX_Q9Y5B6.
PharmGKBiPA25861.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2136. Eukaryota.
ENOG410YU43. LUCA.
GeneTreeiENSGT00390000000455.
HOGENOMiHOG000043757.
HOVERGENiHBG005817.
InParanoidiQ9Y5B6.
KOiK13211.
OMAiPMSQASI.
PhylomeDBiQ9Y5B6.
TreeFamiTF315109.

Miscellaneous databases

GeneWikiiC21orf66.
GenomeRNAii94104.
PROiQ9Y5B6.

Gene expression databases

BgeeiQ9Y5B6.
CleanExiHS_C21orf66.
ExpressionAtlasiQ9Y5B6. baseline and differential.
GenevisibleiQ9Y5B6. HS.

Family and domain databases

InterProiIPR012890. GCFC.
IPR022783. GCFC_dom.
[Graphical view]
PANTHERiPTHR12214. PTHR12214. 2 hits.
PfamiPF07842. GCFC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "From PREDs and open reading frames to cDNA isolation: revisiting the human chromosome 21 transcription map."
    Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.
    Genomics 78:46-54(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY.
  2. "Isolation and initial characterization of a putative human chromosome 21 transcription factor."
    Chapot-Skovsgaard F.M., Guipponi M., Lyle R., Antonarakis S.E.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
    Tissue: Brain, Heart, Kidney, Lung, Muscle, Placenta and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Criteria for gene identification and features of genome organization: analysis of 6.5 Mb of DNA sequence from human chromosome 21."
    Slavov D., Hattori M., Sakaki Y., Rosenthal A., Shimizu N., Minoshima S., Kudoh J., Yaspo M.-L., Ramser J., Reinhardt R., Reimer C., Clancy K., Rynditch A., Gardiner K.
    Gene 247:215-232(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-917 (ISOFORM 1).
  5. "Cloning of candidate of GC-rich sequence DNA-binding factor."
    Teramoto T., Thorgeirsson S.S.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 489-815 (ISOFORM 2).
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-155; SER-158; SER-557 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-557 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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 SER-16; SER-154; SER-155; SER-158; SER-262; SER-295; SER-557 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-154; SER-155; SER-262; SER-557 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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 SER-154; SER-155; SER-191; SER-262; SER-557 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPAXB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5B6
Secondary accession number(s): D3DSE7, Q96DU8, Q9NYQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 19, 2001
Last modified: July 6, 2016
This is version 139 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  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.