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Q9BQG0 (MBB1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myb-binding protein 1A
Gene names
Name:MYBBP1A
Synonyms:P160
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1328 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May activate or repress transcription via interactions with sequence specific DNA-binding proteins. Repression may be mediated at least in part by histone deacetylase activity (HDAC activity) By similarity.

Subunit structure

Binds to and represses JUN and MYB via the leucine zipper regions present in these proteins. Also binds to and represses PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to KPNA2. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 By similarity. Ref.7

Subcellular location

Cytoplasm. Nucleus. Nucleusnucleolus. Note: Shuttles between the nucleus and cytoplasm. Nuclear import may be mediated by KPNA2, while export appears to depend partially on XPO1/CRM1 By similarity. Predominantly nucleolar. Ref.5

Post-translational modification

Citrullinated by PADI4 By similarity.

Sequence caution

The sequence CAB66530.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionActivator
Repressor
   PTMAcetylation
Citrullination
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose starvation

Inferred from direct assay PubMed 21471221. Source: UniProtKB

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

nucleocytoplasmic transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: ProtInc

respiratory electron transport chain

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNLS-dependent protein nuclear import complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay PubMed 21471221. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21471221. Source: UniProtKB

   Molecular_functionDNA-directed DNA polymerase activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BQG0-1)

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.
Isoform 2 (identifier: Q9BQG0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1322-1328: VRKAGKP → TLRFTISSSKK
Note: May be due to competing donor and acceptor splice sites.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13281328Myb-binding protein 1A
PRO_0000096255

Regions

Region1 – 582582Interaction with MYB By similarity
Region1151 – 1328178Required for nuclear and nucleolar localization By similarity
Motif240 – 25819Nuclear export signal 1 By similarity
Motif263 – 28119Nuclear export signal 2 By similarity
Compositional bias720 – 78465Glu-rich

Amino acid modifications

Modified residue111Phosphoserine Ref.6 Ref.8 Ref.10 Ref.11 Ref.16
Modified residue711N6-acetyllysine Ref.15
Modified residue1581N6-acetyllysine Ref.15
Modified residue7751Phosphoserine Ref.6 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.18
Modified residue11591Phosphoserine Ref.11
Modified residue11631Phosphoserine Ref.8 Ref.11 Ref.16 Ref.18
Modified residue11861Phosphoserine Ref.9 Ref.11
Modified residue11901Phosphothreonine Ref.11
Modified residue11961Phosphothreonine Ref.11
Modified residue12071Phosphoserine Ref.11
Modified residue12321Phosphoserine Ref.18
Modified residue12411Phosphoserine By similarity
Modified residue12481Phosphoserine Ref.11
Modified residue12671Phosphoserine Ref.11 Ref.14 Ref.16 Ref.18
Modified residue12691Phosphothreonine Ref.18
Modified residue12901Phosphoserine Ref.10 Ref.16 Ref.18
Modified residue13031Phosphoserine Ref.11
Modified residue13071Citrulline By similarity
Modified residue13081Phosphoserine Ref.11 Ref.16
Modified residue13101Phosphoserine Ref.16
Modified residue13141Phosphoserine Ref.11 Ref.16

Natural variations

Alternative sequence1322 – 13287VRKAGKP → TLRFTISSSKK in isoform 2.
VSP_014786
Natural variant81Q → E.
Corresponds to variant rs3809849 [ dbSNP | Ensembl ].
VAR_023064
Natural variant6801H → Y.
Corresponds to variant rs899440 [ dbSNP | Ensembl ].
VAR_051156
Natural variant9581H → P.
Corresponds to variant rs879797 [ dbSNP | Ensembl ].
VAR_051157
Natural variant12081M → L.
Corresponds to variant rs9905742 [ dbSNP | Ensembl ].
VAR_051158

Experimental info

Sequence conflict3071R → H in AAF33021. Ref.1
Sequence conflict5701R → H in AAF33021. Ref.1
Sequence conflict6011L → F in AAF33021. Ref.1
Sequence conflict10281H → R in AAH50546. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 0B053465D5B3511F

FASTA1,328148,855
        10         20         30         40         50         60 
MESRDPAQPM SPGEATQSGA RPADRYGLLK HSREFLDFFW DIAKPEQETR LAATEKLLEY 

        70         80         90        100        110        120 
LRGRPKGSEM KYALKRLITG LGVGRETARP CYSLALAQLL QSFEDLPLCS ILQQIQEKYD 

       130        140        150        160        170        180 
LHQVKKAMLR PALFANLFGV LALFQSGRLV KDQEALMKSV KLLQALAQYQ NHLQEQPRKA 

       190        200        210        220        230        240 
LVDILSEVSK ATLQEILPEV LKADLNIILS SPEQLELFLL AQQKVPSKLK KLVGSVNLFS 

       250        260        270        280        290        300 
DENVPRLVNV LKMAASSVKK DRKLPAIALD LLRLALKEDK FPRFWKEVVE QGLLKMQFWP 

       310        320        330        340        350        360 
ASYLCFRLLG AALPLLTKEQ LHLVMQGDVI RHYGEHVCTA KLPKQFKFAP EMDDYVGTFL 

       370        380        390        400        410        420 
EGCQDDPERQ LAVLVAFSSV TNQGLPVTPT FWRVVRFLSP PALQGYVAWL RAMFLQPDLD 

       430        440        450        460        470        480 
SLVDFSTNNQ KKAQDSSLHM PERAVFRLRK WIIFRLVSIV DSLHLEMEEA LTEQVARFCL 

       490        500        510        520        530        540 
FHSFFVTKKP TSQIPETKHP FSFPLENQAR EAVSSAFFSL LQTLSTQFKQ APGQTQGGQP 

       550        560        570        580        590        600 
WTYHLVQFAD LLLNHSHNVT TVTPFTAQQR QAWDRMLQTL KELEAHSAEA RAAAFQHLLL 

       610        620        630        640        650        660 
LVGIHLLKSP AESCDLLGDI QTCIRKSLGE KPRRSRTKTI DPQEPPWVEV LVEILLALLA 

       670        680        690        700        710        720 
QPSHLMRQVA RSVFGHICSH LTPRALQLIL DVLNPETSED ENDRVVVTDD SDERRLKGAE 

       730        740        750        760        770        780 
DKSEEGEDNR SSESEEESEG EESEEEERDG DVDQGFREQL MTVLQAGKAL GGEDSENEEE 

       790        800        810        820        830        840 
LGDEAMMALD QSLASLFAEQ KLRIQARRDE KNKLQKEKAL RRDFQIRVLD LVEVLVTKQP 

       850        860        870        880        890        900 
ENALVLELLE PLLSIIRRSL RSSSSKQEQD LLHKTARIFT HHLCRARRYC HDLGERAGAL 

       910        920        930        940        950        960 
HAQVERLVQQ AGRQPDSPTA LYHFNASLYL LRVLKGNTAE GCVHETQEKQ KAGTDPSHMP 

       970        980        990       1000       1010       1020 
TGPQAASCLD LNLVTRVYST ALSSFLTKRN SPLTVPMFLS LFSRHPVLCQ SLLPILVQHI 

      1030       1040       1050       1060       1070       1080 
TGPVRPRHQA CLLLQKTLSM REVRSCFEDP EWKQLMGQVL AKVTENLRVL GEAQTKAQHQ 

      1090       1100       1110       1120       1130       1140 
QALSSLELLN VLFRTCKHEK LTLDLTVLLG VLQGQQQSLQ QGAHSTGSSR LHDLYWQAMK 

      1150       1160       1170       1180       1190       1200 
TLGVQRPKLE KKDAKEIPSA TQSPISKKRK KKGFLPETKK RKKRKSEDGT PAEDGTPAAT 

      1210       1220       1230       1240       1250       1260 
GGSQPPSMGR KKRNRTKAKV PAQANGTPTT KSPAPGAPTR SPSTPAKSPK LQKKNQKPSQ 

      1270       1280       1290       1300       1310       1320 
VNGAPGSPTE PAGQKQHQKA LPKKGVLGKS PLSALARKKA RLSLVIRSPS LLQSGAKKKA 


QVRKAGKP 

« Hide

Isoform 2 [UniParc].

Checksum: CF90678D49D64DB1
Show »

FASTA1,332149,367

References

« Hide 'large scale' references
[1]"Molecular cloning and chromosomal mapping of the human homologue of MYB binding protein (P160) 1A (MYBBP1A) to 17p13.3."
Keough R., Woollatt E., Crawford J., Sutherland G.R., Plummer S., Casey G., Gonda T.J.
Genomics 62:483-489(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[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] (ISOFORM 1).
Tissue: Eye.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-1328 (ISOFORM 2).
Tissue: Amygdala.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1328 (ISOFORM 1).
Tissue: Testis.
[5]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-11 AND SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-1163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-11; SER-775 AND SER-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-775; SER-1159; SER-1163; SER-1186; THR-1190; THR-1196; SER-1207; SER-1248; SER-1267; SER-1303; SER-1308 AND SER-1314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-775 AND SER-1267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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-71 AND LYS-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-11; SER-775; SER-1163; SER-1267; SER-1290; SER-1308; SER-1310 AND SER-1314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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-775; SER-1163; SER-1232; SER-1267; THR-1269 AND SER-1290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF147709 mRNA. Translation: AAF33021.1.
BC000641 mRNA. Translation: AAH00641.2.
BC050546 mRNA. Translation: AAH50546.1.
AL136595 mRNA. Translation: CAB66530.1. Different initiation.
AL133098 mRNA. Translation: CAB61409.1.
PIRT42680.
RefSeqNP_001099008.1. NM_001105538.1.
NP_055335.2. NM_014520.3.
UniGeneHs.22824.
Hs.701718.

3D structure databases

ProteinModelPortalQ9BQG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115770. 80 interactions.
IntActQ9BQG0. 29 interactions.
MINTMINT-1150245.
STRING9606.ENSP00000370968.

PTM databases

PhosphoSiteQ9BQG0.

Polymorphism databases

DMDM71153825.

2D gel databases

SWISS-2DPAGEQ9BQG0.

Proteomic databases

PaxDbQ9BQG0.
PRIDEQ9BQG0.

Protocols and materials databases

DNASU10514.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254718; ENSP00000254718; ENSG00000132382. [Q9BQG0-1]
ENST00000381556; ENSP00000370968; ENSG00000132382. [Q9BQG0-2]
GeneID10514.
KEGGhsa:10514.
UCSCuc002fxz.4. human. [Q9BQG0-2]
uc002fyb.4. human. [Q9BQG0-1]

Organism-specific databases

CTD10514.
GeneCardsGC17M004442.
H-InvDBHIX0013445.
HGNCHGNC:7546. MYBBP1A.
HPAHPA005466.
MIM604885. gene.
neXtProtNX_Q9BQG0.
PharmGKBPA31346.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313877.
HOGENOMHOG000113488.
HOVERGENHBG081961.
KOK02331.
OMAHQAQACL.
PhylomeDBQ9BQG0.
TreeFamTF317401.

Gene expression databases

BgeeQ9BQG0.
CleanExHS_MYBBP1A.
GenevestigatorQ9BQG0.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR007015. DNA_pol_V.
[Graphical view]
PANTHERPTHR13213. PTHR13213. 1 hit.
PfamPF04931. DNA_pol_phi. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
ProtoNetSearch...

Other

GeneWikiMYBBP1A.
GenomeRNAi10514.
NextBio39876.
PMAP-CutDBQ9BQG0.
PROQ9BQG0.
SOURCESearch...

Entry information

Entry nameMBB1A_HUMAN
AccessionPrimary (citable) accession number: Q9BQG0
Secondary accession number(s): Q86VM3 expand/collapse secondary AC list , Q9BW49, Q9P0V5, Q9UF99
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM