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

Ankyrin repeat domain-containing protein 11

Gene

ANKRD11

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

Functioni

Chromatin regulator which modulates histone acetylation and gene expression in neural precursor cells (By similarity). May recruit histone deacetylases (HDACs) to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation (PubMed:15184363). Has a role in proliferation and development of cortical neural precursors (PubMed:25556659). May also regulate bone homeostasis (By similarity).By similarity2 Publications

GO - Biological processi

  • bone development Source: Ensembl
  • face morphogenesis Source: MGI
  • in utero embryonic development Source: Ensembl
  • multicellular organism growth Source: Ensembl
  • odontogenesis of dentin-containing tooth Source: MGI
  • skeletal system morphogenesis Source: MGI
  • tissue homeostasis Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin repeat domain-containing protein 11
Alternative name(s):
Ankyrin repeat-containing cofactor 1
Gene namesi
Name:ANKRD11
Synonyms:ANCO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:21316. ANKRD11.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

KBG syndrome (KBGS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by macrodontia of the upper central incisors, distinctive craniofacial findings, short stature, skeletal anomalies, and neurologic involvement that includes global developmental delay, seizures, and intellectual disability.
See also OMIM:148050
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2512 – 25121R → Q in KBGS; unknown pathological significance. 1 Publication
VAR_075870

Keywords - Diseasei

Disease mutation, Dwarfism, Mental retardation

Organism-specific databases

MalaCardsiANKRD11.
MIMi148050. phenotype.
Orphaneti261250. 16q24.3 microdeletion syndrome.
2332. KBG syndrome.
PharmGKBiPA134861925.

Polymorphism and mutation databases

BioMutaiANKRD11.
DMDMi296439440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26632663Ankyrin repeat domain-containing protein 11PRO_0000066907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei408 – 4081PhosphoserineCombined sources
Modified residuei410 – 4101PhosphothreonineCombined sources
Modified residuei411 – 4111PhosphoserineCombined sources
Modified residuei834 – 8341PhosphoserineCombined sources
Modified residuei1079 – 10791PhosphoserineBy similarity
Modified residuei1120 – 11201PhosphothreonineCombined sources
Modified residuei1123 – 11231PhosphoserineCombined sources
Modified residuei1419 – 14191PhosphothreonineCombined sources
Modified residuei1509 – 15091PhosphoserineCombined sources
Modified residuei1692 – 16921PhosphoserineBy similarity
Modified residuei1792 – 17921PhosphoserineCombined sources
Modified residuei1847 – 18471PhosphoserineCombined sources
Modified residuei1850 – 18501PhosphotyrosineBy similarity
Modified residuei1851 – 18511PhosphotyrosineBy similarity
Modified residuei1852 – 18521PhosphoserineBy similarity
Modified residuei1859 – 18591PhosphoserineCombined sources
Modified residuei1990 – 19901PhosphoserineCombined sources

Post-translational modificationi

Subject to proteasomal degradation which is probably essential to regulate its activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6UB99.
MaxQBiQ6UB99.
PaxDbiQ6UB99.
PeptideAtlasiQ6UB99.
PRIDEiQ6UB99.

PTM databases

iPTMnetiQ6UB99.
PhosphoSiteiQ6UB99.

Expressioni

Developmental stagei

Expression levels are regulated during the cell cycle, reaching maximal levels at M phase and then rapidly declining after late M phase.1 Publication

Gene expression databases

BgeeiQ6UB99.
CleanExiHS_ANKRD11.
ExpressionAtlasiQ6UB99. baseline and differential.
GenevisibleiQ6UB99. HS.

Organism-specific databases

HPAiCAB019288.
HPA041593.
HPA049470.

Interactioni

Subunit structurei

Interacts with the PAS region of the p160 coactivators.1 Publication

Protein-protein interaction databases

BioGridi118888. 25 interactions.
IntActiQ6UB99. 16 interactions.
STRINGi9606.ENSP00000301030.

Structurei

3D structure databases

ProteinModelPortaliQ6UB99.
SMRiQ6UB99. Positions 114-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati167 – 19630ANK 1Add
BLAST
Repeati200 – 22930ANK 2Add
BLAST
Repeati233 – 26230ANK 3Add
BLAST
Repeati266 – 29227ANK 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2369 – 2663295Important for protein degradation1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi478 – 588111Ser-richAdd
BLAST
Compositional biasi621 – 16551035Lys-richAdd
BLAST
Compositional biasi1824 – 2365542Pro-richAdd
BLAST

Sequence similaritiesi

Contains 4 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiENOG410IJ47. Eukaryota.
ENOG4110UQU. LUCA.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000168254.
HOVERGENiHBG106759.
InParanoidiQ6UB99.
OMAiEYEDSKQ.
OrthoDBiEOG7SBNMV.
PhylomeDBiQ6UB99.
TreeFamiTF326440.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6UB99-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKGGCPKAP QQEELPLSSD MVEKQTGKKD KDKVSLTKTP KLERGDGGKE
60 70 80 90 100
VRERASKRKL PFTAGANGEQ KDSDTEKQGP ERKRIKKEPV TRKAGLLFGM
110 120 130 140 150
GLSGIRAGYP LSERQQVALL MQMTAEESAN SPVDTTPKHP SQSTVCQKGT
160 170 180 190 200
PNSASKTKDK VNKRNERGET RLHRAAIRGD ARRIKELISE GADVNVKDFA
210 220 230 240 250
GWTALHEACN RGYYDVAKQL LAAGAEVNTK GLDDDTPLHD AANNGHYKVV
260 270 280 290 300
KLLLRYGGNP QQSNRKGETP LKVANSPTMV NLLLGKGTYT SSEESSTESS
310 320 330 340 350
EEEDAPSFAP SSSVDGNNTD SEFEKGLKHK AKNPEPQKAT APVKDEYEFD
360 370 380 390 400
EDDEQDRVPP VDDKHLLKKD YRKETKSNSF ISIPKMEVKS YTKNNTIAPK
410 420 430 440 450
KASHRILSDT SDEEDASVTV GTGEKLRLSA HTILPGSKTR EPSNAKQQKE
460 470 480 490 500
KNKVKKKRKK ETKGREVRFG KRSDKFCSSE SESESSESGE DDRDSLGSSG
510 520 530 540 550
CLKGSPLVLK DPSLFSSLSA SSTSSHGSSA AQKQNPSHTD QHTKHWRTDN
560 570 580 590 600
WKTISSPAWS EVSSLSDSTR TRLTSESDYS SEGSSVESLK PVRKRQEHRK
610 620 630 640 650
RASLSEKKSP FLSSAEGAVP KLDKEGKVVK KHKTKHKHKN KEKGQCSISQ
660 670 680 690 700
ELKLKSFTYE YEDSKQKSDK AILLENDLST ENKLKVLKHD RDHFKKEEKL
710 720 730 740 750
SKMKLEEKEW LFKDEKSLKR IKDTNKDISR SFREEKDRSN KAEKERSLKE
760 770 780 790 800
KSPKEEKLRL YKEERKKKSK DRPSKLEKKN DLKEDKISKE KEKIFKEDKE
810 820 830 840 850
KLKKEKVYRE DSAFDEYCNK NQFLENEDTK FSLSDDQRDR WFSDLSDSSF
860 870 880 890 900
DFKGEDSWDS PVTDYRDMKS DSVAKLILET VKEDSKERRR DSRAREKRDY
910 920 930 940 950
REPFFRKKDR DYLDKNSEKR KEQTEKHKSV PGYLSEKDKK RRESAEAGRD
960 970 980 990 1000
RKDALESCKE RRDGRAKPEE AHREELKECG CESGFKDKSD GDFGKGLEPW
1010 1020 1030 1040 1050
ERHHPAREKE KKDGPDKERK EKTKPERYKE KSSDKDKSEK SILEKCQKDK
1060 1070 1080 1090 1100
EFDKCFKEKK DTKEKHKDTH GKDKERKASL DQGKEKKEKA FPGIISEDFS
1110 1120 1130 1140 1150
EKKDDKKGKE KSWYIADIFT DESEDDRDSC MGSGFKMGEA SDLPRTDGLQ
1160 1170 1180 1190 1200
EKEEGREAYA SDRHRKSSDK QHPERQKDKE PRDRRKDRGA ADAGRDKKEK
1210 1220 1230 1240 1250
VFEKHKEKKD KESTEKYKDR KDRASVDSTQ DKKNKQKLPE KAEKKHAAED
1260 1270 1280 1290 1300
KAKSKHKEKS DKEHSKERKS SRSADAEKSL LEKLEEEALH EYREDSNDKI
1310 1320 1330 1340 1350
SEVSSDSFTD RGQEPGLTAF LEVSFTEPPG DDKPRESACL PEKLKEKERH
1360 1370 1380 1390 1400
RHSSSSSKKS HDRERAKKEK AEKKEKGEDY KEGGSRKDSG QYEKDFLEAD
1410 1420 1430 1440 1450
AYGVSYNMKA DIEDELDKTI ELFSTEKKDK NDSEREPSKK IEKELKPYGS
1460 1470 1480 1490 1500
SAINILKEKK KREKHREKWR DEKERHRDRH ADGLLRHHRD ELLRHHRDEQ
1510 1520 1530 1540 1550
KPATRDKDSP PRVLKDKSRD EGPRLGDAKL KEKFKDGAEK EKGDPVKMSN
1560 1570 1580 1590 1600
GNDKVAPSKD PGKKDARPRE KLLGDGDLMM TSFERMLSQK DLEIEERHKR
1610 1620 1630 1640 1650
HKERMKQMEK LRHRSGDPKL KEKAKPADDG RKKGLDIPAK KPPGLDPPFK
1660 1670 1680 1690 1700
DKKLKESTPI PPAAENKLHP ASGADSKDWL AGPHMKEVLP ASPRPDQSRP
1710 1720 1730 1740 1750
TGVPTPTSVL SCPSYEEVMH TPRTPSCSAD DYADLVFDCA DSQHSTPVPT
1760 1770 1780 1790 1800
APTSACSPSF FDRFSVASSG LSENASQAPA RPLSTNLYRS VSVDIRRTPE
1810 1820 1830 1840 1850
EEFSVGDKLF RQQSVPAASS YDSPMPPSME DRAPLPPVPA EKFACLSPGY
1860 1870 1880 1890 1900
YSPDYGLPSP KVDALHCPPA AVVTVTPSPE GVFSSLQAKP SPSPRAELLV
1910 1920 1930 1940 1950
PSLEGALPPD LDTSEDQQAT AAIIPPEPSY LEPLDEGPFS AVITEEPVEW
1960 1970 1980 1990 2000
AHPSEQALAS SLIGGTSENP VSWPVGSDLL LKSPQRFPES PKRFCPADPL
2010 2020 2030 2040 2050
HSAAPGPFSA SEAPYPAPPA SPAPYALPVA EPGLEDVKDG VDAVPAAIST
2060 2070 2080 2090 2100
SEAAPYAPPS GLESFFSNCK SLPEAPLDVA PEPACVAAVA QVEALGPLEN
2110 2120 2130 2140 2150
SFLDGSRGLS HLGQVEPVPW ADAFAGPEDD LDLGPFSLPE LPLQTKDAAD
2160 2170 2180 2190 2200
GEAEPVEESL APPEEMPPGA PGVINGGDVS TVVAEEPPAL PPDQASTRLP
2210 2220 2230 2240 2250
AELEPEPSGE PKLDVALEAA VEAETVPEER ARGDPDSSVE PAPVPPEQRP
2260 2270 2280 2290 2300
LGSGDQGAEA EGPPAASLCA PDGPAPNTVA QAQAADGAGP EDDTEASRAA
2310 2320 2330 2340 2350
APAEGPPGGI QPEAAEPKPT AEAPKAPRVE EIPQRMTRNR AQMLANQSKQ
2360 2370 2380 2390 2400
GPPPSEKECA PTPAPVTRAK ARGSEDDDAQ AQHPRKRRFQ RSTQQLQQQL
2410 2420 2430 2440 2450
NTSTQQTREV IQQTLAAIVD AIKLDAIEPY HSDRANPYFE YLQIRKKIEE
2460 2470 2480 2490 2500
KRKILCCITP QAPQCYAEYV TYTGSYLLDG KPLSKLHIPV IAPPPSLAEP
2510 2520 2530 2540 2550
LKELFRQQEA VRGKLRLQHS IEREKLIVSC EQEILRVHCR AARTIANQAV
2560 2570 2580 2590 2600
PFSACTMLLD SEVYNMPLES QGDENKSVRD RFNARQFISW LQDVDDKYDR
2610 2620 2630 2640 2650
MKTCLLMRQQ HEAAALNAVQ RMEWQLKVQE LDPAGHKSLC VNEVPSFYVP
2660
MVDVNDDFVL LPA
Length:2,663
Mass (Da):297,913
Last modified:May 18, 2010 - v3
Checksum:i845B04094AF37CFE
GO

Sequence cautioni

The sequence AAH69013.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761E → EE in AAR25661 (Ref. 1) Curated
Sequence conflicti971 – 9711A → V in AAR25661 (Ref. 1) Curated
Sequence conflicti971 – 9711A → V in AAS45544 (PubMed:15184363).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2512 – 25121R → Q in KBGS; unknown pathological significance. 1 Publication
VAR_075870

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY373756 mRNA. Translation: AAR25661.1.
AY533563 mRNA. Translation: AAS45544.1.
AC137932 Genomic DNA. No translation available.
BC069013 mRNA. Translation: AAH69013.1. Sequence problems.
CCDSiCCDS32513.1.
RefSeqiNP_001243111.1. NM_001256182.1.
NP_001243112.1. NM_001256183.1.
NP_037407.4. NM_013275.5.
XP_011521353.1. XM_011523051.1.
XP_011521354.1. XM_011523052.1.
XP_011521355.1. XM_011523053.1.
UniGeneiHs.335003.
Hs.740440.

Genome annotation databases

EnsembliENST00000301030; ENSP00000301030; ENSG00000167522.
ENST00000378330; ENSP00000367581; ENSG00000167522.
GeneIDi29123.
KEGGihsa:29123.
UCSCiuc002fmx.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY373756 mRNA. Translation: AAR25661.1.
AY533563 mRNA. Translation: AAS45544.1.
AC137932 Genomic DNA. No translation available.
BC069013 mRNA. Translation: AAH69013.1. Sequence problems.
CCDSiCCDS32513.1.
RefSeqiNP_001243111.1. NM_001256182.1.
NP_001243112.1. NM_001256183.1.
NP_037407.4. NM_013275.5.
XP_011521353.1. XM_011523051.1.
XP_011521354.1. XM_011523052.1.
XP_011521355.1. XM_011523053.1.
UniGeneiHs.335003.
Hs.740440.

3D structure databases

ProteinModelPortaliQ6UB99.
SMRiQ6UB99. Positions 114-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118888. 25 interactions.
IntActiQ6UB99. 16 interactions.
STRINGi9606.ENSP00000301030.

PTM databases

iPTMnetiQ6UB99.
PhosphoSiteiQ6UB99.

Polymorphism and mutation databases

BioMutaiANKRD11.
DMDMi296439440.

Proteomic databases

EPDiQ6UB99.
MaxQBiQ6UB99.
PaxDbiQ6UB99.
PeptideAtlasiQ6UB99.
PRIDEiQ6UB99.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301030; ENSP00000301030; ENSG00000167522.
ENST00000378330; ENSP00000367581; ENSG00000167522.
GeneIDi29123.
KEGGihsa:29123.
UCSCiuc002fmx.3. human.

Organism-specific databases

CTDi29123.
GeneCardsiANKRD11.
H-InvDBHIX0013356.
HGNCiHGNC:21316. ANKRD11.
HPAiCAB019288.
HPA041593.
HPA049470.
MalaCardsiANKRD11.
MIMi148050. phenotype.
611192. gene.
neXtProtiNX_Q6UB99.
Orphaneti261250. 16q24.3 microdeletion syndrome.
2332. KBG syndrome.
PharmGKBiPA134861925.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ47. Eukaryota.
ENOG4110UQU. LUCA.
GeneTreeiENSGT00760000119090.
HOGENOMiHOG000168254.
HOVERGENiHBG106759.
InParanoidiQ6UB99.
OMAiEYEDSKQ.
OrthoDBiEOG7SBNMV.
PhylomeDBiQ6UB99.
TreeFamiTF326440.

Miscellaneous databases

ChiTaRSiANKRD11. human.
GenomeRNAii29123.
PROiQ6UB99.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UB99.
CleanExiHS_ANKRD11.
ExpressionAtlasiQ6UB99. baseline and differential.
GenevisibleiQ6UB99. HS.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
[Graphical view]
SMARTiSM00248. ANK. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ANKRD11 and ANKRD12 are novel 9kb genes encoding nuclear-located proteins with ankyrin domains."
    Powell J.A., Settasatian C., Lower K., Callen D.F.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "Identification of a novel family of ankyrin repeats-containing cofactors for p160 nuclear receptor coactivators."
    Zhang A., Yeung P.L., Li C.-W., Tsai S.-C., Dinh G.K., Wu X., Li H., Chen J.D.
    J. Biol. Chem. 279:33799-33805(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH P160.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 1-451.
    Tissue: Pancreas.
  5. "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-1509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410; SER-411; SER-834; THR-1120; SER-1123; THR-1419; SER-1792; SER-1847 AND SER-1859, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-276; SER-408; THR-410 AND SER-411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-276; SER-408; THR-410; SER-411; SER-834 AND THR-1419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Mutations in ANKRD11 cause KBG syndrome, characterized by intellectual disability, skeletal malformations, and macrodontia."
    Sirmaci A., Spiliopoulos M., Brancati F., Powell E., Duman D., Abrams A., Bademci G., Agolini E., Guo S., Konuk B., Kavaz A., Blanton S., Digilio M.C., Dallapiccola B., Young J., Zuchner S., Tekin M.
    Am. J. Hum. Genet. 89:289-294(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN KBGS.
  10. "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-408; THR-410; SER-411 AND SER-834, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-276; SER-834; THR-1419; SER-1792 AND SER-1990, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEASOMAL DEGRADATION, VARIANT KBGS GLN-2512.

Entry informationi

Entry nameiANR11_HUMAN
AccessioniPrimary (citable) accession number: Q6UB99
Secondary accession number(s): Q6NTG1, Q6QMF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 114 of the entry and version 3 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 16
    Human chromosome 16: 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. 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.