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Q9BXF3

- CECR2_HUMAN

UniProt

Q9BXF3 - CECR2_HUMAN

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Protein

Cat eye syndrome critical region protein 2

Gene

CECR2

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

Functioni

Part of the CERF (CECR2-containing-remodeling factor) complex, which facilitates the perturbation of chromatin structure in an ATP-dependent manner. May be involved through its interaction with LRPPRC in the integration of cytoskeletal network with vesicular trafficking, nucleocytosolic shuttling, transcription, chromosome remodeling and cytokinesis.1 Publication

GO - Biological processi

  1. apoptotic DNA fragmentation Source: HGNC
  2. ATP-dependent chromatin remodeling Source: MGI
  3. cytokinesis Source: UniProtKB
  4. cytoskeleton organization Source: UniProtKB
  5. execution phase of apoptosis Source: BHF-UCL
  6. neural tube development Source: InterPro
  7. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Names & Taxonomyi

Protein namesi
Recommended name:
Cat eye syndrome critical region protein 2
Gene namesi
Name:CECR2
Synonyms:KIAA1740
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:1840. CECR2.

Subcellular locationi

GO - Cellular componenti

  1. CERF complex Source: MGI
  2. nucleus Source: HGNC
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26383.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14841484Cat eye syndrome critical region protein 2PRO_0000211192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei422 – 4221Phosphoserine1 Publication
Modified residuei546 – 5461Phosphothreonine1 Publication
Modified residuei571 – 5711Phosphoserine1 Publication
Modified residuei1014 – 10141Phosphoserine1 Publication
Modified residuei1312 – 13121Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9BXF3.
PRIDEiQ9BXF3.

PTM databases

PhosphoSiteiQ9BXF3.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle, thymus, placenta and lung. Expressed at lower level in brain, heart, colon, spleen, kidney.

Gene expression databases

BgeeiQ9BXF3.
CleanExiHS_CECR2.
ExpressionAtlasiQ9BXF3. baseline.
GenevestigatoriQ9BXF3.

Organism-specific databases

HPAiHPA002943.

Interactioni

Subunit structurei

Part of the CECR2-containing remodeling factor (CERF) complex which contains CECR2 and SMARCA1. Interacts with acetylated lysine residues on histone H2A and H3 (in vitro). Interacts with LRPPRC.3 Publications

Protein-protein interaction databases

BioGridi118176. 4 interactions.
STRINGi9606.ENSP00000262608.

Structurei

Secondary structure

1
1484
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi439 – 45214Combined sources
Helixi457 – 4593Combined sources
Turni465 – 4673Combined sources
Helixi471 – 4744Combined sources
Helixi481 – 4899Combined sources
Helixi496 – 51419Combined sources
Helixi519 – 53618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NXBX-ray1.83A/B424-538[»]
ProteinModelPortaliQ9BXF3.
SMRiQ9BXF3. Positions 412-537.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BXF3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 52171BromoPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi333 – 3375Poly-Glu
Compositional biasi611 – 6144Poly-Ser
Compositional biasi1250 – 12534Poly-Pro

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000081808.
HOVERGENiHBG081078.
InParanoidiQ9BXF3.
PhylomeDBiQ9BXF3.
TreeFamiTF324727.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR029614. CECR2.
[Graphical view]
PANTHERiPTHR22880:SF123. PTHR22880:SF123. 1 hit.
PfamiPF00439. Bromodomain. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q9BXF3-1) [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
MCPEEGGAAG LGELRSWWEV PAIAHFCSLF RTAFRLPDFE IEELEAALHR
60 70 80 90 100
DDVEFISDLI ACLLQGCYQR RDITPQTFHS YLEDIINYRW ELEEGKPNPL
110 120 130 140 150
REASFQDLPL RTRVEILHRL CDYRLDADDV FDLLKGLDAD SLRVEPLGED
160 170 180 190 200
NSGALYWYFY GTRMYKEDPV QGKSNGELSL SRESEGQKNV SSIPGKTGKR
210 220 230 240 250
RGRPPKRKKL QEEILLSEKQ EENSLASEPQ TRHGSQGPGQ GTWWLLCQTE
260 270 280 290 300
EEWRQVTESF RERTSLRERQ LYKLLSEDFL PEICNMIAQK GKRPQRTKAE
310 320 330 340 350
LHPRWMSDHL SIKPVKQEET PVLTRIEKQK RKEEEEERQI LLAVQKKEQE
360 370 380 390 400
QMLKEERKRE LEEKVKAVEG MCSVRVVWRG ACLSTSRPVD RAKRRKLREE
410 420 430 440 450
RAWLLAQGKE LPPELSHLDP NSPMREEKKT KDLFELDDDF TAMYKVLDVV
460 470 480 490 500
KAHKDSWPFL EPVDESYAPN YYQIIKAPMD ISSMEKKLNG GLYCTKEEFV
510 520 530 540 550
NDMKTMFRNC RKYNGESSEY TKMSDNLERC FHRAMMKHFP GEDGDTDEEF
560 570 580 590 600
WIREDEKREK RRSRAGRSGG SHVWTRSRDP EGSSRKQQPM ENGGKSLPPT
610 620 630 640 650
RRAPSSGDDQ SSSSTQPPRE VGTSNGRGFS HPLHCGGTPS QAPFLNQMRP
660 670 680 690 700
AVPGTFGPLR GSDPATLYGS SGVPEPHPGE PVQQRQPFTM QPPVGINSLR
710 720 730 740 750
GPRLGTPEEK QMCGGLTHLS NMGPHPGSLQ LGQISGPSQD GSMYAPAQFQ
760 770 780 790 800
PGFIPPRHGG APARPPDFPE SSEIPPSHMY RSYKYLNRVH SAVWNGNHGA
810 820 830 840 850
TNQGPLGPDE KPHLGPGPSH QPRTLGHVMD SRVMRPPVPP NQWTEQSGFL
860 870 880 890 900
PHGVPSSGYM RPPCKSAGHR LQPPPVPAPS SLFGAPAQAL RGVQGGDSMM
910 920 930 940 950
DSPEMIAMQQ LSSRVCPPGV PYHPHQPAHP RLPGPFPQVA HPMSVTVSAP
960 970 980 990 1000
KPALGNPGRA PENSEAQEPE NDQAEPLPGL EEKPPGVGTS EGVYLTQLPH
1010 1020 1030 1040 1050
PTPPLQTDCT RQSSPQERET VGPELKSSSS ESADNCKAMK GKNPWPSDSS
1060 1070 1080 1090 1100
YPGPAAQGCV RDLSTVADRG ALSENGVIGE ASPCGSEGKG LGSSGSEKLL
1110 1120 1130 1140 1150
CPRGRTLQET MPCTGQNAAT PPSTDPGLTG GTVSQFPPLY MPGLEYPNSA
1160 1170 1180 1190 1200
AHYHISPGLQ GVGPVMGGKS PASHPQHFPP RGFQSNHPHS GGFPRYRPPQ
1210 1220 1230 1240 1250
GMRYSYHPPP QPSYHHYQRT PYYACPQSFS DWQRPLHPQG SPSGPPASQP
1260 1270 1280 1290 1300
PPPRSLFSDK NAMASLQGCE TLNAALTSPT RMDAVAAKVP NDGQNPGPEE
1310 1320 1330 1340 1350
EKLDESMERP ESPKEFLDLD NHNAATKRQS SLSASEYLYG TPPPLSSGMG
1360 1370 1380 1390 1400
FGSSAFPPHS VMLQTGPPYT PQRPASHFQP RAYSSPVAAL PPHHPGATQP
1410 1420 1430 1440 1450
NGLSQEGPIY RCQEEGLGHF QAVMMEQIGT RSGIRGPFQE MYRPSGMQMH
1460 1470 1480
PVQSQASFPK TPTAATSQEE VPPHKPPTLP LDQS
Length:1,484
Mass (Da):164,213
Last modified:September 5, 2006 - v2
Checksum:i8680DB16A0B90D0D
GO
Isoform B (identifier: Q9BXF3-2) [UniParc]FASTAAdd to Basket

Also known as: CECR2B

The sequence of this isoform differs from the canonical sequence as follows:
     291-318: Missing.
     519-526: EYTKMSDN → GKQGRSLC
     527-1484: Missing.

Show »
Length:498
Mass (Da):58,108
Checksum:i40A2A890E9B5B9D6
GO
Isoform C (identifier: Q9BXF3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     370-389: Missing.

Show »
Length:1,464
Mass (Da):162,067
Checksum:i3321852BA97D5481
GO

Sequence cautioni

The sequence CAH56122.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH56212.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW57756.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti352 – 3521M → I in CAH56122. (PubMed:17974005)Curated
Sequence conflicti352 – 3521M → I in CAH56212. (PubMed:17974005)Curated
Sequence conflicti1029 – 10291S → C in AAK15343. (PubMed:11381032)Curated
Sequence conflicti1045 – 10451W → R in AAK15343. (PubMed:11381032)Curated
Sequence conflicti1441 – 14411M → T in CAH56122. (PubMed:17974005)Curated
Sequence conflicti1441 – 14411M → T in CAH56212. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti293 – 2931R → H.
Corresponds to variant rs5747211 [ dbSNP | Ensembl ].
VAR_027411
Natural varianti674 – 6741P → L.2 Publications
Corresponds to variant rs1296794 [ dbSNP | Ensembl ].
VAR_027412

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei291 – 31828Missing in isoform B. 1 PublicationVSP_000571Add
BLAST
Alternative sequencei370 – 38920Missing in isoform C. 2 PublicationsVSP_020407Add
BLAST
Alternative sequencei519 – 5268EYTKMSDN → GKQGRSLC in isoform B. 1 PublicationVSP_000572
Alternative sequencei527 – 1484958Missing in isoform B. 1 PublicationVSP_000573Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336133 mRNA. Translation: AAK15343.1.
AC004019 Genomic DNA. No translation available.
CH471193 Genomic DNA. Translation: EAW57756.1. Different initiation.
BX647449 mRNA. Translation: CAH56122.1. Different initiation.
AL832377 mRNA. Translation: CAH56212.1. Different initiation.
AB051527 mRNA. Translation: BAB21831.1.
AF411609 mRNA. Translation: AAL07393.1.
RefSeqiNP_001276975.1. NM_001290046.1.
NP_001276976.1. NM_001290047.1. [Q9BXF3-3]
UniGeneiHs.231895.
Hs.658723.

Genome annotation databases

EnsembliENST00000262608; ENSP00000262608; ENSG00000099954. [Q9BXF3-1]
ENST00000342247; ENSP00000341219; ENSG00000099954. [Q9BXF3-1]
GeneIDi27443.
KEGGihsa:27443.
UCSCiuc010gqw.1. human. [Q9BXF3-1]

Polymorphism databases

DMDMi114152782.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336133 mRNA. Translation: AAK15343.1 .
AC004019 Genomic DNA. No translation available.
CH471193 Genomic DNA. Translation: EAW57756.1 . Different initiation.
BX647449 mRNA. Translation: CAH56122.1 . Different initiation.
AL832377 mRNA. Translation: CAH56212.1 . Different initiation.
AB051527 mRNA. Translation: BAB21831.1 .
AF411609 mRNA. Translation: AAL07393.1 .
RefSeqi NP_001276975.1. NM_001290046.1.
NP_001276976.1. NM_001290047.1. [Q9BXF3-3 ]
UniGenei Hs.231895.
Hs.658723.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NXB X-ray 1.83 A/B 424-538 [» ]
ProteinModelPortali Q9BXF3.
SMRi Q9BXF3. Positions 412-537.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118176. 4 interactions.
STRINGi 9606.ENSP00000262608.

Chemistry

ChEMBLi CHEMBL3108639.

PTM databases

PhosphoSitei Q9BXF3.

Polymorphism databases

DMDMi 114152782.

Proteomic databases

PaxDbi Q9BXF3.
PRIDEi Q9BXF3.

Protocols and materials databases

DNASUi 27443.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262608 ; ENSP00000262608 ; ENSG00000099954 . [Q9BXF3-1 ]
ENST00000342247 ; ENSP00000341219 ; ENSG00000099954 . [Q9BXF3-1 ]
GeneIDi 27443.
KEGGi hsa:27443.
UCSCi uc010gqw.1. human. [Q9BXF3-1 ]

Organism-specific databases

CTDi 27443.
GeneCardsi GC22P017840.
H-InvDB HIX0023032.
HGNCi HGNC:1840. CECR2.
HPAi HPA002943.
MIMi 607576. gene.
neXtProti NX_Q9BXF3.
PharmGKBi PA26383.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00760000119099.
HOGENOMi HOG000081808.
HOVERGENi HBG081078.
InParanoidi Q9BXF3.
PhylomeDBi Q9BXF3.
TreeFami TF324727.

Miscellaneous databases

ChiTaRSi CECR2. human.
EvolutionaryTracei Q9BXF3.
GenomeRNAii 27443.
NextBioi 50516.
PROi Q9BXF3.
SOURCEi Search...

Gene expression databases

Bgeei Q9BXF3.
CleanExi HS_CECR2.
ExpressionAtlasi Q9BXF3. baseline.
Genevestigatori Q9BXF3.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
InterProi IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR029614. CECR2.
[Graphical view ]
PANTHERi PTHR22880:SF123. PTHR22880:SF123. 1 hit.
Pfami PF00439. Bromodomain. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the cat eye syndrome critical region in humans and the region of conserved synteny in mice: a search for candidate genes at or near the human chromosome 22 pericentromere."
    Footz T.K., Brinkman-Mills P., Banting G.S., Maier S.A., Riazi M.A., Bridgland L.J., Hu S., Birren B., Minoshima S., Shimizu N., Pan H., Nguyen T., Fang F., Fu Y., Ray L., Wu H., Shaull S., Phan S.
    , Yao Z., Chen F., Huan A., Hu P., Wang Q., Loh P., Qi S., Roe B.A., McDermid H.E.
    Genome Res. 11:1053-1070(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT LEU-674.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1484 (ISOFORM C).
    Tissue: Skeletal muscle.
  5. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 346-1484 (ISOFORM C), VARIANT LEU-674.
    Tissue: Brain.
  6. "Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
    Liu L., McKeehan W.L.
    Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-1484 (ISOFORM B), INTERACTION WITH LRPPRC.
    Tissue: Liver.
  7. "CECR2, a protein involved in neurulation, forms a novel chromatin remodeling complex with SNF2L."
    Banting G.S., Barak O., Ames T.M., Burnham A.C., Kardel M.D., Cooch N.S., Davidson C.E., Godbout R., McDermid H.E., Shiekhattar R.
    Hum. Mol. Genet. 14:513-524(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE CERF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "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-422; THR-546; SER-571; SER-1014 AND SER-1312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 424-538, SUBUNIT.

Entry informationi

Entry nameiCECR2_HUMAN
AccessioniPrimary (citable) accession number: Q9BXF3
Secondary accession number(s): A8MS90
, A8MX16, Q658Z4, Q96P58, Q9C0C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: September 5, 2006
Last modified: November 26, 2014
This is version 114 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

Miscellaneous

Candidate gene for the Cat Eye Syndrome (CES), a developmental disorder associated with the duplication of a 2 Mb region of 22q11.2. Duplication usually takes in the form of a surpernumerary bisatellited isodicentric chromosome, resulting in four copies of the region (represents an inv dup(22)(q11)). CES is characterized clinically by the combination of coloboma of the iris and anal atresia with fistula, downslanting palpebral fissures, preauricular tags and/or pits, frequent occurrence of heart and renal malformations, and normal or near-normal mental development.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3