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Q8IWY9

- CDAN1_HUMAN

UniProt

Q8IWY9 - CDAN1_HUMAN

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Protein

Codanin-1

Gene
CDAN1, UNQ664/PRO1295
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May acts as a negative regulator of ASF1 in chromatin assembly.1 Publication

GO - Molecular functioni

  1. protein binding Source: UniProtKB

GO - Biological processi

  1. chromatin assembly Source: UniProtKB
  2. negative regulation of DNA replication Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Codanin-1
Gene namesi
Name:CDAN1
ORF Names:UNQ664/PRO1295
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:1713. CDAN1.

Subcellular locationi

Cytoplasm. Nucleus. Membrane; Multi-pass membrane protein Reviewed prediction
Note: Mainly detected as a cytoplasmic protein.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei312 – 33221Helical; Reviewed predictionAdd
BLAST
Transmembranei626 – 64621Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Anemia, congenital dyserythropoietic, 1A (CDAN1A) [MIM:224120]: An autosomal recessive blood disorder characterized by morphological abnormalities of erythroblasts, ineffective erythropoiesis, macrocytic anemia and secondary hemochromatosis. It is occasionally associated with bone abnormalities, especially of the hands and feet (acrodysostosis), nail hypoplasia, and scoliosis. Ultrastructural features include internuclear chromatin bridges connecting some nearly completely separated erythroblasts and an abnormal appearance (spongy or Swiss-cheese appearance) of the heterochromatin in a high proportion of the erythroblasts.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti599 – 5991N → S in CDAN1A. 1 Publication
VAR_017218
Natural varianti672 – 6721P → L in CDAN1A. 1 Publication
VAR_017219
Natural varianti698 – 6981E → K in CDAN1A. 1 Publication
VAR_017220
Natural varianti714 – 7141R → W in CDAN1A; partially disrupts ASF1 binding and loss the ability to arrest cells in S phase and inhibit DNA synthesis. 2 Publications
Corresponds to variant rs80338696 [ dbSNP | Ensembl ].
VAR_017221
Natural varianti868 – 8681F → I in CDAN1A. 1 Publication
VAR_017222
Natural varianti869 – 8691V → M in CDAN1A. 1 Publication
VAR_017223
Natural varianti1042 – 10421R → W in CDAN1A; partially disrupts ASF1 binding. 2 Publications
VAR_017224
Natural varianti1043 – 10431D → V in CDAN1A. 1 Publication
VAR_017225
Natural varianti1130 – 11301P → L in CDAN1A. 1 Publication
VAR_017226

Keywords - Diseasei

Congenital dyserythropoietic anemia, Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi224120. phenotype.
Orphaneti98869. Congenital dyserythropoietic anemia type I.
PharmGKBiPA26249.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12271226Codanin-1PRO_0000089439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8IWY9.
PaxDbiQ8IWY9.
PRIDEiQ8IWY9.

PTM databases

PhosphoSiteiQ8IWY9.

Expressioni

Tissue specificityi

Ubiquitously expressed. Isoform 3 is not found in erythroid cells.1 Publication

Gene expression databases

ArrayExpressiQ8IWY9.
BgeeiQ8IWY9.
CleanExiHS_CDAN1.
GenevestigatoriQ8IWY9.

Organism-specific databases

HPAiHPA039404.
HPA040787.

Interactioni

Subunit structurei

Found in a cytosolic complex with ASF1A, ASF1B, IPO4 and histones H3.1 and H4.1 Publication

Protein-protein interaction databases

BioGridi126963. 7 interactions.
DIPiDIP-24225N.
IntActiQ8IWY9. 4 interactions.
MINTiMINT-1377874.
STRINGi9606.ENSP00000348564.

Structurei

3D structure databases

ProteinModelPortaliQ8IWY9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 20821Interaction with ASF1A/BAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG79208.
HOGENOMiHOG000111492.
HOVERGENiHBG107631.
InParanoidiQ8IWY9.
OMAiREQSSRV.
OrthoDBiEOG715Q3S.
PhylomeDBiQ8IWY9.
TreeFamiTF328405.

Family and domain databases

InterProiIPR028171. Codanin-1_C.
[Graphical view]
PfamiPF15296. Codanin-1_C. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q8IWY9-2) [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

MAAVLESLLR EEVSVAAVVR WIARSTQGSE DNAGEAAALS SLRALRKEFV     50
PFLLNFLREQ SSRVLPQGPP TPAKTPGASA ALPGRPGGPP RGSRGARSQL 100
FPPTEAQSTA AEAPLARRGG RRRGPGPARE RGGRGLEEGV SGESLPGAGG 150
RRLRGSGSPS RPSLTLSDPP NLSNLEEFPP VGSVPPGPTG TKPSRRINPT 200
PVSEERSLSK PKTCFTSPPI SCVPSSQPSA LDTSPWGLGL PPGCRSLQEE 250
REMLRKERSK QLQQSPTPTC PTPELGSPLP SRTGSLTDEP ADPARVSSRQ 300
RLELVALVYS SCIAENLVPN LFLELFFVFQ LLTARRMVTA KDSDPELSPA 350
VLDSLESPLF QSIHDCVFFA VQVLECHFQV LSNLDKGTLK LLAENERLLC 400
FSPALQGRLR AAYEGSVAKV SLVMPPSTQA VSFQPETDNR ANFSSDRAFH 450
TFKKQRDVFY EVLREWEDHH EEPGWDFEKG LGSRIRAMMG QLSAACSHSH 500
FVRLFQKQLL QMCQSPGGAG GTVLGEAPDV LSMLGADKLG RLWRLQERLM 550
APQSSGGPCP PPTFPGCQGF FRDFILSASS FQFNQHLMDS LSLKIQELNG 600
LALPQHEPND EDGESDVDWQ GERKQFAVVL LSLRLLAKFL GFVAFLPYRG 650
PEPPPTGELQ DSILALRSQV PPVLDVRTLL QRGLQARRAV LTVPWLVEFL 700
SFADHVVPLL EYYRDIFTLL LRLHRSLVLS QESEGKMCFL NKLLLLAVLG 750
WLFQIPTVPE DLFFLEEGPS YAFEVDTVAP EHGLDNAPVV DQQLLYTCCP 800
YIGELRKLLA SWVSGSSGRS GGFMRKITPT TTTSLGAQPS QTSQGLQAQL 850
AQAFFHNQPP SLRRTVEFVA ERIGSNCVKH IKATLVADLV RQAESLLQEQ 900
LVTQGEEGGD PAQLLEILCS QLCPHGAQAL ALGREFCQRK SPGAVRALLP 950
EETPAAVLSS AENIAVGLAT EKACAWLSAN ITALIRREVK AAVSRTLRAQ 1000
GPEPAARGER RGCSRACEHH APLPSHLISE IKDVLSLAVG PRDPDEGVSP 1050
EHLEQLLGQL GQTLRCRQFL CPPAEQHLAK CSVELASLLV ADQIPILGPP 1100
AQYRLERGQA RRLLHMLLSL WKEDFQGPVP LQLLLSPRNV GLLADTRPRE 1150
WDLLLFLLRE LVEKGLMGRM EIEACLGSLH QAQWPGDFAE ELATLSNLFL 1200
AEPHLPEPQL RACELVQPNR GTVLAQS 1227
Length:1,227
Mass (Da):134,120
Last modified:May 18, 2010 - v4
Checksum:iE2BC04ACD669DF6F
GO
Isoform 1 (identifier: Q8IWY9-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     190-190: G → GETQLSCRRWVPRRLWGVSHSSSALRSGAPGCR
     226-258: Missing.

Show »
Length:1,226
Mass (Da):133,992
Checksum:i0674D569F19BCD52
GO
Isoform 3 (identifier: Q8IWY9-3)

Sequence is not available
Length:
Mass (Da):

Sequence cautioni

The sequence AAH52568.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAO14994.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAQ88832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Q → L.
Corresponds to variant rs4265781 [ dbSNP | Ensembl ].
VAR_059602
Natural varianti596 – 5961Q → R.
Corresponds to variant rs12917189 [ dbSNP | Ensembl ].
VAR_056785
Natural varianti599 – 5991N → S in CDAN1A. 1 Publication
VAR_017218
Natural varianti672 – 6721P → L in CDAN1A. 1 Publication
VAR_017219
Natural varianti698 – 6981E → K in CDAN1A. 1 Publication
VAR_017220
Natural varianti714 – 7141R → W in CDAN1A; partially disrupts ASF1 binding and loss the ability to arrest cells in S phase and inhibit DNA synthesis. 2 Publications
Corresponds to variant rs80338696 [ dbSNP | Ensembl ].
VAR_017221
Natural varianti868 – 8681F → I in CDAN1A. 1 Publication
VAR_017222
Natural varianti869 – 8691V → M in CDAN1A. 1 Publication
VAR_017223
Natural varianti891 – 8911R → C.
Corresponds to variant rs8023524 [ dbSNP | Ensembl ].
VAR_056786
Natural varianti1042 – 10421R → W in CDAN1A; partially disrupts ASF1 binding. 2 Publications
VAR_017224
Natural varianti1043 – 10431D → V in CDAN1A. 1 Publication
VAR_017225
Natural varianti1130 – 11301P → L in CDAN1A. 1 Publication
VAR_017226

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei190 – 1901G → GETQLSCRRWVPRRLWGVSH SSSALRSGAPGCR in isoform 1. VSP_027097
Alternative sequencei226 – 25833Missing in isoform 1. VSP_027098Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 322DN → VT in AAO14994. 1 Publication
Sequence conflicti39 – 391L → V in AAO14994. 1 Publication
Sequence conflicti42 – 454LRAL → FGAW in AAO14994. 1 Publication
Sequence conflicti51 – 522PF → RS in AAO14994. 1 Publication
Sequence conflicti55 – 551N → T in AAO14994. 1 Publication
Sequence conflicti73 – 731A → P in AAO14994. 1 Publication
Sequence conflicti76 – 761P → R in AAO14994. 1 Publication
Sequence conflicti82 – 821L → C in AAO14994. 1 Publication
Sequence conflicti93 – 931S → T in AAO14994. 1 Publication
Sequence conflicti380 – 3801V → F in AAO14994. 1 Publication
Sequence conflicti421 – 4211S → F in AAH52568. 1 Publication
Sequence conflicti421 – 4211S → F in AAH66640. 1 Publication
Sequence conflicti669 – 6691Q → P in AAQ88832. 1 Publication
Sequence conflicti726 – 7261S → C in AAO14994. 1 Publication
Sequence conflicti946 – 9461R → W in AAH01092. 1 Publication
Sequence conflicti946 – 9461R → W in AAH08333. 1 Publication
Sequence conflicti946 – 9461R → W in AAH08334. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF525398 mRNA. Translation: AAO14994.1. Different initiation.
AC090510 Genomic DNA. No translation available.
BC001092 mRNA. Translation: AAH01092.1.
BC008333 mRNA. Translation: AAH08333.1.
BC008334 mRNA. Translation: AAH08334.1.
BC052568 mRNA. Translation: AAH52568.1. Different initiation.
BC066640 mRNA. Translation: AAH66640.1.
AY358467 mRNA. Translation: AAQ88832.1. Different initiation.
CCDSiCCDS32209.1. [Q8IWY9-2]
RefSeqiNP_612486.2. NM_138477.2. [Q8IWY9-2]
UniGeneiHs.599232.

Genome annotation databases

EnsembliENST00000356231; ENSP00000348564; ENSG00000140326. [Q8IWY9-2]
GeneIDi146059.
KEGGihsa:146059.
UCSCiuc001zql.3. human. [Q8IWY9-2]

Polymorphism databases

DMDMi296439465.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF525398 mRNA. Translation: AAO14994.1 . Different initiation.
AC090510 Genomic DNA. No translation available.
BC001092 mRNA. Translation: AAH01092.1 .
BC008333 mRNA. Translation: AAH08333.1 .
BC008334 mRNA. Translation: AAH08334.1 .
BC052568 mRNA. Translation: AAH52568.1 . Different initiation.
BC066640 mRNA. Translation: AAH66640.1 .
AY358467 mRNA. Translation: AAQ88832.1 . Different initiation.
CCDSi CCDS32209.1. [Q8IWY9-2 ]
RefSeqi NP_612486.2. NM_138477.2. [Q8IWY9-2 ]
UniGenei Hs.599232.

3D structure databases

ProteinModelPortali Q8IWY9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126963. 7 interactions.
DIPi DIP-24225N.
IntActi Q8IWY9. 4 interactions.
MINTi MINT-1377874.
STRINGi 9606.ENSP00000348564.

PTM databases

PhosphoSitei Q8IWY9.

Polymorphism databases

DMDMi 296439465.

Proteomic databases

MaxQBi Q8IWY9.
PaxDbi Q8IWY9.
PRIDEi Q8IWY9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356231 ; ENSP00000348564 ; ENSG00000140326 . [Q8IWY9-2 ]
GeneIDi 146059.
KEGGi hsa:146059.
UCSCi uc001zql.3. human. [Q8IWY9-2 ]

Organism-specific databases

CTDi 146059.
GeneCardsi GC15M043015.
GeneReviewsi CDAN1.
H-InvDB HIX0202162.
HGNCi HGNC:1713. CDAN1.
HPAi HPA039404.
HPA040787.
MIMi 224120. phenotype.
607465. gene.
neXtProti NX_Q8IWY9.
Orphaneti 98869. Congenital dyserythropoietic anemia type I.
PharmGKBi PA26249.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG79208.
HOGENOMi HOG000111492.
HOVERGENi HBG107631.
InParanoidi Q8IWY9.
OMAi REQSSRV.
OrthoDBi EOG715Q3S.
PhylomeDBi Q8IWY9.
TreeFami TF328405.

Miscellaneous databases

ChiTaRSi CDAN1. human.
GenomeRNAii 146059.
NextBioi 85255.
PROi Q8IWY9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IWY9.
Bgeei Q8IWY9.
CleanExi HS_CDAN1.
Genevestigatori Q8IWY9.

Family and domain databases

InterProi IPR028171. Codanin-1_C.
[Graphical view ]
Pfami PF15296. Codanin-1_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, VARIANTS CDAN1A SER-599; LEU-672; LYS-698; TRP-714; ILE-868; MET-869; TRP-1042; VAL-1043 AND LEU-1130.
  2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 2).
    Tissue: Kidney and Ovary.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 669-1016 (ISOFORM 2).
  5. "Codanin-1 mutations in congenital dyserythropoietic anemia type 1 affect HP1-alpha localization in erythroblasts."
    Renella R., Roberts N.A., Brown J.M., De Gobbi M., Bird L.E., Hassanali T., Sharpe J.A., Sloane-Stanley J., Ferguson D.J., Cordell J., Buckle V.J., Higgs D.R., Wood W.G.
    Blood 117:6928-6938(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Codanin-1, mutated in the anaemic disease CDAI, regulates Asf1 function in S-phase histone supply."
    Ask K., Jasencakova Z., Menard P., Feng Y., Almouzni G., Groth A.
    EMBO J. 31:2013-2023(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ASF1A AND ASF1B, IDENTIFICATION IN A COMPLEX WITH ASF1A; ASF1B; IPO4; HISTONES H3.2 AND H4, CHARACTERIZATION OF VARIANTS TRP-714 AND TRP-1042, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDAN1_HUMAN
AccessioniPrimary (citable) accession number: Q8IWY9
Secondary accession number(s): Q6NYD0, Q7Z7L5, Q969N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 99 of the entry and version 4 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 15
    Human chromosome 15: 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

External Data

Dasty 3

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