Skip Header

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

Q8IWY9

- CDAN1_HUMAN

UniProt

Q8IWY9 - CDAN1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Codanin-1

Gene

CDAN1

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 - Biological processi

  1. chromatin assembly Source: UniProtKB
  2. chromatin organization Source: MGI
  3. negative regulation of DNA replication Source: UniProtKB
  4. protein localization Source: MGI
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 Curated; Multi-pass membrane protein Curated
Note: Mainly detected as a cytoplasmic protein.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endomembrane system Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. nucleus Source: UniProtKB
  5. 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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. 1 Publication
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. 1 Publication
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

BgeeiQ8IWY9.
CleanExiHS_CDAN1.
ExpressionAtlasiQ8IWY9. baseline and differential.
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. 8 interactions.
DIPiDIP-24225N.
IntActiQ8IWY9. 4 interactions.
MINTiMINT-1377874.
STRINGi9606.ENSP00000348564.

Structurei

3D structure databases

ProteinModelPortaliQ8IWY9.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei312 – 33221HelicalSequence AnalysisAdd
BLAST
Transmembranei626 – 64621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG79208.
GeneTreeiENSGT00390000000491.
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

        10         20         30         40         50
MAAVLESLLR EEVSVAAVVR WIARSTQGSE DNAGEAAALS SLRALRKEFV
60 70 80 90 100
PFLLNFLREQ SSRVLPQGPP TPAKTPGASA ALPGRPGGPP RGSRGARSQL
110 120 130 140 150
FPPTEAQSTA AEAPLARRGG RRRGPGPARE RGGRGLEEGV SGESLPGAGG
160 170 180 190 200
RRLRGSGSPS RPSLTLSDPP NLSNLEEFPP VGSVPPGPTG TKPSRRINPT
210 220 230 240 250
PVSEERSLSK PKTCFTSPPI SCVPSSQPSA LDTSPWGLGL PPGCRSLQEE
260 270 280 290 300
REMLRKERSK QLQQSPTPTC PTPELGSPLP SRTGSLTDEP ADPARVSSRQ
310 320 330 340 350
RLELVALVYS SCIAENLVPN LFLELFFVFQ LLTARRMVTA KDSDPELSPA
360 370 380 390 400
VLDSLESPLF QSIHDCVFFA VQVLECHFQV LSNLDKGTLK LLAENERLLC
410 420 430 440 450
FSPALQGRLR AAYEGSVAKV SLVMPPSTQA VSFQPETDNR ANFSSDRAFH
460 470 480 490 500
TFKKQRDVFY EVLREWEDHH EEPGWDFEKG LGSRIRAMMG QLSAACSHSH
510 520 530 540 550
FVRLFQKQLL QMCQSPGGAG GTVLGEAPDV LSMLGADKLG RLWRLQERLM
560 570 580 590 600
APQSSGGPCP PPTFPGCQGF FRDFILSASS FQFNQHLMDS LSLKIQELNG
610 620 630 640 650
LALPQHEPND EDGESDVDWQ GERKQFAVVL LSLRLLAKFL GFVAFLPYRG
660 670 680 690 700
PEPPPTGELQ DSILALRSQV PPVLDVRTLL QRGLQARRAV LTVPWLVEFL
710 720 730 740 750
SFADHVVPLL EYYRDIFTLL LRLHRSLVLS QESEGKMCFL NKLLLLAVLG
760 770 780 790 800
WLFQIPTVPE DLFFLEEGPS YAFEVDTVAP EHGLDNAPVV DQQLLYTCCP
810 820 830 840 850
YIGELRKLLA SWVSGSSGRS GGFMRKITPT TTTSLGAQPS QTSQGLQAQL
860 870 880 890 900
AQAFFHNQPP SLRRTVEFVA ERIGSNCVKH IKATLVADLV RQAESLLQEQ
910 920 930 940 950
LVTQGEEGGD PAQLLEILCS QLCPHGAQAL ALGREFCQRK SPGAVRALLP
960 970 980 990 1000
EETPAAVLSS AENIAVGLAT EKACAWLSAN ITALIRREVK AAVSRTLRAQ
1010 1020 1030 1040 1050
GPEPAARGER RGCSRACEHH APLPSHLISE IKDVLSLAVG PRDPDEGVSP
1060 1070 1080 1090 1100
EHLEQLLGQL GQTLRCRQFL CPPAEQHLAK CSVELASLLV ADQIPILGPP
1110 1120 1130 1140 1150
AQYRLERGQA RRLLHMLLSL WKEDFQGPVP LQLLLSPRNV GLLADTRPRE
1160 1170 1180 1190 1200
WDLLLFLLRE LVEKGLMGRM EIEACLGSLH QAQWPGDFAE ELATLSNLFL
1210 1220
AEPHLPEPQL RACELVQPNR GTVLAQS
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 322DN → VT in AAO14994. (PubMed:12434312)Curated
Sequence conflicti39 – 391L → V in AAO14994. (PubMed:12434312)Curated
Sequence conflicti42 – 454LRAL → FGAW in AAO14994. (PubMed:12434312)Curated
Sequence conflicti51 – 522PF → RS in AAO14994. (PubMed:12434312)Curated
Sequence conflicti55 – 551N → T in AAO14994. (PubMed:12434312)Curated
Sequence conflicti73 – 731A → P in AAO14994. (PubMed:12434312)Curated
Sequence conflicti76 – 761P → R in AAO14994. (PubMed:12434312)Curated
Sequence conflicti82 – 821L → C in AAO14994. (PubMed:12434312)Curated
Sequence conflicti93 – 931S → T in AAO14994. (PubMed:12434312)Curated
Sequence conflicti380 – 3801V → F in AAO14994. (PubMed:12434312)Curated
Sequence conflicti421 – 4211S → F in AAH52568. (PubMed:15489334)Curated
Sequence conflicti421 – 4211S → F in AAH66640. (PubMed:15489334)Curated
Sequence conflicti669 – 6691Q → P in AAQ88832. (PubMed:12975309)Curated
Sequence conflicti726 – 7261S → C in AAO14994. (PubMed:12434312)Curated
Sequence conflicti946 – 9461R → W in AAH01092. (PubMed:15489334)Curated
Sequence conflicti946 – 9461R → W in AAH08333. (PubMed:15489334)Curated
Sequence conflicti946 – 9461R → W in AAH08334. (PubMed:15489334)Curated

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. 1 Publication
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. 1 Publication
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. 1 PublicationVSP_027097
Alternative sequencei226 – 25833Missing in isoform 1. 1 PublicationVSP_027098Add
BLAST

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. 8 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.
GeneTreei ENSGT00390000000491.
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

Bgeei Q8IWY9.
CleanExi HS_CDAN1.
ExpressionAtlasi Q8IWY9. baseline and differential.
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: October 29, 2014
This is version 101 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