Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P46100 (ATRX_HUMAN)

Last modified January 19, 2010. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Transcriptional regulator ATRX
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent helicase ATRX
    X-linked helicase II
    X-linked nuclear protein
      Short name=XNP
    Znf-HX
Gene names
Name: ATRX
Synonyms: RAD54L, XH2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length2492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis.

Subunit structure

Probably binds EZH2. Binds annexin V in a calcium and phosphatidylcholine/phosphatidylserine-dependent manner By similarity. Interacts directly with CBX5 via the PxVxL motif. Ref.9 Ref.14

Subcellular location

Nucleus. Note: Associated with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with HP1. Ref.10

Tissue specificity

Ubiquitous.

Domain

Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is required for interaction with chromoshadow domains. This motif requires additional residues -7, -6, +4 and +5 of the central Val which contact the chromoshadow domain. Ref.23

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21

Involvement in disease

Defects in ATRX are the cause of X-linked alpha-thalassemia/mental retardation syndrome (ATR-X) [MIM:301040]. ATR-X is an X-linked disorder comprising severe psychomotor retardation, facial dysmorphism, urogenital abnormalities, and alpha-thalassemia. An essential phenotypic trait are hemoglobin H erythrocyte inclusions. Ref.1 Ref.8 Ref.24 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.33 Ref.36

Defects in ATRX are the cause of mental retardation syndromic X-linked with hypotonic facies syndrome type 1 (MRXSHF1) [MIM:309580]; also called Carpenter-Waziri syndrome (CWS), Juberg-Marsidi syndrome (JMS), Smith-Fineman-Myers syndrome type 1 (SFM1). Clinical features include severe mental retardation, dysmorphic facies, and a highly skewed X-inactivation pattern in carrier women. Other more variable features include hypogonadism, deafness, renal anomalies, and mild skeletal defects. Ref.11 Ref.25 Ref.29 Ref.32 Ref.34 Ref.35

Defects in ATRX are a cause of alpha-thalassemia myelodysplasia syndrome (ATMDS) [MIM:300448]. In this disorder, alpha-thalassemia occurs as an acquired abnormality in association with a multilineage myelodysplasia. Ref.12

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 GATA-type zinc finger.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 PHD-type zinc finger.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DAXXQ9UER71EBI-396461,EBI-77321
EIF4A2Q142401EBI-396461,EBI-73473

Hide | Top

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: P46100-1)

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 1 (identifier: P46100-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.
Isoform 2 (identifier: P46100-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
Isoform 3 (identifier: P46100-4)

The sequence of this isoform differs from the canonical sequence as follows:
     124-161: Missing.
Isoform 5 (identifier: P46100-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.
     124-161: Missing.
Isoform 6 (identifier: P46100-6)

The sequence of this isoform differs from the canonical sequence as follows:
     124-162: Missing.
     573-601: Missing.
     1419-2492: Missing.
Note: No experimental confirmation available.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24922492Transcriptional regulator ATRX
PRO_0000074301

Regions

Domain1581 – 1768188Helicase ATP-binding
Domain2025 – 2205181Helicase C-terminal
Zinc finger171 – 20030GATA-type; atypical
Zinc finger220 – 26849PHD-type
Nucleotide binding1594 – 16018ATP Potential
Motif581 – 59414PxVxL motif
Motif1719 – 17224DEGH box
Compositional bias745 – 7506Poly-Ser
Compositional bias1151 – 11566Poly-Ser
Compositional bias1166 – 11694Poly-Lys
Compositional bias1202 – 12065Poly-Ser
Compositional bias1259 – 12668Poly-Asp
Compositional bias1443 – 146624Poly-Glu
Compositional bias1499 – 15024Poly-Glu
Compositional bias1929 – 193911Poly-Lys
Compositional bias1941 – 19488Poly-Ser
Compositional bias2222 – 22254Poly-Lys
Compositional bias2262 – 22654Poly-Glu
Compositional bias2420 – 24256Poly-Gln

Amino acid modifications

Modified residue341Phosphoserine Ref.13 Ref.15 Ref.21
Modified residue711Phosphoserine Ref.17
Modified residue741Phosphoserine Ref.17
Modified residue871Phosphothreonine Ref.16
Modified residue891Phosphotyrosine Ref.21
Modified residue921Phosphoserine By similarity
Modified residue1121Phosphoserine Ref.21
Modified residue5941Phosphoserine Ref.19
Modified residue5981Phosphoserine Ref.19
Modified residue6341Phosphoserine Ref.15
Modified residue6741Phosphothreonine Ref.19
Modified residue6751Phosphoserine Ref.19
Modified residue6771Phosphoserine Ref.19
Modified residue7291Phosphoserine Ref.15 Ref.19 Ref.20 Ref.21
Modified residue7311Phosphoserine Ref.15 Ref.19 Ref.20 Ref.21
Modified residue8491Phosphoserine Ref.15
Modified residue8501Phosphoserine Ref.15
Modified residue8711Phosphoserine Ref.18 Ref.19
Modified residue8751Phosphoserine Ref.19
Modified residue8761Phosphoserine Ref.19
Modified residue9671N6-acetyllysine Ref.22
Modified residue10611Phosphoserine By similarity
Modified residue13481Phosphoserine Ref.15 Ref.19 Ref.20
Modified residue13521Phosphoserine Ref.15 Ref.19 Ref.20
Modified residue15271Phosphoserine Ref.15
Modified residue19911Phosphoserine Ref.19 Ref.20
Modified residue19921Phosphoserine Ref.20
Modified residue19961Phosphoserine Ref.19 Ref.20 Ref.21
Modified residue22201Phosphoserine Ref.19

Natural variations

Alternative sequence1 – 204204Missing in isoform 1.
VSP_000575
Alternative sequence1 – 117117Missing in isoform 2 and isoform 5.
VSP_000574
Alternative sequence124 – 16239Missing in isoform 6.
VSP_015499
Alternative sequence124 – 16138Missing in isoform 3 and isoform 5.
VSP_000576
Alternative sequence573 – 60129Missing in isoform 6.
VSP_015500
Alternative sequence1419 – 24921074Missing in isoform 6.
VSP_015501
Natural variant1751G → E in ATR-X. Ref.30
VAR_012113
Natural variant178 – 19821Missing in ATR-X.
VAR_012114
Natural variant1791N → S in ATR-X. Ref.31
VAR_012115
Natural variant1901P → A in ATR-X.
VAR_001226
Natural variant1901P → L in ATR-X. Ref.31
VAR_012116
Natural variant1901P → S in ATR-X. Ref.30
VAR_012117
Natural variant1921L → F in ATR-X.
VAR_001227
Natural variant1941V → I in ATR-X. Ref.31
VAR_012118
Natural variant2001C → S in ATR-X.
VAR_001228
Natural variant2191Q → P in ATR-X. Ref.30
VAR_012119
Natural variant2201C → R in ATR-X.
VAR_001229
Natural variant2201C → Y in MRXSHF1. Ref.32
VAR_032625
Natural variant2221W → S in ATR-X.
VAR_001230
Natural variant2431C → F in ATR-X.
VAR_001231
Natural variant2461R → C in ATR-X. Ref.31 Ref.36
VAR_001232
Natural variant2461R → L in ATR-X. Ref.27 Ref.30
VAR_010914
Natural variant2491G → C in ATR-X. Ref.30
VAR_012120
Natural variant2491G → D in ATR-X.
VAR_001233
Natural variant4091L → S in MRXSHF1. Ref.35
VAR_032626
Natural variant5451Q → E: dbSNP rs35738915.
VAR_055939
Natural variant5961P → S: dbSNP rs1051678. Ref.1 Ref.3 Ref.5
VAR_016914
Natural variant7401G → E: dbSNP rs1051680. Ref.1 Ref.3 Ref.5 Ref.4
VAR_016915
Natural variant9291Q → E: dbSNP rs3088074. Ref.4
VAR_023438
Natural variant15381V → G in ATR-X; could be a polymorphism.
VAR_012121
Natural variant15521V → F in ATR-X. Ref.31
VAR_012122
Natural variant16091H → R in ATR-X.
VAR_001234
Natural variant16141C → R in ATR-X.
VAR_001235
Natural variant16211T → M in ATR-X. Ref.33
VAR_016916
Natural variant16451L → S in ATR-X. Ref.31
VAR_012123
Natural variant16501K → N in ATR-X.
VAR_001236
Natural variant17131P → S in ATR-X; without alpha-thalassemia. Ref.24
VAR_012124
Natural variant17421R → K in ATR-X; atypical; patients presents spastic paraplegia at birth. Ref.28
VAR_012125
Natural variant18471Y → C in ATR-X. Ref.31
VAR_012126
Natural variant18601N → S Rare polymorphism. dbSNP rs45439799. Ref.1
VAR_001237
Natural variant20351D → V in ATR-X.
VAR_001238
Natural variant20501I → T in MRXSHF1; originally reported as Carpenter-Waziri syndrome. Ref.29
VAR_012127
Natural variant20841Y → H in ATR-X.
VAR_001239
Natural variant21311R → Q in MRXSHF1; originally reported as Juberg-Marsidi syndrome. Ref.25
VAR_001240
Natural variant21631Y → C in ATR-X.
VAR_001241
Natural variant22711R → G in MRXSHF1. Ref.34
VAR_032627

Experimental info

Sequence conflict8791A → R in AAC50069. Ref.6
Sequence conflict12861S → P in BAD92165. Ref.4
Sequence conflict1625 – 16328VCPLNTAL → GLSSSILAF in AAC50069. Ref.6
Sequence conflict2259 – 22657DHKEEEE → TTKKKKR in AAC50069. Ref.6
Sequence conflict22801A → G in AAC50069. Ref.6
Sequence conflict2283 – 22842KG → RV in AAC50069. Ref.6
Sequence conflict2403 – 243129SCVQR…TYQQA → QLCSANTYEQKAPAAVQSAA TATNDLSTT in AAC50069. Ref.6
Sequence conflict24361L → H in AAC50069. Ref.6
Sequence conflict24421P → R in AAC50069. Ref.6
Sequence conflict2475 – 249218APPPM…QGKSM → CTTPNEKQKIQDLPKGNQCD FA in AAC50069. Ref.6

Secondary structure

1 ...................... 2492
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 [UniParc].

Last modified December 16, 2008. Version 4.
Checksum: 30DE41CA38A18F89

FASTA2,492282,524
        10         20         30         40         50         60 
MTAEPMSESK LNTLVQKLHD FLAHSSEESE ETSSPPRLAM NQNTDKISGS GSNSDMMENS 

        70         80         90        100        110        120 
KEEGTSSSEK SKSSGSSRSK RKPSIVTKYV ESDDEKPLDD ETVNEDASNE NSENDITMQS 

       130        140        150        160        170        180 
LPKGTVIVQP EPVLNEDKDD FKGPEFRSRS KMKTENLKKR GEDGLHGIVS CTACGQQVNH 

       190        200        210        220        230        240 
FQKDSIYRHP SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC 

       250        260        270        280        290        300 
KKCILRNLGR KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV 

       310        320        330        340        350        360 
DSEKSNKVYE HTSRFSPKKT SSNCNGEEKK LDDSCSGSVT YSYSALIVPK EMIKKAKKLI 

       370        380        390        400        410        420 
ETTANMNSSY VKFLKQATDN SEISSATKLR QLKAFKSVLA DIKKAHLALE EDLNSEFRAM 

       430        440        450        460        470        480 
DAVNKEKNTK EHKVIDAKFE TKARKGEKPC ALEKKDISKS EAKLSRKQVD SEHMHQNVPT 

       490        500        510        520        530        540 
EEQRTNKSTG GEHKKSDRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQS 

       550        560        570        580        590        600 
SVDHQGDGSS GTEQEVESSS VKLNISSKDN RGGIKSKTTA KVTKELYVKL TPVSLPNSPI 

       610        620        630        640        650        660 
KGADCQEVPQ DKDGYKSCGL NPKLEKCGLG QENSDNEHLV ENEVSLLLEE SDLRRSPRVK 

       670        680        690        700        710        720 
TTPLRRPTET NPVTSNSDEE CNETVKEKQK LSVPVRKKDK RNSSDSAIDN PKPNKLPKSK 

       730        740        750        760        770        780 
QSETVDQNSD SDEMLAILKG VSRMSHSSSS DTDINEIHTN HKTLYDLKTQ AGKDDKGKRK 

       790        800        810        820        830        840 
RKSSTSGSDF DTKKGKSAKS SIISKKKRQT QSESSNYDSE LEKEIKSMSK IGAARTTKKR 

       850        860        870        880        890        900 
IPNTKDFDSS EDEKHSKKGM DNQGHKNLKT SQEGSSDDAE RKQERETFSS AEGTVDKDTT 

       910        920        930        940        950        960 
IMELRDRLPK KQQASASTDG VDKLSGKEQS FTSLEVRKVA ETKEKSKHLK TKTCKKVQDG 

       970        980        990       1000       1010       1020 
LSDIAEKFLK KDQSDETSED DKKQSKKGTE EKKKPSDFKK KVIKMEQQYE SSSDGTEKLP 

      1030       1040       1050       1060       1070       1080 
EREEICHFPK GIKQIKNGTT DGEKKSKKIR DKTSKKKDEL SDYAEKSTGK GDSCDSSEDK 

      1090       1100       1110       1120       1130       1140 
KSKNGAYGRE KKRCKLLGKS SRKRQDCSSS DTEKYSMKED GCNSSDKRLK RIELRERRNL 

      1150       1160       1170       1180       1190       1200 
SSKRNTKEIQ SGSSSSDAEE SSEDNKKKKQ RTSSKKKAVI VKEKKRNSLR TSTKRKQADI 

      1210       1220       1230       1240       1250       1260 
TSSSSSDIED DDQNSIGEGS SDEQKIKPVT ENLVLSSHTG FCQSSGDEAL SKSVPVTVDD 

      1270       1280       1290       1300       1310       1320 
DDDDNDPENR IAKKMLLEEI KANLSSDEDG SSDDEPEEGK KRTGKQNEEN PGDEEAKNQV 

      1330       1340       1350       1360       1370       1380 
NSESDSDSEE SKKPRYRHRL LRHKLTVSDG ESGEEKKTKP KEHKEVKGRN RRKVSSEDSE 

      1390       1400       1410       1420       1430       1440 
DSDFQESGVS EEVSESEDEQ RPRTRSAKKA ELEENQRSYK QKKKRRRIKV QEDSSSENKS 

      1450       1460       1470       1480       1490       1500 
NSEEEEEEKE EEEEEEEEEE EEEEDENDDS KSPGKGRKKI RKILKDDKLR TETQNALKEE 

      1510       1520       1530       1540       1550       1560 
EERRKRIAER EREREKLREV IEIEDASPTK CPITTKLVLD EDEETKEPLV QVHRNMVIKL 

      1570       1580       1590       1600       1610       1620 
KPHQVDGVQF MWDCCCESVK KTKKSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFS 

      1630       1640       1650       1660       1670       1680 
TALVVCPLNT ALNWMNEFEK WQEGLKDDEK LEVSELATVK RPQERSYMLQ RWQEDGGVMI 

      1690       1700       1710       1720       1730       1740 
IGYEMYRNLA QGRNVKSRKL KEIFNKALVD PGPDFVVCDE GHILKNEASA VSKAMNSIRS 

      1750       1760       1770       1780       1790       1800 
RRRIILTGTP LQNNLIEYHC MVNFIKENLL GSIKEFRNRF INPIQNGQCA DSTMVDVRVM 

      1810       1820       1830       1840       1850       1860 
KKRAHILYEM LAGCVQRKDY TALTKFLPPK HEYVLAVRMT SIQCKLYQYY LDHLTGVGNN 

      1870       1880       1890       1900       1910       1920 
SEGGRGKAGA KLFQDFQMLS RIWTHPWCLQ LDYISKENKG YFDEDSMDEF IASDSDETSM 

      1930       1940       1950       1960       1970       1980 
SLSSDDYTKK KKKGKKGKKD SSSSGSGSDN DVEVIKVWNS RSRGGGEGNV DETGNNPSVS 

      1990       2000       2010       2020       2030       2040 
LKLEESKATS SSNPSSPAPD WYKDFVTDAD AEVLEHSGKM VLLFEILRMA EEIGDKVLVF 

      2050       2060       2070       2080       2090       2100 
SQSLISLDLI EDFLELASRE KTEDKDKPLI YKGEGKWLRN IDYYRLDGST TAQSRKKWAE 

      2110       2120       2130       2140       2150       2160 
EFNDETNVRG RLFIISTKAG SLGINLVAAN RVIIFDASWN PSYDIQSIFR VYRFGQTKPV 

      2170       2180       2190       2200       2210       2220 
YVYRFLAQGT MEDKIYDRQV TKQSLSFRVV DQQQVERHFT MNELTELYTF EPDLLDDPNS 

      2230       2240       2250       2260       2270       2280 
EKKKKRDTPM LPKDTILAEL LQIHKEHIVG YHEHDSLLDH KEEEELTEEE RKAAWAEYEA 

      2290       2300       2310       2320       2330       2340 
EKKGLTMRFN IPTGTNLPPV SFNSQTPYIP FNLGALSAMS NQQLEDLINQ GREKVVEATN 

      2350       2360       2370       2380       2390       2400 
SVTAVRIQPL EDIISAVWKE NMNLSEAQVQ ALALSRQASQ ELDVKRREAI YNDVLTKQQM 

      2410       2420       2430       2440       2450       2460 
LISCVQRILM NRRLQQQYNQ QQQQQMTYQQ ATLGHLMMPK PPNLIMNPSN YQQIDMRGMY 

      2470       2480       2490 
QPVAGGMQPP PLQRAPPPMR SKNPGPSQGK SM

« Hide

Isoform 1.

Checksum: F88BE152771C8B38
Show »

FASTA2,288259,781
Isoform 2.

Checksum: 20B4375FF0F030C8
Show »

FASTA2,375269,749
Isoform 3.

Checksum: BE335573100AB865
Show »

FASTA2,454278,167
Isoform 5.

Checksum: 10D21D37906BD9A5
Show »

FASTA2,337265,392
Isoform 6.

Checksum: A5AE88D0B27BE1B8
Show »

FASTA1,350151,484

Hide | Top

References

« Hide 'large scale' references
[1]"ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome."
Picketts D.J., Higgs D.R., Bachoo S., Blake D.J., Quarrell O.W.J., Gibbons R.J.
Hum. Mol. Genet. 5:1899-1907(1996) [PubMed: 8968741] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), VARIANTS SER-596; GLU-740 AND SER-1860, VARIANTS ATR-X.
[2]"Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase."
Villard L., Lossi A.-M., Cardoso C., Proud V., Chiaroni P., Colleaux L., Schwartz C., Fontes M.
Genomics 43:149-155(1997) [PubMed: 9244431] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
[3]"Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
Kitano T., Schwarz C., Nickel B., Paeaebo S.
Mol. Biol. Evol. 20:1281-1289(2003) [PubMed: 12777533] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 163-198, VARIANTS SER-596 AND GLU-740.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 704-1927 (ISOFORMS 1/2/3/4/5), VARIANTS GLU-740 AND GLU-929.
Tissue: Brain.
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS SER-596 AND GLU-740.
[6]"Cloning and characterization of a new human Xq13 gene, encoding a putative helicase."
Stayton C.L., Dabovic B., Gulisano M., Gecz J., Broccoli V., Giovanazzi S., Bossolasco M., Monaco L., Rastan S., Boncinelli E., Bianchi M.E., Consalez G.G.
Hum. Mol. Genet. 3:1957-1964(1994) [PubMed: 7874112] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 860-2492.
[7]"Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3."
Gecz J., Pollard H., Consalez G., Villard L., Stayton C.L., Millasseau P., Khrestchatisky M., Fontes M.
Hum. Mol. Genet. 3:39-44(1994) [PubMed: 8162050] [Abstract]
Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome)."
Gibbons R.J., Picketts D.J., Villard L., Higgs D.R.
Cell 80:837-845(1995) [PubMed: 7697714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2401-2492, VARIANTS ATR-X.
[9]"Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein."
Cardoso C., Timsit S., Villard L., Khrestchatisky M., Fontes M., Colleaux L.
Hum. Mol. Genet. 7:679-684(1998) [PubMed: 9499421] [Abstract]
Cited for: INTERACTION WITH EZH2.
[10]"Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes."
McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M., Bickmore W.A., Pombo A., Turley H., Gatter K., Picketts D.J., Buckle V.J., Chapman L., Rhodes D., Higgs D.R.
Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999) [PubMed: 10570185] [Abstract]
Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH PERICENTROMERIC HETEROCHROMATIN.
[11]"Identification of a mutation in the XNP/ATR-X gene in a family reported as Smith-Fineman-Myers syndrome."
Villard L., Fontes M., Ades L.C., Gecz J.
Am. J. Med. Genet. 91:83-85(2000) [PubMed: 10751095] [Abstract]
Cited for: INVOLVEMENT IN MRXSHF1.
[12]"Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS)."
Gibbons R.J., Pellagatti A., Garrick D., Wood W.G., Malik N., Ayyub H., Langford C., Boultwood J., Wainscoat J.S., Higgs D.R.
Nat. Genet. 34:446-449(2003) [PubMed: 12858175] [Abstract]
Cited for: INVOLVEMENT IN ATMDS.
[13]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, MASS SPECTROMETRY.
Tissue: Epithelium.
[14]"The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain."
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III
Biochem. Biophys. Res. Commun. 331:929-937(2005) [PubMed: 15882967] [Abstract]
Cited for: INTERACTION WITH CBX5.
[15]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-634; SER-729; SER-731; SER-849; SER-850; SER-1348; SER-1352 AND SER-1527, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87, MASS SPECTROMETRY.
Tissue: Epithelium.
[17]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-74, MASS SPECTROMETRY.
[18]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871, MASS SPECTROMETRY.
[19]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594; SER-598; THR-674; SER-675; SER-677; SER-729; SER-731; SER-871; SER-875; SER-876; SER-1348; SER-1352; SER-1991; SER-1996 AND SER-2220, MASS SPECTROMETRY.
[20]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729; SER-731; SER-1348; SER-1352; SER-1991; SER-1992 AND SER-1996, MASS SPECTROMETRY.
[21]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; TYR-89; SER-112; SER-729; SER-731 AND SER-1996, MASS SPECTROMETRY.
Tissue: T-cell.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-967, MASS SPECTROMETRY.
[23]"Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX."
Argentaro A., Yang J.C., Chapman L., Kowalczyk M.S., Gibbons R.J., Higgs D.R., Neuhaus D., Rhodes D.
Proc. Natl. Acad. Sci. U.S.A. 104:11939-11944(2007) [PubMed: 17609377] [Abstract]
Cited for: STRUCTURE BY NMR OF 159-296, DOMAIN GATA-TYPE ZINC FINGER.
[24]"A point mutation in the XNP gene, associated with an ATR-X phenotype without alpha-thalassemia."
Villard L., Lacombe D., Fontes M.
Eur. J. Hum. Genet. 4:316-320(1996) [PubMed: 9043863] [Abstract]
Cited for: VARIANT ATR-X SER-1713.
[25]"XNP mutation in a large family with Juberg-Marsidi syndrome."
Villard L., Gecz J., Mattei J.-F., Fontes M., Saugier-Veber P., Munnich A., Lyonnet S.
Nat. Genet. 12:359-360(1996) [PubMed: 8630485] [Abstract]
Cited for: VARIANT MRXSHF1 GLN-2131.
[26]"Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain."
Gibbons R.J., Bachoo S., Picketts D.J., Aftimos S., Asenbauer B., Bergoffen J., Berry S.A., Dahl N., Fryer A., Keppler K., Kurosawa K., Levin M.L., Masuno M., Neri G., Pierpont M.E., Slaney S.F., Higgs D.R.
Nat. Genet. 17:146-148(1997) [PubMed: 9326931] [Abstract]
Cited for: VARIANTS ATR-X.
[27]"New mutations in XNP/ATR-X gene: a further contribution to genotype/phenotype relationship in ATR/X syndrome."
Fichera M., Romano C., Castiglia L., Failla P., Ruberto C., Amata S., Greco D., Cardoso C., Fontes M., Ragusa A.
Hum. Mutat. 12:214-214(1998) [PubMed: 10660327] [Abstract]
Cited for: VARIANT ATR-X LEU-246.
[28]"Mutation of the XNP/ATR-X gene in a family with severe mental retardation, spastic paraplegia and skewed pattern of X inactivation: demonstration that the mutation is involved in the inactivation bias."
Lossi A.-M., Millan J.M., Villard L., Orellana C., Cardoso C., Prieto F., Fontes M., Martinez F.
Am. J. Hum. Genet. 65:558-562(1999) [PubMed: 10417298] [Abstract]
Cited for: VARIANT ATR-X LYS-1742.
[29]"Carpenter-Waziri syndrome results from a mutation in XNP."
Abidi F., Schwartz C.E., Carpenter N.J., Villard L., Fontes M., Curtis M.
Am. J. Med. Genet. 85:249-251(1999) [PubMed: 10398237] [Abstract]
Cited for: VARIANT MRXSHF1 THR-2050.
[30]"Evaluation of a mutation screening strategy for sporadic cases of ATR-X syndrome."
Villard L., Bonino M.-C., Abidi F., Ragusa A., Belougne J., Lossi A.-M., Seaver L., Bonnefont J.-P., Romano C., Fichera M., Lacombe D., Hanauer A., Philip N., Schwartz C.E., Fontes M.
J. Med. Genet. 36:183-186(1999) [PubMed: 10204841] [Abstract]
Cited for: VARIANTS ATR-X GLU-175; 178-VAL--LYS-198 DEL; SER-190; PRO-219; LEU-246 AND CYS-249.
[31]"Molecular genetic study of Japanese patients with X-linked alpha-thalassemia/mental retardation syndrome (ATR-X)."
Wada T., Kubota T., Fukushima Y., Saitoh S.
Am. J. Med. Genet. 94:242-248(2000) [PubMed: 10995512] [Abstract]
Cited for: VARIANTS ATR-X SER-179; LEU-190; ILE-194; CYS-246; PHE-1552; SER-1645 AND CYS-1847.
[32]"Holmes-Gang syndrome is allelic with XLMR-hypotonic face syndrome."
Stevenson R.E., Abidi F., Schwartz C.E., Lubs H.A., Holmes L.B.
Am. J. Med. Genet. 94:383-385(2000) [PubMed: 11050622] [Abstract]
Cited for: VARIANT MRXSHF1 TYR-220.
[33]"Expanding phenotype of XNP mutations: mild to moderate mental retardation."
Yntema H.G., Poppelaars F.A., Derksen E., Oudakker A.R., van Roosmalen T., Jacobs A., Obbema H., Brunner H.G., Hamel B.C.J., van Bokhoven H.
Am. J. Med. Genet. 110:243-247(2002) [PubMed: 12116232] [Abstract]
Cited for: VARIANT ATR-X MET-1621.
[34]"Asplenia in ATR-X syndrome: a second report."
Leahy R.T., Philip R.K., Gibbons R.J., Fisher C., Suri M., Reardon W.
Am. J. Med. Genet. A 139:37-39(2005) [PubMed: 16222662] [Abstract]
Cited for: VARIANT MRXSHF1 GLY-2271.
[35]"A missense mutation in the coiled-coil motif of the HP1-interacting domain of ATR-X in a family with X-linked mental retardation."
Wieland I., Sabathil J., Ostendorf A., Rittinger O., Roepke A., Winnepenninckx B., Kooy F., Holinski-Feder E., Wieacker P.
Neurogenetics 6:45-47(2005) [PubMed: 15565397] [Abstract]
Cited for: VARIANT MRXSHF1 SER-409.
[36]"ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn finger domain and a totally skewed X-inactivation pattern."
Badens C., Martini N., Courrier S., DesPortes V., Touraine R., Levy N., Edery P.
Am. J. Med. Genet. A 140:2212-2215(2006) [PubMed: 16955409] [Abstract]
Cited for: VARIANT ATR-X CYS-246.
+Additional computationally mapped references.

Hide | Top

Web resources

GeneReviews

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U72937 mRNA. Translation: AAB49970.2.
U72938 mRNA. Translation: AAB49971.2.
U72935 expand/collapse EMBL AC list , U72904, U72905, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40698.1.
U72935 expand/collapse EMBL AC list , U72904, U72907, U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72918, U72919, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40699.1.
U72936 mRNA. Translation: AAB49969.1.
U72935 expand/collapse EMBL AC list , U72908, U72909, U72910, U72911, U72912, U72913, U72914, U72915, U72916, U72917, U72918, U72920, U72921, U72922, U72923, U72924, U72925, U72926, U72927, U72928, U72929, U72930, U72931, U72932, U72933, U72934 Genomic DNA. Translation: AAB40700.1.
U75653 Genomic DNA. Translation: AAC51655.1.
U97103 expand/collapse EMBL AC list , AF000157, AF000158, AF000159, AF000160, U97080, U97081, U97082, U97083, U97084, U97085, U97086, U97087, U97088, U97089, U97090, U97091, U97092, U97093, U97094, U97095, U97096, U97097, U97098, U97099, U97100, U97101, U97102 Genomic DNA. Translation: AAC51657.1.
AB102641 mRNA. Translation: BAC81110.1.
AB101681 Genomic DNA. Translation: BAC80270.1.
AB101682 Genomic DNA. Translation: BAC80271.1.
AB101683 Genomic DNA. Translation: BAC80272.1.
AB101685 Genomic DNA. Translation: BAC80274.1.
AB101687 Genomic DNA. Translation: BAC80276.1.
AB101689 Genomic DNA. Translation: BAC80278.1.
AB101691 Genomic DNA. Translation: BAC80280.1.
AB101693 Genomic DNA. Translation: BAC80282.1.
AB101695 Genomic DNA. Translation: BAC80284.1.
AB101700 Genomic DNA. Translation: BAC80289.1.
AB101699 Genomic DNA. Translation: BAC80288.1.
AB101698 Genomic DNA. Translation: BAC80287.1.
AB101697 Genomic DNA. Translation: BAC80286.1.
AB101696 Genomic DNA. Translation: BAC80285.1.
AB101694 Genomic DNA. Translation: BAC80283.1.
AB101692 Genomic DNA. Translation: BAC80281.1.
AB101690 Genomic DNA. Translation: BAC80279.1.
AB101688 Genomic DNA. Translation: BAC80277.1.
AB101686 Genomic DNA. Translation: BAC80275.1.
AB101684 Genomic DNA. Translation: BAC80273.1.
AB208928 mRNA. Translation: BAD92165.1. Different initiation.
AB209545 mRNA. Translation: BAD92782.1.
AL121874 Genomic DNA. Translation: CAB90351.2.
AL121874, AL109753, Z84487 Genomic DNA. Translation: CAI40710.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42674.1.
Z84487, AL109753, AL121874 Genomic DNA. Translation: CAI42675.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43115.1.
AL109753, AL121874, Z84487 Genomic DNA. Translation: CAI43116.1.
U09820 mRNA. Translation: AAC50069.1.
L34363 Genomic DNA. Translation: AAA20872.1. Sequence problems.
X83753 Genomic DNA. Translation: CAA58711.1.
IPIIPI00220109.
IPI00297633.
IPI00845355.
IPI00883721.
IPI00938010.
IPI00940810.
PIRI38614.
I54367.
RefSeqNP_000480.2.
NP_612114.1.
UniGeneHs.533526
Hs.653797

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JM1NMR-A159-296[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP46100. 8 interactions.
STRINGP46100.

PTM databases

PhosphoSiteP46100.

Proteomic databases

PRIDEP46100.

Genome annotation databases

EnsemblENST00000373344; ENSP00000362441; ENSG00000085224; Homo sapiens. [Genome view]
GeneID546.
KEGGhsa:546.
UCSCuc004eco.2. human.

Organism-specific databases

CTD546.
GeneCardsGC0XM076567.
GC0XM076647.
HGNCHGNC:886. ATRX.
HPACAB009372.
HPA001906.
MIM300032. gene.
300448. phenotype.
301040. phenotype.
309580. phenotype.
Orphanet847. Alpha thalassemia - intellectual deficit, X-linked.
93973. Carpenter-Waziri syndrome.
93971. Chudley-Lowry-Hoar syndrome.
93970. Holmes-Gang syndrome.
73220. Intellectual deficit, X-linked - hypotonic face.
93972. Juberg-Marsidi syndrome.
93974. Smith-Fineman-Myers syndrome.
PharmGKBPA25179.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05984.
HOVERGENP46100.
InParanoidP46100.

Gene expression databases

ArrayExpressP46100.
BgeeP46100.
CleanExHS_RAD54L.
GenevestigatorP46100.
GermOnlineENSG00000085224. Homo sapiens.

Family and domain databases

InterProIPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR000330. SNF2_N.
IPR011011. Znf_FYVE_PHD.
IPR001841. Znf_RING.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00344. GATA_ZN_FINGER_1. False negative.
PS50114. GATA_ZN_FINGER_2. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. False negative.
PS50016. ZF_PHD_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00144. Phosphatidylserine.
NextBio2259.
SOURCESearch...

Hide | Top

Entry information

Entry nameATRX_HUMAN
AccessionPrimary (citable) accession number: P46100
Secondary accession number(s): P51068 expand/collapse secondary AC list , Q15886, Q59FB5, Q59H31, Q5H9A2, Q5JWI4, Q7Z2J1, Q9H0Z1, Q9NTS3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 16, 2008
Last modified: January 19, 2010
This is version 120 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Hide | Top

Relevant documents

Human chromosome X

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents