Reviewed, UniProtKB/Swiss-Prot Q9NRL2 (BAZ1A_HUMAN)

Names and origin

Protein names

Recommended name:
    Bromodomain adjacent to zinc finger domain protein 1A
Alternative name(s):
    ATP-utilizing chromatin assembly and remodeling factor 1
      Short name=hACF1
    ATP-dependent chromatin-remodeling protein
    Williams syndrome transcription factor-related chromatin-remodeling factor 180
      Short name=WCRF180
      Short name=hWALp1
    CHRAC subunit ACF1

Gene names

Name:	BAZ1A
Synonyms:	ACF1, WCRF180
ORF Names:	HSPC317

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1556 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in transcriptional regulation. May be involved in the formation or maintenance of heterochromatin playing a critical role in developmental control.
Subunit structure	Together with CHRAC1, POLE3 and SMARCA5 proteins, it forms the ISWI chromatin-remodeling complex, CHRAC.
Subcellular location	Nucleus. Note: May target the CHRAC complex to heterochromatin.
Tissue specificity	Highly expressed in testis and at low or undetectable levels in other tissues analyzed.
Miscellaneous	Stimulated by double-stranded DNA and nucleosomal DNA.
Sequence similarities	Belongs to the WAL family. Contains 1 bromo domain. Contains 1 DDT domain. Contains 1 PHD-type zinc finger. Contains 1 WAC domain.
Sequence caution	The sequence AAF28995.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Bromodomain Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NRL2-1)

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 2 (identifier: Q9NRL2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     504-535: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1556	1556	Bromodomain adjacent to zinc finger domain protein 1A		PRO_0000211167
Regions
	Domain	22 – 128	107	WAC
	Domain	422 – 487	66	DDT
	Domain	1446 – 1516	71	Bromo
	Zinc finger	1148 – 1198	51	PHD-type
	Coiled coil	306 – 397	92	Potential
	Coiled coil	634 – 709	76	Potential
Amino acid modifications
	Modified residue	270	1	Phosphoserine
	Modified residue	606	1	Phosphotyrosine Ref.7
	Modified residue	702	1	Phosphoserine
	Modified residue	731	1	Phosphothreonine
	Modified residue	1279	1	Phosphoserine Ref.8
	Modified residue	1281	1	Phosphoserine Ref.8
	Modified residue	1339	1	Phosphoserine Ref.10
	Modified residue	1353	1	Phosphoserine Ref.10
	Modified residue	1363	1	Phosphoserine Ref.10
	Modified residue	1367	1	Phosphothreonine Ref.10
	Modified residue	1371	1	Phosphoserine Ref.10
	Modified residue	1402	1	Phosphoserine Ref.10
	Modified residue	1413	1	Phosphoserine Ref.10 Ref.6 Ref.9
	Modified residue	1417	1	Phosphoserine Ref.10 Ref.6
	Modified residue	1547	1	Phosphothreonine Ref.10
Natural variations
	Alternative sequence	504 – 535	32	Missing in isoform 2.		VSP_000551
	Natural variant	344	1	D → E: dbSNP rs1133285.		VAR_028049
	Natural variant	1366	1	N → K: dbSNP rs1044140. Ref.1 Ref.5		VAR_048423
Experimental info
	Sequence conflict	135	1	R → T in BAA89209. Ref.3
	Sequence conflict	236	1	D → E in BAA89209. Ref.3
	Sequence conflict	494	1	K → Q in AAF28995. Ref.4
	Sequence conflict	503 – 508	6	KDLTEA → QDFTEP in AAF28995. Ref.4
	Sequence conflict	525	1	S → P in AAF28995. Ref.4
	Sequence conflict	536 – 540	5	GCSLK → AALKF in AAF28995. Ref.4
	Sequence conflict	551	1	E → D in AAF70601. Ref.1
	Sequence conflict	730	1	V → F in BAA89209. Ref.3
	Sequence conflict	769	1	P → L in BAA89209. Ref.3
	Sequence conflict	1201	1	S → C in BAA89209. Ref.3
	Sequence conflict	1206	1	S → F in BAA89209. Ref.3
	Sequence conflict	1409	1	R → K in AAF70601. Ref.1
	Sequence conflict	1409	1	R → K in CAB43261. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 4D78B9A8ADBF715B	FASTA	1,556	178,702
	10 20 30 40 50 60 MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP 70 80 90 100 110 120 GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE 130 140 150 160 170 180 TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK 190 200 210 220 230 240 KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK 250 260 270 280 290 300 IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY 310 320 330 340 350 360 RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER 370 380 390 400 410 420 LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL 430 440 450 460 470 480 PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA 490 500 510 520 530 540 IFQAIAEEEE EVAKEQLTDA DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK 550 560 570 580 590 600 SLDLDSCTLS EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL 610 620 630 640 650 660 SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE LKAEQHRKER 670 680 690 700 710 720 EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD ISIGEEERED FDTSIESKDT 730 740 750 760 770 780 EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ NGFKEFTRQE QINCVTREPL TADEEEALKQ 790 800 810 820 830 840 EHQRKEKELL EKIQSAIACT NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR 850 860 870 880 890 900 PSSFQNNVQS QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ 910 920 930 940 950 960 LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD SKPTYSRGRS 970 980 990 1000 1010 1020 SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV TDRHIWRSAL ESGRYELLSE 1030 1040 1050 1060 1070 1080 ENKENGIIKT VNEDVEEMEI DEQTKVIVKD RLLGIKTETP STVSTNASTP QSVSSVVHYL 1090 1100 1110 1120 1130 1140 AMALFQIEQG IERRFLKAPL DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV 1150 1160 1170 1180 1190 1200 IWSKSILNAR CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR 1210 1220 1230 1240 1250 1260 SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED DSQEEEEVSL 1270 1280 1290 1300 1310 1320 PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ STPKTTVSSK TGRSLRKINS 1330 1340 1350 1360 1370 1380 APPTETKSLR IASRSTRHSH GPLQADVFVE LLSPRRKRRG RKSANNTPEN SPNFPNFRVI 1390 1400 1410 1420 1430 1440 ATKSSEQSRS VNIASKLSLQ ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ 1450 1460 1470 1480 1490 1500 LVVELVRHDD SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL 1510 1520 1530 1540 1550 MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA AKKSRI
	Isoform 2. Checksum: 2DB787369178282B	FASTA	1,524	175,385
	10 20 30 40 50 60 MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP 70 80 90 100 110 120 GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE 130 140 150 160 170 180 TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK 190 200 210 220 230 240 KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK 250 260 270 280 290 300 IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY 310 320 330 340 350 360 RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER 370 380 390 400 410 420 LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL 430 440 450 460 470 480 PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA 490 500 510 520 530 540 IFQAIAEEEE EVAKEQLTDA DTKGCSLKSL DLDSCTLSEI LRLHILASGA DVTSANAKYR 550 560 570 580 590 600 YQKRGGFDAT DDACMELRLS NPSLVKKLSS TSVYDLTPGE KMKILHALCG KLLTLVSTRD 610 620 630 640 650 660 FIEDYVDILR QAKQEFRELK AEQHRKEREE AAARIRKRKE EKLKEQEQKM KEKQEKLKED 670 680 690 700 710 720 EQRNSTADIS IGEEEREDFD TSIESKDTEQ KELDQDMVTE DEDDPGSHKR GRRGKRGQNG 730 740 750 760 770 780 FKEFTRQEQI NCVTREPLTA DEEEALKQEH QRKEKELLEK IQSAIACTNI FPLGRDRMYR 790 800 810 820 830 840 RYWIFPSIPG LFIEEDYSGL TEDMLLPRPS SFQNNVQSQD PQVSTKTGEP LMSESTSNID 850 860 870 880 890 900 QGPRDHSVQL PKPVHKPNRW CFYSSCEQLD QLIEALNSRG HRESALKETL LQEKSRICAQ 910 920 930 940 950 960 LARFSEEKFH FSDKPQPDSK PTYSRGRSSN AYDPSQMCAE KQLELRLRDF LLDIEDRIYQ 970 980 990 1000 1010 1020 GTLGAIKVTD RHIWRSALES GRYELLSEEN KENGIIKTVN EDVEEMEIDE QTKVIVKDRL 1030 1040 1050 1060 1070 1080 LGIKTETPST VSTNASTPQS VSSVVHYLAM ALFQIEQGIE RRFLKAPLDA SDSGRSYKTV 1090 1100 1110 1120 1130 1140 LDRWRESLLS SASLSQVFLH LSTLDRSVIW SKSILNARCK ICRKKGDAEN MVLCDGCDRG 1150 1160 1170 1180 1190 1200 HHTYCVRPKL KTVPEGDWFC PECRPKQRSR RLSSRQRPSL ESDEDVEDSM GGEDDEVDGD 1210 1220 1230 1240 1250 1260 EEEGQSEEEE YEVEQDEDDS QEEEEVSLPK RGRPQVRLPV KTRGKLSSSF SSRGQQQEPG 1270 1280 1290 1300 1310 1320 RYPSRSQQST PKTTVSSKTG RSLRKINSAP PTETKSLRIA SRSTRHSHGP LQADVFVELL 1330 1340 1350 1360 1370 1380 SPRRKRRGRK SANNTPENSP NFPNFRVIAT KSSEQSRSVN IASKLSLQES ESKRRCRKRQ 1390 1400 1410 1420 1430 1440 SPEPSPVTLG RRSSGRQGGV HELSAFEQLV VELVRHDDSW PFLKLVSKIQ VPDYYDIIKK 1450 1460 1470 1480 1490 1500 PIALNIIREK VNKCEYKLAS EFIDDIELMF SNCFEYNPRN TSEAKAGTRL QAFFHIQAQK 1510 1520 LGLHVTPSNV DQVSTPPAAK KSRI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins." Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V., Becker P.B., Bickmore W.A., Varga-Weisz P.D. EMBO J. 19:3377-3387(2000) [PubMed: 10880450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MASS SPECTROMETRY, VARIANT LYS-1366. Tissue: Cervix carcinoma.
[2]	"A family of chromatin remodeling factors related to Williams syndrome transcription factor." Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J., Shiekhattar R. Proc. Natl. Acad. Sci. U.S.A. 97:1038-1043(2000) [PubMed: 10655480] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"A novel family of bromodomain genes." Jones M.H., Hamana N., Nezu J., Shimane M. Genomics 63:40-45(2000) [PubMed: 10662543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[4]	"Human partial CDS from CD34+ stem cells." Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-540 (ISOFORM 1). Tissue: Umbilical cord blood.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-1556 (ISOFORM 1), VARIANT LYS-1366. Tissue: Uterus.
[6]	"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-1413 AND SER-1417, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-606, MASS SPECTROMETRY.
[8]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1279 AND SER-1281, MASS SPECTROMETRY.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1413, MASS SPECTROMETRY.
[10]	"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-1339; SER-1353; SER-1363; THR-1367; SER-1371; SER-1402; SER-1413; SER-1417 AND THR-1547, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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-1402, MASS SPECTROMETRY.
[13]	"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-270; SER-702 AND THR-731, MASS SPECTROMETRY. Tissue: T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF213467 mRNA. Translation: AAF70601.1. AF221130 mRNA. Translation: AAF32366.1. AB032252 mRNA. Translation: BAA89209.1. AF161435 mRNA. Translation: AAF28995.1. Frameshift. AL050089 mRNA. Translation: CAB43261.1.
IPI	IPI00383565. IPI00412415.
PIR	T08738.
RefSeq	NP_038476.2. NP_872589.1.
UniGene	Hs.509140
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRL2. 2 interactions.
STRING	Q9NRL2.
PTM databases
PhosphoSite	Q9NRL2.
Genome annotation databases
Ensembl	ENST00000360310; ENSP00000353458; ENSG00000198604; Homo sapiens. [Genome view] ENST00000382422; ENSP00000371859; ENSG00000198604; Homo sapiens. [Genome view]
GeneID	11177.
KEGG	hsa:11177.
UCSC	uc001wsk.1. human. uc001wsl.1. human.
Organism-specific databases
CTD	11177.
GeneCards	GC14M034291.
H-InvDB	HIX0011594.
HGNC	HGNC:960. BAZ1A.
HPA	HPA002730.
MIM	605680. gene.
PharmGKB	PA25270.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG717122.
HOVERGEN	Q9NRL2.
InParanoid	Q9NRL2.
OMA	NGARLQC.
OrthoDB	EOG9N8TQT.
Gene expression databases
ArrayExpress	Q9NRL2.
Bgee	Q9NRL2.
CleanEx	HS_BAZ1A.
Genevestigator	Q9NRL2.
GermOnline	ENSG00000198604. Homo sapiens.
Family and domain databases
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR004022. DDT_dom. IPR018500. DDT_dom_subgr. IPR018501. DDT_dom_superfamily. IPR013136. WSTF_Acf1_Cbp146. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. [Graphical view]
Gene3D	G3DSA:1.20.920.10. Bromodomain. 1 hit.
Pfam	PF00439. Bromodomain. 1 hit. PF02791. DDT. 1 hit. PF00628. PHD. 1 hit. PF10537. WAC_Acf1_DNA_bd. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00571. DDT. 1 hit. SM00249. PHD. 1 hit. SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS50827. DDT. 1 hit. PS51136. WAC. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	42529.
SOURCE	Search...

Entry information

Entry name

BAZ1A_HUMAN

Accession

Primary (citable) accession number: Q9NRL2
Secondary accession number(s): Q9NZ15 , Q9P065, Q9UIG1, Q9Y3V3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	October 17, 2006
Last modified:	December 15, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.