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Q9HBE1 (PATZ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
POZ-, AT hook-, and zinc finger-containing protein 1
Alternative name(s):
BTB/POZ domain zinc finger transcription factor
Protein kinase A RI subunit alpha-associated protein
Zinc finger and BTB domain-containing protein 19
Zinc finger protein 278
Zinc finger sarcoma gene protein
Gene names
Name:PATZ1
Synonyms:PATZ, RIAZ, ZBTB19, ZNF278, ZSG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length687 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor. Ref.1

Subcellular location

Nucleus Ref.1.

Tissue specificity

Ubiquitous.

Involvement in disease

A chromosomal aberration involving PATZ1 is associated with small round cell sarcoma. Translocation t(1;22)(p36.1;q12) with EWSR1.

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 1 A.T hook DNA-binding domain.

Contains 1 BTB (POZ) domain.

Contains 7 C2H2-type zinc fingers.

Sequence caution

The sequence CAB51404.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HBE1-1)

Also known as: C;

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: Q9HBE1-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     504-537: FSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGA → LQAPGAHPEWGSSVPLRQDLWQQRRPEMLTSGSD
     538-687: Missing.
Isoform 3 (identifier: Q9HBE1-3)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     503-548: Missing.
Isoform 4 (identifier: Q9HBE1-4)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     446-537: TCNASFATRD...HQEPILNGGA → VWVGSSSGLP...SRAFTQWPVG
     538-687: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 687687POZ-, AT hook-, and zinc finger-containing protein 1
PRO_0000047504

Regions

Domain41 – 13090BTB
DNA binding264 – 27613A.T hook
Zinc finger292 – 31423C2H2-type 1
Zinc finger355 – 37723C2H2-type 2
Zinc finger383 – 40523C2H2-type 3
Zinc finger413 – 43624C2H2-type 4
Zinc finger442 – 46423C2H2-type 5
Zinc finger495 – 51824C2H2-type 6
Zinc finger605 – 62824C2H2-type 7

Amino acid modifications

Modified residue2821Phosphoserine Ref.8

Natural variations

Alternative sequence446 – 53792TCNAS…LNGGA → VWVGSSSGLPPLEPLPSDLP SWDFAQPALWRSSHSVPDTA FSLSLKKSFPALENLGPAHS SNTLFCPAPPGYLRQGWTTP EGSRAFTQWPVG in isoform 4.
VSP_008802
Alternative sequence503 – 54846Missing in isoform 3.
VSP_008801
Alternative sequence504 – 53734FSSAS…LNGGA → LQAPGAHPEWGSSVPLRQDL WQQRRPEMLTSGSD in isoform 2.
VSP_008799
Alternative sequence538 – 687150Missing in isoform 2 and isoform 4.
VSP_008800
Natural variant6851E → D.
Corresponds to variant rs2240424 [ dbSNP | Ensembl ].
VAR_052724

Experimental info

Sequence conflict631S → N in AAF32518. Ref.1
Sequence conflict2591P → L in AAF32518. Ref.1
Sequence conflict3941R → K in AAF32518. Ref.1

Secondary structure

.......................... 687
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (C) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 0F1C59A78C6D110A

FASTA68774,060
        10         20         30         40         50         60 
MERVNDASCG PSGCYTYQVS RHSTEMLHNL NQQRKNGGRF CDVLLRVGDE SFPAHRAVLA 

        70         80         90        100        110        120 
ACSEYFESVF SAQLGDGGAA DGGPADVGGA TAAPGGGAGG SRELEMHTIS SKVFGDILDF 

       130        140        150        160        170        180 
AYTSRIVVRL ESFPELMTAA KFLLMRSVIE ICQEVIKQSN VQILVPPARA DIMLFRPPGT 

       190        200        210        220        230        240 
SDLGFPLDMT NGAALAANSN GIAGSMQPEE EAARAAGAAI AGQASLPVLP GVDRLPMVAG 

       250        260        270        280        290        300 
PLSPQLLTSP FPSVASSAPP LTGKRGRGRP RKANLLDSMF GSPGGLREAG ILPCGLCGKV 

       310        320        330        340        350        360 
FTDANRLRQH EAQHGVTSLQ LGYIDLPPPR LGENGLPISE DPDGPRKRSR TRKQVACEIC 

       370        380        390        400        410        420 
GKIFRDVYHL NRHKLSHSGE KPYSCPVCGL RFKRKDRMSY HVRSHDGSVG KPYICQSCGK 

       430        440        450        460        470        480 
GFSRPDHLNG HIKQVHTSER PHKCQTCNAS FATRDRLRSH LACHEDKVPC QVCGKYLRAA 

       490        500        510        520        530        540 
YMADHLKKHS EGPSNFCSIC NRGFSSASYL KVHVKTHHGV PLPQVSRHQE PILNGGAAFH 

       550        560        570        580        590        600 
CARTYGNKEG QKCSHQDPIE SSDSYGDLSD ASDLKTPEKQ SANGSFSCDM AVPKNKMESD 

       610        620        630        640        650        660 
GEKKYPCPEC GSFFRSKSYL NKHIQKVHVR ALGGPLGDLG PALGSPFSPQ QNMSLLESFG 

       670        680 
FQIVQSAFAS SLVDPEVDQQ PMGPEGK 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 950792413BF1F5DB
Show »

FASTA53757,995
Isoform 3 (A) [UniParc].

Checksum: 29515535E380F0CE
Show »

FASTA64169,079
Isoform 4 (Short) [UniParc].

Checksum: BA4A909E24800F13
Show »

FASTA53757,601

References

« Hide 'large scale' references
[1]"A novel member of the BTB/POZ family, PATZ, associates with the RNF4 RING finger protein and acts as a transcriptional repressor."
Fedele M., Benvenuto G., Pero R., Majello B., Battista S., Lembo F., Vollono E., Day P.M., Santoro M., Lania L., Bruni C.B., Fusco A., Chiatiotti L.
J. Biol. Chem. 275:7894-7901(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH RNF4.
[2]"A novel zinc finger gene is fused to EWS in small round cell tumor."
Mastrangelo T., Modena P., Tornielli S., Bullrich F., Testi A., Mezzelani A., Radice P., Azzarelli A., Pilotti S., Croce C., Pierotti M., Sozzi G.
Oncogene 19:3799-3804(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), CHROMOSOMAL TRANSLOCATION WITH EWSR1.
[3]"Novel cAMP signalling via the regulatory subunit of the cAMP-dependent protein kinase."
Chin K.-V., Yang W.-L., Kudoh K.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 3).
[4]Collins J.E., Huckle E.J.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 4).
Tissue: Colon.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Solution structure of zinc finger domains in zinc finger protein 278."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 359-437.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF119256 mRNA. Translation: AAF32518.1.
AF254082 mRNA. Translation: AAG09031.1.
AF254083 mRNA. Translation: AAG09032.1.
AF254084 mRNA. Translation: AAG09033.1.
AF254085 mRNA. Translation: AAG09034.1.
AY028384 mRNA. Translation: AAK19024.1.
AL096880 mRNA. Translation: CAB51404.1. Different initiation.
CR456613 mRNA. Translation: CAG30499.1.
AC005003 Genomic DNA. Translation: AAF01349.1.
BC021091 mRNA. Translation: AAH21091.1.
RefSeqNP_055138.2. NM_014323.2.
NP_114439.1. NM_032050.1.
NP_114440.1. NM_032051.1.
NP_114441.1. NM_032052.1.
UniGeneHs.731398.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EPPNMR-A285-339[»]
2EPQNMR-A378-411[»]
2EPRNMR-A350-384[»]
2EPSNMR-A407-445[»]
2YT9NMR-A355-436[»]
ProteinModelPortalQ9HBE1.
SMRQ9HBE1. Positions 10-152, 281-670.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117133. 9 interactions.
STRING9606.ENSP00000266269.

PTM databases

PhosphoSiteQ9HBE1.

Polymorphism databases

DMDM38258840.

Proteomic databases

PaxDbQ9HBE1.
PRIDEQ9HBE1.

Protocols and materials databases

DNASU23598.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215919; ENSP00000215919; ENSG00000100105. [Q9HBE1-4]
ENST00000266269; ENSP00000266269; ENSG00000100105. [Q9HBE1-1]
ENST00000351933; ENSP00000337520; ENSG00000100105. [Q9HBE1-3]
ENST00000405309; ENSP00000384173; ENSG00000100105. [Q9HBE1-2]
GeneID23598.
KEGGhsa:23598.
UCSCuc003akp.3. human. [Q9HBE1-2]
uc003akq.3. human. [Q9HBE1-1]
uc003akr.3. human. [Q9HBE1-3]
uc003aks.3. human. [Q9HBE1-4]

Organism-specific databases

CTD23598.
GeneCardsGC22M031721.
HGNCHGNC:13071. PATZ1.
HPAHPA047893.
MIM605165. gene.
neXtProtNX_Q9HBE1.
PharmGKBPA162398806.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000037943.
HOVERGENHBG056645.
InParanoidQ9HBE1.
OMACPHLESE.
OrthoDBEOG79SDWK.
PhylomeDBQ9HBE1.
TreeFamTF331686.

Gene expression databases

ArrayExpressQ9HBE1.
BgeeQ9HBE1.
CleanExHS_PATZ1.
GenevestigatorQ9HBE1.

Family and domain databases

Gene3D3.30.160.60. 6 hits.
3.30.710.10. 1 hit.
InterProIPR017956. AT_hook_DNA-bd_motif.
IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR000637. HMGI/Y_DNA-bd_CS.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 2 hits.
[Graphical view]
SMARTSM00384. AT_hook. 2 hits.
SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 2 hits.
PROSITEPS50097. BTB. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPATZ1. human.
EvolutionaryTraceQ9HBE1.
GeneWikiPATZ1.
GenomeRNAi23598.
NextBio46268.
PROQ9HBE1.
SOURCESearch...

Entry information

Entry namePATZ1_HUMAN
AccessionPrimary (citable) accession number: Q9HBE1
Secondary accession number(s): Q9HBE2 expand/collapse secondary AC list , Q9HBE3, Q9P1A9, Q9UDU0, Q9Y529
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM