Q9HBE1 (PATZ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	687 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell differentiation Inferred from electronic annotation. Source: Ensembl male gonad development Inferred from electronic annotation. Source: Ensembl negative regulation of transcription, DNA-templated Traceable author statement Ref.1. Source: UniProtKB positive regulation of transcription, DNA-templated Inferred from electronic annotation. Source: Ensembl regulation of transcription, DNA-templated Traceable author statement Ref.1. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: Ensembl transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Traceable author statement Ref.1. Source: UniProtKB
Molecular_function	DNA binding Non-traceable author statement Ref.2. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: Ensembl metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 687

687

POZ-, AT hook-, and zinc finger-containing protein 1

PRO_0000047504

Regions

Domain

41 – 130

90

BTB

DNA binding

264 – 276

13

A.T hook

Zinc finger

292 – 314

23

C2H2-type 1

Zinc finger

355 – 377

23

C2H2-type 2

Zinc finger

383 – 405

23

C2H2-type 3

Zinc finger

413 – 436

24

C2H2-type 4

Zinc finger

442 – 464

23

C2H2-type 5

Zinc finger

495 – 518

24

C2H2-type 6

Zinc finger

605 – 628

24

C2H2-type 7

Amino acid modifications

Modified residue

282

1

Phosphoserine Ref.8

Natural variations

Alternative sequence

446 – 537

92

TCNAS…LNGGA → VWVGSSSGLPPLEPLPSDLP SWDFAQPALWRSSHSVPDTA FSLSLKKSFPALENLGPAHS SNTLFCPAPPGYLRQGWTTP EGSRAFTQWPVG in isoform 4.

VSP_008802

Alternative sequence

503 – 548

46

Missing in isoform 3.

VSP_008801

Alternative sequence

504 – 537

34

FSSAS…LNGGA → LQAPGAHPEWGSSVPLRQDL WQQRRPEMLTSGSD in isoform 2.

VSP_008799

Alternative sequence

538 – 687

150

Missing in isoform 2 and isoform 4.

VSP_008800

Natural variant

685

1

E → D.
Corresponds to variant rs2240424 [ dbSNP | Ensembl ].

VAR_052724

Experimental info

Sequence conflict

63

1

S → N in AAF32518. Ref.1

Sequence conflict

259

1

P → L in AAF32518. Ref.1

Sequence conflict

394

1

R → K in AAF32518. Ref.1

Secondary structure

1

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687

Helix Strand Turn

Details...

Turn

295 – 297

3

Helix

304 – 314

11

Turn

315 – 317

3

Beta strand

354 – 357

4

Turn

358 – 361

4

Beta strand

362 – 366

5

Helix

367 – 373

7

Helix

374 – 376

3

Beta strand

382 – 385

4

Turn

386 – 389

4

Beta strand

391 – 393

3

Helix

395 – 405

11

Beta strand

411 – 413

3

Beta strand

416 – 418

3

Beta strand

421 – 424

4

Helix

425 – 434

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (C) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 0F1C59A78C6D110A	FASTA	687	74,060
	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
	Isoform 2 (B) [UniParc]. Checksum: 950792413BF1F5DB	FASTA	537	57,995
	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 YMADHLKKHS EGPSNFCSIC NRGLQAPGAH PEWGSSVPLR QDLWQQRRPE MLTSGSD
	Isoform 3 (A) [UniParc]. Checksum: 29515535E380F0CE	FASTA	641	69,079
	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 NREGQKCSHQ DPIESSDSYG DLSDASDLKT PEKQSANGSF 550 560 570 580 590 600 SCDMAVPKNK MESDGEKKYP CPECGSFFRS KSYLNKHIQK VHVRALGGPL GDLGPALGSP 610 620 630 640 FSPQQNMSLL ESFGFQIVQS AFASSLVDPE VDQQPMGPEG K
	Isoform 4 (Short) [UniParc]. Checksum: BA4A909E24800F13	FASTA	537	57,601
	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 PHKCQVWVGS SSGLPPLEPL PSDLPSWDFA QPALWRSSHS 490 500 510 520 530 VPDTAFSLSL KKSFPALENL GPAHSSNTLF CPAPPGYLRQ GWTTPEGSRA FTQWPVG

References

	« Hide 'large scale' referencesShow '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. , 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.

CCDS

CCDS13894.1. [Q9HBE1-1]
CCDS13895.1. [Q9HBE1-3]
CCDS13896.1. [Q9HBE1-4]
CCDS46691.1. [Q9HBE1-2]

RefSeq

NP_055138.2. NM_014323.2. [Q9HBE1-1]
NP_114439.1. NM_032050.1. [Q9HBE1-3]
NP_114440.1. NM_032051.1. [Q9HBE1-4]
NP_114441.1. NM_032052.1. [Q9HBE1-2]

UniGene

Hs.731398.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EPP	NMR	-	A	286-338	[»]
2EPQ	NMR	-	A	380-411	[»]
2EPR	NMR	-	A	350-384	[»]
2EPS	NMR	-	A	408-445	[»]
2YT9	NMR	-	A	355-436	[»]

ProteinModelPortal

Q9HBE1.

SMR

Q9HBE1. Positions 10-152, 281-637.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

117133. 9 interactions.

STRING

9606.ENSP00000266269.

PTM databases

PhosphoSite

Q9HBE1.

Polymorphism databases

DMDM

38258840.

Proteomic databases

MaxQB

Q9HBE1.

PaxDb

Q9HBE1.

PRIDE

Q9HBE1.

Protocols and materials databases

DNASU

23598.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215919; ENSP00000215919; ENSG00000100105. [Q9HBE1-4]
ENST00000266269; ENSP00000266269; ENSG00000100105. [Q9HBE1-1]
ENST00000351933; ENSP00000337520; ENSG00000100105. [Q9HBE1-3]
ENST00000405309; ENSP00000384173; ENSG00000100105. [Q9HBE1-2]

GeneID

23598.

KEGG

hsa:23598.

UCSC

uc003akp.3. human. [Q9HBE1-2]
uc003akq.3. human. [Q9HBE1-1]
uc003akr.3. human. [Q9HBE1-3]
uc003aks.3. human. [Q9HBE1-4]

Organism-specific databases

CTD

23598.

GeneCards

GC22M031721.

HGNC

HGNC:13071. PATZ1.

HPA

HPA047893.

MIM

605165. gene.

neXtProt

NX_Q9HBE1.

PharmGKB

PA162398806.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000037943.

HOVERGEN

HBG056645.

InParanoid

Q9HBE1.

OMA

MPEDEAT.

OrthoDB

EOG79SDWK.

PhylomeDB

Q9HBE1.

TreeFam

TF331686.

Gene expression databases

ArrayExpress

Q9HBE1.

Bgee

Q9HBE1.

CleanEx

HS_PATZ1.

Genevestigator

Q9HBE1.

Family and domain databases

Gene3D

3.30.160.60. 6 hits.
3.30.710.10. 1 hit.

InterPro

IPR017956. 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]

Pfam

PF00651. BTB. 1 hit.
PF00096. zf-C2H2. 2 hits.
[Graphical view]

SMART

SM00384. AT_hook. 2 hits.
SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]

SUPFAM

SSF54695. SSF54695. 2 hits.

PROSITE

PS50097. BTB. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PATZ1. human.

EvolutionaryTrace

Q9HBE1.

GeneWiki

PATZ1.

GenomeRNAi

23598.

NextBio

46268.

PRO

Q9HBE1.

SOURCE

Search...

Entry information

Entry name

PATZ1_HUMAN

Accession

Primary (citable) accession number: Q9HBE1
Secondary accession number(s): Q9HBE2 , Q9HBE3, Q9P1A9, Q9UDU0, Q9Y529

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	March 1, 2001
Last modified:	July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.