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Q9HBE1

- PATZ1_HUMAN

UniProt

Q9HBE1 - PATZ1_HUMAN

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Protein

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

Gene

PATZ1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (4)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Transcriptional repressor.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi264 – 27613A.T hookAdd
BLAST
Zinc fingeri292 – 31423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri355 – 37723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri383 – 40523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri413 – 43624C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri442 – 46423C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri495 – 51824C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri605 – 62824C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. male gonad development Source: Ensembl
  2. negative regulation of transcription, DNA-templated Source: UniProtKB
  3. positive regulation of transcription, DNA-templated Source: Ensembl
  4. regulation of transcription, DNA-templated Source: UniProtKB
  5. spermatogenesis Source: Ensembl
  6. T cell differentiation Source: Ensembl
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:PATZ1
Synonyms:PATZ, RIAZ, ZBTB19, ZNF278, ZSG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:13071. PATZ1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA162398806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687POZ-, AT hook-, and zinc finger-containing protein 1PRO_0000047504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HBE1.
PaxDbiQ9HBE1.
PRIDEiQ9HBE1.

PTM databases

PhosphoSiteiQ9HBE1.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9HBE1.
CleanExiHS_PATZ1.
ExpressionAtlasiQ9HBE1. baseline and differential.
GenevestigatoriQ9HBE1.

Organism-specific databases

HPAiHPA047893.

Interactioni

Protein-protein interaction databases

BioGridi117133. 11 interactions.
STRINGi9606.ENSP00000266269.

Structurei

Secondary structure

1
687
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni295 – 2973Combined sources
Helixi304 – 31411Combined sources
Turni315 – 3173Combined sources
Beta strandi354 – 3574Combined sources
Turni358 – 3614Combined sources
Beta strandi362 – 3665Combined sources
Helixi367 – 3737Combined sources
Helixi374 – 3763Combined sources
Beta strandi382 – 3854Combined sources
Turni386 – 3894Combined sources
Beta strandi391 – 3933Combined sources
Helixi395 – 40511Combined sources
Beta strandi411 – 4133Combined sources
Beta strandi416 – 4183Combined sources
Beta strandi421 – 4244Combined sources
Helixi425 – 43410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EPPNMR-A286-338[»]
2EPQNMR-A380-411[»]
2EPRNMR-A350-384[»]
2EPSNMR-A408-445[»]
2YT9NMR-A355-436[»]
ProteinModelPortaliQ9HBE1.
SMRiQ9HBE1. Positions 10-152, 281-637.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HBE1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 13090BTBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the krueppel C2H2-type zinc-finger protein family.Curated
Contains 1 A.T hook DNA-binding domain.Curated
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri292 – 31423C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri355 – 37723C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri383 – 40523C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri413 – 43624C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri442 – 46423C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri495 – 51824C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri605 – 62824C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00530000063522.
HOGENOMiHOG000037943.
HOVERGENiHBG056645.
InParanoidiQ9HBE1.
OMAiRSVIDIC.
OrthoDBiEOG79SDWK.
PhylomeDBiQ9HBE1.
TreeFamiTF331686.

Family and domain databases

Gene3Di3.30.160.60. 6 hits.
InterProiIPR017956. 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]
PfamiPF00651. BTB. 1 hit.
PF00096. zf-C2H2. 2 hits.
[Graphical view]
SMARTiSM00384. AT_hook. 2 hits.
SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 2 hits.
PROSITEiPS50097. BTB. 1 hit.
PS00354. HMGI_Y. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9HBE1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MERVNDASCG PSGCYTYQVS RHSTEMLHNL NQQRKNGGRF CDVLLRVGDE 
        60         70         80         90        100
SFPAHRAVLA ACSEYFESVF SAQLGDGGAA DGGPADVGGA TAAPGGGAGG 
       110        120        130        140        150
SRELEMHTIS SKVFGDILDF AYTSRIVVRL ESFPELMTAA KFLLMRSVIE 
       160        170        180        190        200
ICQEVIKQSN VQILVPPARA DIMLFRPPGT SDLGFPLDMT NGAALAANSN 
       210        220        230        240        250
GIAGSMQPEE EAARAAGAAI AGQASLPVLP GVDRLPMVAG PLSPQLLTSP 
       260        270        280        290        300
FPSVASSAPP LTGKRGRGRP RKANLLDSMF GSPGGLREAG ILPCGLCGKV 
       310        320        330        340        350
FTDANRLRQH EAQHGVTSLQ LGYIDLPPPR LGENGLPISE DPDGPRKRSR 
       360        370        380        390        400
TRKQVACEIC GKIFRDVYHL NRHKLSHSGE KPYSCPVCGL RFKRKDRMSY 
       410        420        430        440        450
HVRSHDGSVG KPYICQSCGK GFSRPDHLNG HIKQVHTSER PHKCQTCNAS 
       460        470        480        490        500
FATRDRLRSH LACHEDKVPC QVCGKYLRAA YMADHLKKHS EGPSNFCSIC 
       510        520        530        540        550
NRGFSSASYL KVHVKTHHGV PLPQVSRHQE PILNGGAAFH CARTYGNKEG 
       560        570        580        590        600
QKCSHQDPIE SSDSYGDLSD ASDLKTPEKQ SANGSFSCDM AVPKNKMESD 
       610        620        630        640        650
GEKKYPCPEC GSFFRSKSYL NKHIQKVHVR ALGGPLGDLG PALGSPFSPQ 
       660        670        680 
QNMSLLESFG FQIVQSAFAS SLVDPEVDQQ PMGPEGK
Length:687
Mass (Da):74,060
Last modified:March 1, 2001 - v1
Checksum:i0F1C59A78C6D110A
GO
Isoform 2 (identifier: Q9HBE1-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     504-537: FSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGA → LQAPGAHPEWGSSVPLRQDLWQQRRPEMLTSGSD
     538-687: Missing.

Show »
Length:537
Mass (Da):57,995
Checksum:i950792413BF1F5DB
GO
Isoform 3 (identifier: Q9HBE1-3) [UniParc]FASTAAdd to Basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     503-548: Missing.

Show »
Length:641
Mass (Da):69,079
Checksum:i29515535E380F0CE
GO
Isoform 4 (identifier: Q9HBE1-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:537
Mass (Da):57,601
Checksum:iBA4A909E24800F13
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631S → N in AAF32518. (PubMed:10713105)Curated
Sequence conflicti259 – 2591P → L in AAF32518. (PubMed:10713105)Curated
Sequence conflicti394 – 3941R → K in AAF32518. (PubMed:10713105)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti685 – 6851E → D.
Corresponds to variant rs2240424 [ dbSNP | Ensembl ].		VAR_052724

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei446 – 53792TCNAS…LNGGA → VWVGSSSGLPPLEPLPSDLP SWDFAQPALWRSSHSVPDTA FSLSLKKSFPALENLGPAHS SNTLFCPAPPGYLRQGWTTP EGSRAFTQWPVG in isoform 4. 3 PublicationsVSP_008802Add
BLAST
Alternative sequencei503 – 54846Missing in isoform 3. 3 PublicationsVSP_008801Add
BLAST
Alternative sequencei504 – 53734FSSAS…LNGGA → LQAPGAHPEWGSSVPLRQDL WQQRRPEMLTSGSD in isoform 2. 1 PublicationVSP_008799Add
BLAST
Alternative sequencei538 – 687150Missing in isoform 2 and isoform 4. 3 PublicationsVSP_008800Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13894.1. [Q9HBE1-1]
CCDS13895.1. [Q9HBE1-3]
CCDS13896.1. [Q9HBE1-4]
CCDS46691.1. [Q9HBE1-2]
RefSeqiNP_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]
UniGeneiHs.731398.

Genome annotation databases

EnsembliENST00000215919; ENSP00000215919; ENSG00000100105. [Q9HBE1-4]
ENST00000266269; ENSP00000266269; ENSG00000100105. [Q9HBE1-1]
ENST00000351933; ENSP00000337520; ENSG00000100105. [Q9HBE1-3]
ENST00000405309; ENSP00000384173; ENSG00000100105. [Q9HBE1-2]
GeneIDi23598.
KEGGihsa:23598.
UCSCiuc003akp.3. human. [Q9HBE1-2]
uc003akq.3. human. [Q9HBE1-1]
uc003akr.3. human. [Q9HBE1-3]
uc003aks.3. human. [Q9HBE1-4]

Polymorphism databases

DMDMi38258840.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 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 .
CCDSi CCDS13894.1. [Q9HBE1-1 ]
CCDS13895.1. [Q9HBE1-3 ]
CCDS13896.1. [Q9HBE1-4 ]
CCDS46691.1. [Q9HBE1-2 ]
RefSeqi 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 ]
UniGenei Hs.731398.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9HBE1.
SMRi Q9HBE1. Positions 10-152, 281-637.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117133. 11 interactions.
STRINGi 9606.ENSP00000266269.

PTM databases

PhosphoSitei Q9HBE1.

Polymorphism databases

DMDMi 38258840.

Proteomic databases

MaxQBi Q9HBE1.
PaxDbi Q9HBE1.
PRIDEi Q9HBE1.

Protocols and materials databases

DNASUi 23598.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215919 ; ENSP00000215919 ; ENSG00000100105 . [Q9HBE1-4 ]
ENST00000266269 ; ENSP00000266269 ; ENSG00000100105 . [Q9HBE1-1 ]
ENST00000351933 ; ENSP00000337520 ; ENSG00000100105 . [Q9HBE1-3 ]
ENST00000405309 ; ENSP00000384173 ; ENSG00000100105 . [Q9HBE1-2 ]
GeneIDi 23598.
KEGGi hsa:23598.
UCSCi uc003akp.3. human. [Q9HBE1-2 ]
uc003akq.3. human. [Q9HBE1-1 ]
uc003akr.3. human. [Q9HBE1-3 ]
uc003aks.3. human. [Q9HBE1-4 ]

Organism-specific databases

CTDi 23598.
GeneCardsi GC22M031721.
HGNCi HGNC:13071. PATZ1.
HPAi HPA047893.
MIMi 605165. gene.
neXtProti NX_Q9HBE1.
PharmGKBi PA162398806.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00530000063522.
HOGENOMi HOG000037943.
HOVERGENi HBG056645.
InParanoidi Q9HBE1.
OMAi RSVIDIC.
OrthoDBi EOG79SDWK.
PhylomeDBi Q9HBE1.
TreeFami TF331686.

Miscellaneous databases

ChiTaRSi PATZ1. human.
EvolutionaryTracei Q9HBE1.
GeneWikii PATZ1.
GenomeRNAii 23598.
NextBioi 46268.
PROi Q9HBE1.
SOURCEi Search...

Gene expression databases

Bgeei Q9HBE1.
CleanExi HS_PATZ1.
ExpressionAtlasi Q9HBE1. baseline and differential.
Genevestigatori Q9HBE1.

Family and domain databases

Gene3Di 3.30.160.60. 6 hits.
InterProi 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 ]
Pfami PF00651. BTB. 1 hit.
PF00096. zf-C2H2. 2 hits.
[Graphical view ]
SMARTi SM00384. AT_hook. 2 hits.
SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 8 hits.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiPATZ1_HUMAN
AccessioniPrimary (citable) accession number: Q9HBE1
Secondary accession number(s): Q9HBE2
, Q9HBE3, Q9P1A9, Q9UDU0, Q9Y529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 133 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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