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Q9UHF7

- TRPS1_HUMAN

UniProt

Q9UHF7 - TRPS1_HUMAN

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Protein

Zinc finger transcription factor Trps1

Gene

TRPS1

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

Functioni

Transcriptional repressor. Binds specifically to GATA sequences and represses expression of GATA-regulated genes at selected sites and stages in vertebrate development. Regulates chondrocyte proliferation and differentiation. Executes multiple functions in proliferating chondrocytes, expanding the region of distal chondrocytes, activating proliferation in columnar cells and supporting the differentiation of columnar into hypertrophic chondrocytes.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri222 – 24726C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri333 – 35826C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri614 – 63724C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri666 – 68924C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri692 – 71524C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri896 – 92025GATA-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1215 – 123723C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1243 – 126725C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc
  3. zinc ion binding Source: ProtInc

GO - Biological processi

  1. chondrocyte differentiation Source: Ensembl
  2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. NLS-bearing protein import into nucleus Source: ProtInc
  4. positive regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
  5. regulation of chondrocyte differentiation Source: UniProtKB
  6. regulation of histone deacetylation Source: InterPro
  7. skeletal system development Source: ProtInc
  8. transcription from RNA polymerase II promoter Source: ProtInc
  9. transmembrane receptor protein serine/threonine kinase signaling pathway Source: Ensembl
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:
Zinc finger transcription factor Trps1
Alternative name(s):
Tricho-rhino-phalangeal syndrome type I protein
Zinc finger protein GC79
Gene namesi
Name:TRPS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:12340. TRPS1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Tricho-rhino-phalangeal syndrome 1 (TRPS1) [MIM:190350]: Autosomal dominant disorder characterized by craniofacial and skeletal abnormalities. It is allelic with tricho-rhino-phalangeal type 3. Typical features include sparse scalp hair, a bulbous tip of the nose, protruding ears, a long flat philtrum and a thin upper vermilion border. Skeletal defects include cone-shaped epiphyses at the phalanges, hip malformations and short stature.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti894 – 8941V → D in TRPS3; in heterozygous status has a milder effect causing TRPS1. 1 Publication
VAR_012807
Natural varianti952 – 9521R → C in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency. 1 Publication
VAR_038198
Natural varianti952 – 9521R → H in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency. 1 Publication
VAR_038199
Tricho-rhino-phalangeal syndrome 2 (TRPS2) [MIM:150230]: A syndrome that combines the clinical features of tricho-rhino-phalangeal syndrome type 1 and multiple exostoses type 1. Affected individuals manifest multiple dysmorphic facial features including large, laterally protruding ears, a bulbous nose, an elongated upper lip, as well as sparse scalp hair, winged scapulae, multiple cartilaginous exostoses, redundant skin, and mental retardation.
Note: The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration resulting in the loss of functional copies of TRPS1 and EXT1 has been found in TRPS2 patients.
Tricho-rhino-phalangeal syndrome 3 (TRPS3) [MIM:190351]: Autosomal dominant disorder characterized by craniofacial and skeletal abnormalities. It is allelic with tricho-rhino-phalangeal type 1. In TRPS3 a more severe brachydactyly and growth retardation are observed.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti894 – 8941V → D in TRPS3; in heterozygous status has a milder effect causing TRPS1. 1 Publication
VAR_012807
Natural varianti901 – 9011T → P in TRPS3; severe. 1 Publication
VAR_012808
Natural varianti908 – 9081R → P in TRPS3; severe. 1 Publication
VAR_012809
Natural varianti908 – 9081R → Q in TRPS3. 2 Publications
VAR_012810
Natural varianti919 – 9191A → T in TRPS3. 1 Publication
VAR_012811

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1192 – 11921K → R: Very little change in sumoylation and 30% reduction in repression activity. Almost complete loss of sumoylation and 70% reduction in repression activity; when associated with R-1201. 1 Publication
Mutagenesisi1201 – 12011K → R: Great loss of sumoylation and 30% reduction in repression activity. Almost complete loss of sumoylation and 70% reduction in repression activity; when associated with R-1192. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi150230. phenotype.
190350. phenotype.
190351. phenotype.
Orphaneti502. Langer-Giedion syndrome.
77258. Trichorhinophalangeal syndrome type 1 and 3.
PharmGKBiPA37013.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12811281Zinc finger transcription factor Trps1PRO_0000083508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei751 – 7511Phosphothreonine1 Publication
Modified residuei1041 – 10411Phosphoserine1 Publication
Modified residuei1085 – 10851Phosphoserine2 Publications
Cross-linki1192 – 1192Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki1201 – 1201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylated. Sumoylation in the repressor domain inhibits the transcription repression activity. Sumoylation on Lys-1201 is the major site. Appears to be sumoylated on multiple sites.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UHF7.
PaxDbiQ9UHF7.
PRIDEiQ9UHF7.

PTM databases

PhosphoSiteiQ9UHF7.

Expressioni

Tissue specificityi

Ubiquitously expressed in the adult. Found in fetal brain, lung, kidney, liver, spleen and thymus. More highly expressed in androgen-dependent than in androgen-independent prostate cancer cells.

Gene expression databases

BgeeiQ9UHF7.
CleanExiHS_TRPS1.
ExpressionAtlasiQ9UHF7. baseline and differential.
GenevestigatoriQ9UHF7.

Interactioni

Subunit structurei

Interacts with RNF4; regulates TRPS1 repressor activity. Interacts specifically with the activator form of GLI3 (GLI3A) but not with the repressor form (GLI3R).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ORFQ9Q2G43EBI-2556151,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi113078. 9 interactions.
IntActiQ9UHF7. 5 interactions.
MINTiMINT-271027.
STRINGi9606.ENSP00000379065.

Structurei

3D structure databases

ProteinModelPortaliQ9UHF7.
SMRiQ9UHF7. Positions 427-465, 612-642, 687-712, 893-938.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni635 – 819185Mediates interaction with GLI3Add
BLAST
Regioni985 – 1184200Mediates interaction with RNF4By similarityAdd
BLAST
Regioni1163 – 1281119Transcriptional repressor domainBy similarityAdd
BLAST

Sequence similaritiesi

Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri222 – 24726C2H2-type 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri333 – 35826C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri614 – 63724C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri666 – 68924C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri692 – 71524C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri896 – 92025GATA-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1215 – 123723C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1243 – 126725C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5641.
GeneTreeiENSGT00550000074392.
HOGENOMiHOG000146438.
HOVERGENiHBG067120.
InParanoidiQ9UHF7.
OMAiHYESVHE.
OrthoDBiEOG72ZCD8.
PhylomeDBiQ9UHF7.
TreeFamiTF350812.

Family and domain databases

Gene3Di3.30.50.10. 1 hit.
InterProiIPR028440. Trps1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF6. PTHR10071:SF6. 1 hit.
PfamiPF00320. GATA. 1 hit.
[Graphical view]
PRINTSiPR00619. GATAZNFINGER.
SMARTiSM00355. ZnF_C2H2. 9 hits.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
PROSITEiPS00344. GATA_ZN_FINGER_1. 1 hit.
PS50114. GATA_ZN_FINGER_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UHF7-1) [UniParc]FASTAAdd to Basket

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
MVRKKNPPLR NVASEGEGQI LEPIGTESKV SGKNKEFSAD QMSENTDQSD
60 70 80 90 100
AAELNHKEEH SLHVQDPSSS SKKDLKSAVL SEKAGFNYES PSKGGNFPSF
110 120 130 140 150
PHDEVTDRNM LAFSSPAAGG VCEPLKSPQR AEADDPQDMA CTPSGDSLET
160 170 180 190 200
KEDQKMSPKA TEETGQAQSG QANCQGLSPV SVASKNPQVP SDGGVRLNKS
210 220 230 240 250
KTDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI KHFRKYHLGL
260 270 280 290 300
HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVFSGV LQDINSSRPV
310 320 330 340 350
LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL
360 370 380 390 400
EQHFLQTHPN KIKASLPSSE VAKPSEKNSN KSIPALQSSD SGDLGKWQDK
410 420 430 440 450
ITVKAGDDTP VGYSVPIKPL DSSRQNGTEA TSYYWCKFCS FSCESSSSLK
460 470 480 490 500
LLEHYGKQHG AVQSGGLNPE LNDKLSRGSV INQNDLAKSS EGETMTKTDK
510 520 530 540 550
SSSGAKKKDF SSKGAEDNMV TSYNCQFCDF RYSKSHGPDV IVVGPLLRHY
560 570 580 590 600
QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL
610 620 630 640 650
HLSPGAAGSS RVKHQCHQCS FTTPDVDVLL FHYESVHESQ ASDVKQEANH
660 670 680 690 700
LQGSDGQQSV KESKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT
710 720 730 740 750
AADTQSLLEH FNTVHCQEQD ITTANGEEDG HAISTIKEEP KIDFRVYNLL
760 770 780 790 800
TPDSKMGEPV SESVVKREKL EEKDGLKEKV WTESSSDDLR NVTWRGADIL
810 820 830 840 850
RGSPSYTQAS LGLLTPVSGT QEQTKTLRDS PNVEAAHLAR PIYGLAVETK
860 870 880 890 900
GFLQGAPAGG EKSGALPQQY PASGENKSKD ESQSLLRRRR GSGVFCANCL
910 920 930 940 950
TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR
960 970 980 990 1000
KRLNPEALQA EQLNKQQRGS NEEQVNGSPL ERRSEDHLTE SHQREIPLPS
1010 1020 1030 1040 1050
LSKYEAQGSL TKSHSAQQPV LVSQTLDIHK RMQPLHIQIK SPQESTGDPG
1060 1070 1080 1090 1100
NSSSVSEGKG SSERGSPIEK YMRPAKHPNY SPPGSPIEKY QYPLFGLPFV
1110 1120 1130 1140 1150
HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN YVPYPTFNLP
1160 1170 1180 1190 1200
PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPN VKNEGPLNVV
1210 1220 1230 1240 1250
KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH
1260 1270 1280
LCTDKYDFTT HIQRGLHRNN AQVEKNGKPK E
Length:1,281
Mass (Da):141,521
Last modified:March 27, 2002 - v2
Checksum:i2157B04F5BEB71CC
GO
Isoform 2 (identifier: Q9UHF7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPYEVNAGYDFTNM

Show »
Length:1,294
Mass (Da):143,023
Checksum:i0801087C5B0E5196
GO
Isoform 3 (identifier: Q9UHF7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQSNM

Show »
Length:1,285
Mass (Da):141,981
Checksum:iACA951C56206BA8F
GO

Sequence cautioni

The sequence AAI25021.1 differs from that shown. Reason: Erroneous termination at position 854. Translated as Gln.Curated
The sequence BAA91441.1 differs from that shown. Reason: Frameshift at position 1276. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151S → F in AAF23614. (PubMed:10615131)Curated
Sequence conflicti582 – 5821T → A in BAG64957. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti654 – 6541S → L.
Corresponds to variant rs7002384 [ dbSNP | Ensembl ].
VAR_038197
Natural varianti894 – 8941V → D in TRPS3; in heterozygous status has a milder effect causing TRPS1. 1 Publication
VAR_012807
Natural varianti901 – 9011T → P in TRPS3; severe. 1 Publication
VAR_012808
Natural varianti908 – 9081R → P in TRPS3; severe. 1 Publication
VAR_012809
Natural varianti908 – 9081R → Q in TRPS3. 2 Publications
VAR_012810
Natural varianti919 – 9191A → T in TRPS3. 1 Publication
VAR_012811
Natural varianti952 – 9521R → C in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency. 1 Publication
VAR_038198
Natural varianti952 – 9521R → H in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency. 1 Publication
VAR_038199

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPYEVNAGYDFTNM in isoform 2. 1 PublicationVSP_037549
Alternative sequencei1 – 11M → MQSNM in isoform 3. 1 PublicationVSP_037550

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF183810 mRNA. Translation: AAF23614.1.
AF264784 mRNA. Translation: AAG21134.1.
AK000948 mRNA. Translation: BAA91441.1. Frameshift.
AK304046 mRNA. Translation: BAG64957.1.
AF178030 Genomic DNA. No translation available.
BC125020 mRNA. Translation: AAI25021.1. Sequence problems.
CCDSiCCDS6318.2. [Q9UHF7-2]
CCDS64957.1. [Q9UHF7-3]
RefSeqiNP_001269831.1. NM_001282902.2. [Q9UHF7-3]
NP_001269832.1. NM_001282903.2.
NP_054831.2. NM_014112.4. [Q9UHF7-2]
XP_005251106.1. XM_005251049.2. [Q9UHF7-1]
XP_006716687.1. XM_006716624.1. [Q9UHF7-2]
XP_006716688.1. XM_006716625.1. [Q9UHF7-2]
UniGeneiHs.657018.

Genome annotation databases

EnsembliENST00000220888; ENSP00000220888; ENSG00000104447. [Q9UHF7-1]
ENST00000395715; ENSP00000379065; ENSG00000104447. [Q9UHF7-2]
ENST00000520276; ENSP00000428680; ENSG00000104447. [Q9UHF7-3]
GeneIDi7227.
KEGGihsa:7227.
UCSCiuc003yny.3. human. [Q9UHF7-2]
uc003ynz.3. human. [Q9UHF7-1]
uc011lhy.2. human. [Q9UHF7-3]

Polymorphism databases

DMDMi20140909.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF183810 mRNA. Translation: AAF23614.1 .
AF264784 mRNA. Translation: AAG21134.1 .
AK000948 mRNA. Translation: BAA91441.1 . Frameshift.
AK304046 mRNA. Translation: BAG64957.1 .
AF178030 Genomic DNA. No translation available.
BC125020 mRNA. Translation: AAI25021.1 . Sequence problems.
CCDSi CCDS6318.2. [Q9UHF7-2 ]
CCDS64957.1. [Q9UHF7-3 ]
RefSeqi NP_001269831.1. NM_001282902.2. [Q9UHF7-3 ]
NP_001269832.1. NM_001282903.2.
NP_054831.2. NM_014112.4. [Q9UHF7-2 ]
XP_005251106.1. XM_005251049.2. [Q9UHF7-1 ]
XP_006716687.1. XM_006716624.1. [Q9UHF7-2 ]
XP_006716688.1. XM_006716625.1. [Q9UHF7-2 ]
UniGenei Hs.657018.

3D structure databases

ProteinModelPortali Q9UHF7.
SMRi Q9UHF7. Positions 427-465, 612-642, 687-712, 893-938.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113078. 9 interactions.
IntActi Q9UHF7. 5 interactions.
MINTi MINT-271027.
STRINGi 9606.ENSP00000379065.

PTM databases

PhosphoSitei Q9UHF7.

Polymorphism databases

DMDMi 20140909.

Proteomic databases

MaxQBi Q9UHF7.
PaxDbi Q9UHF7.
PRIDEi Q9UHF7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220888 ; ENSP00000220888 ; ENSG00000104447 . [Q9UHF7-1 ]
ENST00000395715 ; ENSP00000379065 ; ENSG00000104447 . [Q9UHF7-2 ]
ENST00000520276 ; ENSP00000428680 ; ENSG00000104447 . [Q9UHF7-3 ]
GeneIDi 7227.
KEGGi hsa:7227.
UCSCi uc003yny.3. human. [Q9UHF7-2 ]
uc003ynz.3. human. [Q9UHF7-1 ]
uc011lhy.2. human. [Q9UHF7-3 ]

Organism-specific databases

CTDi 7227.
GeneCardsi GC08M116489.
HGNCi HGNC:12340. TRPS1.
MIMi 150230. phenotype.
190350. phenotype.
190351. phenotype.
604386. gene.
neXtProti NX_Q9UHF7.
Orphaneti 502. Langer-Giedion syndrome.
77258. Trichorhinophalangeal syndrome type 1 and 3.
PharmGKBi PA37013.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5641.
GeneTreei ENSGT00550000074392.
HOGENOMi HOG000146438.
HOVERGENi HBG067120.
InParanoidi Q9UHF7.
OMAi HYESVHE.
OrthoDBi EOG72ZCD8.
PhylomeDBi Q9UHF7.
TreeFami TF350812.

Miscellaneous databases

ChiTaRSi TRPS1. human.
GeneWikii Tricho-rhino-phalangeal_syndrome_Type_1.
GenomeRNAii 7227.
NextBioi 28303.
PROi Q9UHF7.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHF7.
CleanExi HS_TRPS1.
ExpressionAtlasi Q9UHF7. baseline and differential.
Genevestigatori Q9UHF7.

Family and domain databases

Gene3Di 3.30.50.10. 1 hit.
InterProi IPR028440. Trps1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
PANTHERi PTHR10071:SF6. PTHR10071:SF6. 1 hit.
Pfami PF00320. GATA. 1 hit.
[Graphical view ]
PRINTSi PR00619. GATAZNFINGER.
SMARTi SM00355. ZnF_C2H2. 9 hits.
SM00401. ZnF_GATA. 1 hit.
[Graphical view ]
PROSITEi PS00344. GATA_ZN_FINGER_1. 1 hit.
PS50114. GATA_ZN_FINGER_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in a new gene, encoding a zinc-finger protein, cause tricho-rhino-phalangeal syndrome type I."
    Momeni P., Gloeckner G., Schmidt O., von Holtum D., Albrecht B., Gillessen-Kaesbach G., Hennekam R.C.M., Meinecke P., Zabel B., Rosenthal A., Horsthemke B., Luedecke H.-J.
    Nat. Genet. 24:71-74(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Characterization of a zinc-finger protein and its association with apoptosis in prostate cancer cells."
    Chang G.T.G., Steenbeek M., Schippers E., Blok L.J., van Weerden W.M., van Alewijk D.C.J.G., Eussen B.H.J., van Steenbrugge G.J., Brinkmann A.O.
    J. Natl. Cancer Inst. 92:1414-1421(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Prostate.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1281 (ISOFORM 1).
    Tissue: Embryo and Trachea.
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
  6. "The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor."
    Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.
    J. Biol. Chem. 278:38780-38785(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RNF4, SUBCELLULAR LOCATION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1085, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "SUMOylation modulates transcriptional repression by TRPS1."
    Kaiser F.J., Ludecke H.J., Weger S.
    Biol. Chem. 388:381-390(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-1192 AND LYS-1201, FUNCTION, MUTAGENESIS OF LYS-1192 AND LYS-1201.
  9. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Trps1, a regulator of chondrocyte proliferation and differentiation, interacts with the activator form of Gli3."
    Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A., Depping R., Vortkamp A.
    Dev. Biol. 328:40-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLI3.
  11. "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 THR-751; SER-1041 AND SER-1085, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS TRPS3 ASP-894; PRO-901; GLN-908; PRO-908 AND THR-919.
  14. "Missense mutation of TRPS1 in a family of tricho-rhino-phalangeal syndrome type III."
    Kobayashi H., Hino M., Shimodahira M., Iwakura T., Ishihara T., Ikekubo K., Ogawa Y., Nakao K., Kurahachi H.
    Am. J. Med. Genet. 107:26-29(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TRPS3 GLN-908.
  15. "Novel missense mutations in the TRPS1 transcription factor define the nuclear localization signal."
    Kaiser F.J., Brega P., Raff M.L., Byers P.H., Gallati S., Kay T.T., de Almeida S., Horsthemke B., Luedecke H.-J.
    Eur. J. Hum. Genet. 12:121-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS TRPS1 CYS-952 AND HIS-952, CHARACTERIZATION OF VARIANTS TRPS1 CYS-952 AND HIS-952.

Entry informationi

Entry nameiTRPS1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHF7
Secondary accession number(s): B4E1Z5
, Q08AU2, Q9NWE1, Q9UHH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: November 26, 2014
This is version 131 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3