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Q9UHF7

- TRPS1_HUMAN

UniProt

Q9UHF7 - TRPS1_HUMAN

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (27 Mar 2002)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc
    4. 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

    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

    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

    ArrayExpressiQ9UHF7.
    BgeeiQ9UHF7.
    CleanExiHS_TRPS1.
    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. 8 interactions.
    IntActiQ9UHF7. 5 interactions.
    MINTiMINT-271027.
    STRINGi9606.ENSP00000379065.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UHF7.
    SMRiQ9UHF7. Positions 424-467, 608-646, 686-719, 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.
    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

    MVRKKNPPLR NVASEGEGQI LEPIGTESKV SGKNKEFSAD QMSENTDQSD     50
    AAELNHKEEH SLHVQDPSSS SKKDLKSAVL SEKAGFNYES PSKGGNFPSF 100
    PHDEVTDRNM LAFSSPAAGG VCEPLKSPQR AEADDPQDMA CTPSGDSLET 150
    KEDQKMSPKA TEETGQAQSG QANCQGLSPV SVASKNPQVP SDGGVRLNKS 200
    KTDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI KHFRKYHLGL 250
    HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVFSGV LQDINSSRPV 300
    LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL 350
    EQHFLQTHPN KIKASLPSSE VAKPSEKNSN KSIPALQSSD SGDLGKWQDK 400
    ITVKAGDDTP VGYSVPIKPL DSSRQNGTEA TSYYWCKFCS FSCESSSSLK 450
    LLEHYGKQHG AVQSGGLNPE LNDKLSRGSV INQNDLAKSS EGETMTKTDK 500
    SSSGAKKKDF SSKGAEDNMV TSYNCQFCDF RYSKSHGPDV IVVGPLLRHY 550
    QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL 600
    HLSPGAAGSS RVKHQCHQCS FTTPDVDVLL FHYESVHESQ ASDVKQEANH 650
    LQGSDGQQSV KESKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT 700
    AADTQSLLEH FNTVHCQEQD ITTANGEEDG HAISTIKEEP KIDFRVYNLL 750
    TPDSKMGEPV SESVVKREKL EEKDGLKEKV WTESSSDDLR NVTWRGADIL 800
    RGSPSYTQAS LGLLTPVSGT QEQTKTLRDS PNVEAAHLAR PIYGLAVETK 850
    GFLQGAPAGG EKSGALPQQY PASGENKSKD ESQSLLRRRR GSGVFCANCL 900
    TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR 950
    KRLNPEALQA EQLNKQQRGS NEEQVNGSPL ERRSEDHLTE SHQREIPLPS 1000
    LSKYEAQGSL TKSHSAQQPV LVSQTLDIHK RMQPLHIQIK SPQESTGDPG 1050
    NSSSVSEGKG SSERGSPIEK YMRPAKHPNY SPPGSPIEKY QYPLFGLPFV 1100
    HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN YVPYPTFNLP 1150
    PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPN VKNEGPLNVV 1200
    KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH 1250
    LCTDKYDFTT HIQRGLHRNN AQVEKNGKPK E 1281
    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 BAA91441.1 differs from that shown. Reason: Frameshift at position 1276.
    The sequence AAI25021.1 differs from that shown. Reason: Erroneous termination at position 854. Translated as Gln.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 424-467, 608-646, 686-719, 893-938.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113078. 8 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.
    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

    ArrayExpressi Q9UHF7.
    Bgeei Q9UHF7.
    CleanExi HS_TRPS1.
    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

    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: October 1, 2014
    This is version 129 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