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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; atypical
Add
BLAST
Zinc fingeri333 – 35826C2H2-type 2; atypical
Add
BLAST
Zinc fingeri614 – 63724C2H2-type 3; atypical
Add
BLAST
Zinc fingeri666 – 68924C2H2-type 4
Add
BLAST
Zinc fingeri692 – 71524C2H2-type 5
Add
BLAST
Zinc fingeri896 – 92025GATA-type
Add
BLAST
Zinc fingeri1215 – 123723C2H2-type 6
Add
BLAST
Zinc fingeri1243 – 126725C2H2-type 7
Add
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
Complete GO annotation...

GO - Biological processi

  1. NLS-bearing protein import into nucleus Source: ProtInc
  2. chondrocyte differentiation Source: Ensembl
  3. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 Trps1
PRO_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)1 Publication
Cross-linki1201 – 1201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni635 – 819185Mediates interaction with GLI3
Add
BLAST
Regioni985 – 1184200Mediates interaction with RNF4 By similarity
Add
BLAST
Regioni1163 – 1281119Transcriptional repressor domain By similarity
Add
BLAST

Sequence similaritiesi

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.

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.
VSP_037549
Alternative sequencei1 – 11M → MQSNM in isoform 3.
VSP_037550

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151S → F in AAF23614. 1 Publication
Sequence conflicti582 – 5821T → A in BAG64957. 1 Publication

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...

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

« 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: July 9, 2014
This is version 128 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

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