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Q9UHF7 (TRPS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger transcription factor Trps1
Alternative name(s):
Tricho-rhino-phalangeal syndrome type I protein
Zinc finger protein GC79
Gene names
Name:TRPS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8

Subunit structure

Interacts with RNF4; regulates TRPS1 repressor activity. Interacts specifically with the activator form of GLI3 (GLI3A) but not with the repressor form (GLI3R). Ref.6 Ref.10

Subcellular location

Nucleus Ref.6.

Tissue specificity

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.

Post-translational modification

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. Ref.8

Involvement in disease

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. Ref.15

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. Ref.13 Ref.14

Sequence similarities

Contains 7 C2H2-type zinc fingers.

Contains 1 GATA-type zinc finger.

Sequence caution

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

The sequence BAA91441.1 differs from that shown. Reason: Frameshift at position 1276.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Traceable author statement Ref.1. Source: ProtInc

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

regulation of chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of histone deacetylation

Inferred from electronic annotation. Source: InterPro

skeletal system development

Traceable author statement Ref.1. Source: ProtInc

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

transmembrane receptor protein serine/threonine kinase signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.6Ref.10. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G43EBI-2556151,EBI-6248094From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UHF7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UHF7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPYEVNAGYDFTNM
Isoform 3 (identifier: Q9UHF7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12811281Zinc finger transcription factor Trps1
PRO_0000083508

Regions

Zinc finger222 – 24726C2H2-type 1; atypical
Zinc finger333 – 35826C2H2-type 2; atypical
Zinc finger614 – 63724C2H2-type 3; atypical
Zinc finger666 – 68924C2H2-type 4
Zinc finger692 – 71524C2H2-type 5
Zinc finger896 – 92025GATA-type
Zinc finger1215 – 123723C2H2-type 6
Zinc finger1243 – 126725C2H2-type 7
Region635 – 819185Mediates interaction with GLI3
Region985 – 1184200Mediates interaction with RNF4 By similarity
Region1163 – 1281119Transcriptional repressor domain By similarity

Amino acid modifications

Modified residue7511Phosphothreonine Ref.11
Modified residue10411Phosphoserine Ref.11
Modified residue10851Phosphoserine Ref.7 Ref.11
Cross-link1192Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8
Cross-link1201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Natural variations

Alternative sequence11M → MPYEVNAGYDFTNM in isoform 2.
VSP_037549
Alternative sequence11M → MQSNM in isoform 3.
VSP_037550
Natural variant6541S → L.
Corresponds to variant rs7002384 [ dbSNP | Ensembl ].
VAR_038197
Natural variant8941V → D in TRPS3; in heterozygous status has a milder effect causing TRPS1. Ref.13
VAR_012807
Natural variant9011T → P in TRPS3; severe. Ref.13
VAR_012808
Natural variant9081R → P in TRPS3; severe. Ref.13
VAR_012809
Natural variant9081R → Q in TRPS3. Ref.13 Ref.14
VAR_012810
Natural variant9191A → T in TRPS3. Ref.13
VAR_012811
Natural variant9521R → C in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency. Ref.15
VAR_038198
Natural variant9521R → H in TRPS1; prevents the transport into the nucleus and thus reduces the nuclear TRPS1 concentration consistent with haploinsufficiency. Ref.15
VAR_038199

Experimental info

Mutagenesis11921K → 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. Ref.8
Mutagenesis12011K → 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. Ref.8
Sequence conflict1151S → F in AAF23614. Ref.1
Sequence conflict5821T → A in BAG64957. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 2157B04F5BEB71CC

FASTA1,281141,521
        10         20         30         40         50         60 
MVRKKNPPLR NVASEGEGQI LEPIGTESKV SGKNKEFSAD QMSENTDQSD AAELNHKEEH 

        70         80         90        100        110        120 
SLHVQDPSSS SKKDLKSAVL SEKAGFNYES PSKGGNFPSF PHDEVTDRNM LAFSSPAAGG 

       130        140        150        160        170        180 
VCEPLKSPQR AEADDPQDMA CTPSGDSLET KEDQKMSPKA TEETGQAQSG QANCQGLSPV 

       190        200        210        220        230        240 
SVASKNPQVP SDGGVRLNKS KTDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI 

       250        260        270        280        290        300 
KHFRKYHLGL HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVFSGV LQDINSSRPV 

       310        320        330        340        350        360 
LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL EQHFLQTHPN 

       370        380        390        400        410        420 
KIKASLPSSE VAKPSEKNSN KSIPALQSSD SGDLGKWQDK ITVKAGDDTP VGYSVPIKPL 

       430        440        450        460        470        480 
DSSRQNGTEA TSYYWCKFCS FSCESSSSLK LLEHYGKQHG AVQSGGLNPE LNDKLSRGSV 

       490        500        510        520        530        540 
INQNDLAKSS EGETMTKTDK SSSGAKKKDF SSKGAEDNMV TSYNCQFCDF RYSKSHGPDV 

       550        560        570        580        590        600 
IVVGPLLRHY QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL 

       610        620        630        640        650        660 
HLSPGAAGSS RVKHQCHQCS FTTPDVDVLL FHYESVHESQ ASDVKQEANH LQGSDGQQSV 

       670        680        690        700        710        720 
KESKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT AADTQSLLEH FNTVHCQEQD 

       730        740        750        760        770        780 
ITTANGEEDG HAISTIKEEP KIDFRVYNLL TPDSKMGEPV SESVVKREKL EEKDGLKEKV 

       790        800        810        820        830        840 
WTESSSDDLR NVTWRGADIL RGSPSYTQAS LGLLTPVSGT QEQTKTLRDS PNVEAAHLAR 

       850        860        870        880        890        900 
PIYGLAVETK GFLQGAPAGG EKSGALPQQY PASGENKSKD ESQSLLRRRR GSGVFCANCL 

       910        920        930        940        950        960 
TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR KRLNPEALQA 

       970        980        990       1000       1010       1020 
EQLNKQQRGS NEEQVNGSPL ERRSEDHLTE SHQREIPLPS LSKYEAQGSL TKSHSAQQPV 

      1030       1040       1050       1060       1070       1080 
LVSQTLDIHK RMQPLHIQIK SPQESTGDPG NSSSVSEGKG SSERGSPIEK YMRPAKHPNY 

      1090       1100       1110       1120       1130       1140 
SPPGSPIEKY QYPLFGLPFV HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN 

      1150       1160       1170       1180       1190       1200 
YVPYPTFNLP PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPN VKNEGPLNVV 

      1210       1220       1230       1240       1250       1260 
KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH LCTDKYDFTT 

      1270       1280 
HIQRGLHRNN AQVEKNGKPK E 

« Hide

Isoform 2 [UniParc].

Checksum: 0801087C5B0E5196
Show »

FASTA1,294143,023
Isoform 3 [UniParc].

Checksum: ACA951C56206BA8F
Show »

FASTA1,285141,981

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Genotypic and phenotypic spectrum in tricho-rhino-phalangeal syndrome types I and III."
Luedecke H.-J., Schaper J., Meinecke P., Momeni P., Gross S., von Holtum D., Hirche H., Abramowicz M.J., Albrecht B., Apacik C., Christen H.-J., Claussen U., Devriendt K., Fastnacht E., Forderer A., Friedrich U., Goodship T.H.J., Greiwe M. expand/collapse author list , Hamm H., Hennekam R.C.M., Hinkel G.K., Hoeltzenbein M., Kayserili H., Majewski F., Mathieu M., McLeod R., Midro A.T., Moog U., Nagai T., Niikawa N., Oerstavik K.H., Ploechl E., Seitz C., Schmidtke J., Tranebjaerg L., Tsukahara M., Wittwer B., Zabel B., Gillessen-Kaesbach G., Horsthemke B.
Am. J. Hum. Genet. 68:81-91(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6318.2. [Q9UHF7-2]
CCDS64957.1. [Q9UHF7-3]
RefSeqNP_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]
UniGeneHs.657018.

3D structure databases

ProteinModelPortalQ9UHF7.
SMRQ9UHF7. Positions 424-467, 608-646, 686-719, 893-938.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113078. 8 interactions.
IntActQ9UHF7. 5 interactions.
MINTMINT-271027.
STRING9606.ENSP00000379065.

PTM databases

PhosphoSiteQ9UHF7.

Polymorphism databases

DMDM20140909.

Proteomic databases

MaxQBQ9UHF7.
PaxDbQ9UHF7.
PRIDEQ9UHF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220888; ENSP00000220888; ENSG00000104447. [Q9UHF7-1]
ENST00000395715; ENSP00000379065; ENSG00000104447. [Q9UHF7-2]
ENST00000520276; ENSP00000428680; ENSG00000104447. [Q9UHF7-3]
GeneID7227.
KEGGhsa:7227.
UCSCuc003yny.3. human. [Q9UHF7-2]
uc003ynz.3. human. [Q9UHF7-1]
uc011lhy.2. human. [Q9UHF7-3]

Organism-specific databases

CTD7227.
GeneCardsGC08M116489.
HGNCHGNC:12340. TRPS1.
MIM150230. phenotype.
190350. phenotype.
190351. phenotype.
604386. gene.
neXtProtNX_Q9UHF7.
Orphanet502. Langer-Giedion syndrome.
77258. Trichorhinophalangeal syndrome type 1 and 3.
PharmGKBPA37013.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5641.
HOGENOMHOG000146438.
HOVERGENHBG067120.
InParanoidQ9UHF7.
OMAHYESVHE.
OrthoDBEOG72ZCD8.
PhylomeDBQ9UHF7.
TreeFamTF350812.

Gene expression databases

ArrayExpressQ9UHF7.
BgeeQ9UHF7.
CleanExHS_TRPS1.
GenevestigatorQ9UHF7.

Family and domain databases

Gene3D3.30.50.10. 1 hit.
InterProIPR028440. Trps1.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERPTHR10071:SF6. PTHR10071:SF6. 1 hit.
PfamPF00320. GATA. 1 hit.
[Graphical view]
PRINTSPR00619. GATAZNFINGER.
SMARTSM00355. ZnF_C2H2. 9 hits.
SM00401. ZnF_GATA. 1 hit.
[Graphical view]
PROSITEPS00344. 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]
ProtoNetSearch...

Other

ChiTaRSTRPS1. human.
GeneWikiTricho-rhino-phalangeal_syndrome_Type_1.
GenomeRNAi7227.
NextBio28303.
PROQ9UHF7.
SOURCESearch...

Entry information

Entry nameTRPS1_HUMAN
AccessionPrimary (citable) accession number: Q9UHF7
Secondary accession number(s): B4E1Z5 expand/collapse secondary AC list , Q08AU2, Q9NWE1, Q9UHH6
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM