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Protein

PIH1 domain-containing protein 1

Gene

PIH1D1

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

Functioni

Involved in the assembly of C/D box small nucleolar ribonucleoprotein (snoRNP) particles (PubMed:17636026). Recruits the SWI/SNF complex to the core promoter of rRNA genes and enhances pre-rRNA transcription (PubMed:22368283, PubMed:24036451). Mediates interaction of TELO2 with the R2TP complex which is necessary for the stability of MTOR and SMG1 (PubMed:20864032). Positively regulates the assembly and activity of the mTORC1 complex (PubMed:24036451).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interacts with TELO21 Publication
Sitei64 – 641Interacts with TELO21 Publication
Sitei113 – 1131Interacts with TELO2By similarity

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • phosphoprotein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • RNA polymerase I CORE element sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • box C/D snoRNP assembly Source: BHF-UCL
  • chromatin remodeling Source: UniProtKB
  • epithelial cell differentiation Source: UniProtKB
  • establishment of protein localization to chromatin Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: UniProtKB
  • negative regulation of histone H3-K9 dimethylation Source: UniProtKB
  • negative regulation of histone H3-K9 trimethylation Source: UniProtKB
  • negative regulation of histone H4-K16 acetylation Source: UniProtKB
  • positive regulation of glucose mediated signaling pathway Source: UniProtKB
  • positive regulation of histone H3-K9 acetylation Source: UniProtKB
  • positive regulation of histone H4 acetylation Source: UniProtKB
  • positive regulation of protein complex assembly Source: UniProtKB
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of TORC1 signaling Source: UniProtKB
  • positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProtKB
  • regulation of histone H3-K4 methylation Source: UniProtKB
  • snoRNA localization Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
PIH1 domain-containing protein 1
Alternative name(s):
Nucleolar protein 17 homolog
Gene namesi
Name:PIH1D1
Synonyms:NOP17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:26075. PIH1D1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • pre-snoRNP complex Source: BHF-UCL
  • R2TP complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541F → A: Abolishes binding to histone H4. 1 Publication
Mutagenesisi55 – 551C → A: No effect on binding to histone H4. 1 Publication
Mutagenesisi57 – 571K → A: Abolishes binding to TELO2. 1 Publication
Mutagenesisi64 – 641K → A: Abolishes binding to ECD, EFTUD2, RPB1, TELO2 and UBR5. 1 Publication
Mutagenesisi113 – 1131K → A: Reduces binding to TELO2. 1 Publication
Mutagenesisi163 – 1631R → A: Reduces binding to TELO2. 1 Publication
Mutagenesisi166 – 1661K → A: Reduces binding to TELO2. 1 Publication
Mutagenesisi168 – 1681R → A: Abolishes binding to TELO2. 1 Publication

Organism-specific databases

PharmGKBiPA162399535.

Polymorphism and mutation databases

BioMutaiPIH1D1.
DMDMi74719379.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290PIH1 domain-containing protein 1PRO_0000307328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei173 – 1731PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NWS0.
MaxQBiQ9NWS0.
PaxDbiQ9NWS0.
PeptideAtlasiQ9NWS0.
PRIDEiQ9NWS0.

PTM databases

iPTMnetiQ9NWS0.
PhosphoSiteiQ9NWS0.

Expressioni

Tissue specificityi

Expressed at low levels in normal mammary epithelial cells (at protein level) (PubMed:24036451). Highest expression in lung, leukocyte and placenta. Expressed at lower levels in brain, prostate, colon, heart, small intestine, liver, ovary, pancreas, skeletal muscle, spleen, testis and thymus (PubMed:21078300).2 Publications

Gene expression databases

BgeeiQ9NWS0.
CleanExiHS_PIH1D1.
ExpressionAtlasiQ9NWS0. baseline and differential.
GenevisibleiQ9NWS0. HS.

Organism-specific databases

HPAiHPA047258.

Interactioni

Subunit structurei

Component of the R2TP complex composed at least of PIHD1, RUVBL1, RUVBL2 and RPAP3 (PubMed:20864032). Interacts with phosphorylated TELO2 and mediates interaction of TELO2 with the R2TP complex (PubMed:20864032, PubMed:24656813). Interacts with phosphorylated ECD, EFTUD2/SNRP116, RPB1 and UBR5 and with RPB1 in a phosphorylation-independent manner (PubMed:24656813). Interacts with the core C/D box snoRNP particle components NOP58 and FBL and with RUVBL1/TIP49 (PubMed:17636026). Interacts with RPAP3 and WDR92 (PubMed:21078300). Interacts with histone H4 and with SWI/SNF complex member SMARCB1/SNF5 (PubMed:22368283). Interacts with the mTORC1 complex member RPTOR (PubMed:24036451).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ECDO9590511EBI-357318,EBI-2557598
RBPMSQ930623EBI-357318,EBI-740322
Ruvbl1P601222EBI-357318,EBI-1634999From a different organism.
TELO2Q9Y4R814EBI-357318,EBI-1043674
TSC22D4Q9Y3Q84EBI-357318,EBI-739485

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • phosphoprotein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120343. 61 interactions.
IntActiQ9NWS0. 50 interactions.
MINTiMINT-1163048.
STRINGi9606.ENSP00000262265.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 599Combined sources
Beta strandi61 – 7212Combined sources
Helixi83 – 9210Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi116 – 12510Combined sources
Helixi126 – 1338Combined sources
Helixi136 – 15419Combined sources
Beta strandi163 – 1675Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PSFX-ray1.58A/B51-174[»]
4PSIX-ray2.45A/B51-174[»]
ProteinModelPortaliQ9NWS0.
SMRiQ9NWS0. Positions 51-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal region is required for binding to phosphorylated substrates while the C-terminal region binds to the other R2TP complex components.1 Publication

Sequence similaritiesi

Belongs to the PIH1 family.Curated

Phylogenomic databases

eggNOGiKOG4356. Eukaryota.
ENOG410XQ8C. LUCA.
GeneTreeiENSGT00510000048192.
HOGENOMiHOG000067888.
HOVERGENiHBG108251.
InParanoidiQ9NWS0.
OMAiLDIFLPY.
PhylomeDBiQ9NWS0.
TreeFamiTF324376.

Family and domain databases

InterProiIPR012981. PIH1.
[Graphical view]
PANTHERiPTHR22997. PTHR22997. 1 hit.
PfamiPF08190. PIH1. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NWS0-1) [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
MANPKLLGMG LSEAEAIGAD SARFEELLLQ ASKELQQAQT TRPESTQIQP
60 70 80 90 100
QPGFCIKTNS SEGKVFINIC HSPSIPPPAD VTEEELLQML EEDQAGFRIP
110 120 130 140 150
MSLGEPHAEL DAKGQGCTAY DVAVNSDFYR RMQNSDFLRE LVITIAREGL
160 170 180 190 200
EDKYNLQLNP EWRMMKNRPF MGSISQQNIR SEQRPRIQEL GDLYTPAPGR
210 220 230 240 250
AESGPEKPHL NLWLEAPDLL LAEVDLPKLD GALGLSLEIG ENRLVMGGPQ
260 270 280 290
QLYHLDAYIP LQINSHESKA AFHRKRKQLM VAMPLLPVPS
Length:290
Mass (Da):32,363
Last modified:October 1, 2000 - v1
Checksum:i074A9CD4037A4882
GO
Isoform 2 (identifier: Q9NWS0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-290: ASKELQQAQT...VAMPLLPVPS → LSCIRIAPFE...ARDHHRQGGP

Show »
Length:180
Mass (Da):19,911
Checksum:iA5D8D025BB07B746
GO
Isoform 3 (identifier: Q9NWS0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-290: KGQGCTAYDV...VAMPLLPVPS → SQCPQRTQES...GGLGRVLFVH

Show »
Length:199
Mass (Da):21,376
Checksum:iEFAF44E772FDD8E1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 102MG → LE in AAH01108 (PubMed:15489334).Curated
Sequence conflicti102 – 1021S → G in BAG57848 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91M → L.1 Publication
Corresponds to variant rs2293012 [ dbSNP | Ensembl ].
VAR_035410
Natural varianti10 – 101G → E.1 Publication
Corresponds to variant rs2293013 [ dbSNP | Ensembl ].
VAR_035411
Natural varianti224 – 2241V → I.1 Publication
Corresponds to variant rs13394 [ dbSNP | Ensembl ].
VAR_035412
Natural varianti230 – 2301D → E.
Corresponds to variant rs34198213 [ dbSNP | Ensembl ].
VAR_035413
Natural varianti287 – 2871P → L.1 Publication
Corresponds to variant rs7462 [ dbSNP | Ensembl ].
VAR_035414

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 290260ASKEL…LPVPS → LSCIRIAPFEEQMRGLMAQT PSLEVVFLYTGLEGAPASPD NQTRIDTNPASAWFLHKDQL LGREGFHQHLPLPLYPSSRR RDRGGAASDARGGPSWVSHP HESGRASCRTGCKRPGMYRL RRSCQQRLLPEDAEQRFLAG ARDHHRQGGP in isoform 2. 1 PublicationVSP_044424Add
BLAST
Alternative sequencei113 – 290178KGQGC…LPVPS → SQCPQRTQESGPLGPFFPRT QESWAQDPPPSAPGDLAPRS DSFPYGRSLVPWTSHTRAVL VLPPGQAGTFPCPTPGPGGL GRVLFVH in isoform 3. 1 PublicationVSP_044425Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000650 mRNA. Translation: BAA91307.1.
AK294687 mRNA. Translation: BAG57848.1.
AK304476 mRNA. Translation: BAG65289.1.
BC001108 mRNA. Translation: AAH01108.1.
CCDSiCCDS12765.1. [Q9NWS0-1]
RefSeqiNP_060386.1. NM_017916.2. [Q9NWS0-1]
UniGeneiHs.5245.

Genome annotation databases

EnsembliENST00000262265; ENSP00000262265; ENSG00000104872. [Q9NWS0-1]
ENST00000596049; ENSP00000470445; ENSG00000104872. [Q9NWS0-1]
GeneIDi55011.
KEGGihsa:55011.
UCSCiuc002pns.3. human. [Q9NWS0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000650 mRNA. Translation: BAA91307.1.
AK294687 mRNA. Translation: BAG57848.1.
AK304476 mRNA. Translation: BAG65289.1.
BC001108 mRNA. Translation: AAH01108.1.
CCDSiCCDS12765.1. [Q9NWS0-1]
RefSeqiNP_060386.1. NM_017916.2. [Q9NWS0-1]
UniGeneiHs.5245.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PSFX-ray1.58A/B51-174[»]
4PSIX-ray2.45A/B51-174[»]
ProteinModelPortaliQ9NWS0.
SMRiQ9NWS0. Positions 51-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120343. 61 interactions.
IntActiQ9NWS0. 50 interactions.
MINTiMINT-1163048.
STRINGi9606.ENSP00000262265.

PTM databases

iPTMnetiQ9NWS0.
PhosphoSiteiQ9NWS0.

Polymorphism and mutation databases

BioMutaiPIH1D1.
DMDMi74719379.

Proteomic databases

EPDiQ9NWS0.
MaxQBiQ9NWS0.
PaxDbiQ9NWS0.
PeptideAtlasiQ9NWS0.
PRIDEiQ9NWS0.

Protocols and materials databases

DNASUi55011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262265; ENSP00000262265; ENSG00000104872. [Q9NWS0-1]
ENST00000596049; ENSP00000470445; ENSG00000104872. [Q9NWS0-1]
GeneIDi55011.
KEGGihsa:55011.
UCSCiuc002pns.3. human. [Q9NWS0-1]

Organism-specific databases

CTDi55011.
GeneCardsiPIH1D1.
HGNCiHGNC:26075. PIH1D1.
HPAiHPA047258.
MIMi611480. gene.
neXtProtiNX_Q9NWS0.
PharmGKBiPA162399535.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4356. Eukaryota.
ENOG410XQ8C. LUCA.
GeneTreeiENSGT00510000048192.
HOGENOMiHOG000067888.
HOVERGENiHBG108251.
InParanoidiQ9NWS0.
OMAiLDIFLPY.
PhylomeDBiQ9NWS0.
TreeFamiTF324376.

Miscellaneous databases

ChiTaRSiPIH1D1. human.
GenomeRNAii55011.
PROiQ9NWS0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NWS0.
CleanExiHS_PIH1D1.
ExpressionAtlasiQ9NWS0. baseline and differential.
GenevisibleiQ9NWS0. HS.

Family and domain databases

InterProiIPR012981. PIH1.
[Graphical view]
PANTHERiPTHR22997. PTHR22997. 1 hit.
PfamiPF08190. PIH1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1; 2 AND 3), VARIANTS LEU-9 AND GLU-10.
    Tissue: Brain, Signet-ring cell carcinoma and Uterus.
  2. "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), VARIANTS ILE-224 AND LEU-287.
    Tissue: Skin.
  3. "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly."
    McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.
    Mol. Cell. Biol. 27:6782-6793(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBL; NOP58 AND RUVBL1.
  4. "PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced apoptosis."
    Inoue M., Saeki M., Egusa H., Niwa H., Kamisaki Y.
    Biochem. Biophys. Res. Commun. 403:340-344(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPAP3 AND WDR92, TISSUE SPECIFICITY.
  5. "CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for mTOR and SMG1 stability."
    Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S., Skehel J.M., de Lange T., Boulton S.J.
    Mol. Cell 39:839-850(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TELO2, IDENTIFICATION IN THE R2TP COMPLEX.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Human PIH1 associates with histone H4 to mediate the glucose-dependent enhancement of pre-rRNA synthesis."
    Zhai N., Zhao Z.L., Cheng M.B., Di Y.W., Yan H.X., Cao C.Y., Dai H., Zhang Y., Shen Y.F.
    J. Mol. Cell Biol. 4:231-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H4 AND SMARCB1, MUTAGENESIS OF PHE-54 AND CYS-55.
  8. "PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA transcription."
    Kamano Y., Saeki M., Egusa H., Kakihara Y., Houry W.A., Yatani H., Kamisaki Y.
    FEBS Lett. 587:3303-3308(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPTOR, TISSUE SPECIFICITY.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  10. "Phosphorylation-dependent PIH1D1 interactions define substrate specificity of the R2TP cochaperone complex."
    Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M., O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.
    Cell Rep. 7:19-26(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 51-174 IN COMPLEX WITH TELO2 PHOSPHOPEPTIDE, INTERACTION WITH EFTUD2; ECD; RPAP3; RPB1; TELO2 AND UBR5, DOMAIN, MUTAGENESIS OF LYS-57; LYS-64; LYS-113; ARG-163; LYS-166 AND ARG-168.

Entry informationi

Entry nameiPIHD1_HUMAN
AccessioniPrimary (citable) accession number: Q9NWS0
Secondary accession number(s): B4DGN7, B4E2X7, Q9BVL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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