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Protein

Phosphatase and actin regulator 3

Gene

PHACTR3

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

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Protein phosphatase inhibitor

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatase and actin regulator 3
Alternative name(s):
Scaffold-associated PP1-inhibiting protein
Short name:
Scapinin
Gene namesi
Name:PHACTR3
Synonyms:C20orf101, SCAPIN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15833. PHACTR3.

Subcellular locationi

  • Nucleus matrix

  • Note: Localized to the nuclear matrix-intermediate filament scaffold. Isoform 2 is also found in some cytoplasmic extensions.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394750.

Polymorphism and mutation databases

BioMutaiPHACTR3.
DMDMi38605426.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Phosphatase and actin regulator 3PRO_0000126638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701PhosphothreonineCombined sources
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei236 – 2361PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ96KR7.
PaxDbiQ96KR7.
PRIDEiQ96KR7.

PTM databases

iPTMnetiQ96KR7.
PhosphoSiteiQ96KR7.

Expressioni

Tissue specificityi

Abundantly expressed in brain. Also found in several tumors such as lung carcinomas, nervous tumors and HL-60 leukemia cells. Isoform 3 is the major form in U-937, GOTO and HL-60 leukemia cells.

Inductioni

Down-regulated in HL-60 leukemia cells by RA, PMA and dimethyl sulfoxide.

Gene expression databases

BgeeiQ96KR7.
CleanExiHS_PHACTR3.
ExpressionAtlasiQ96KR7. baseline and differential.
GenevisibleiQ96KR7. HS.

Organism-specific databases

HPAiHPA051834.
HPA054847.

Interactioni

Subunit structurei

Binds actin and PPP1CA; thus inhibiting the protein phosphatase 1 (PP1) activity.

Protein-protein interaction databases

BioGridi125483. 4 interactions.
IntActiQ96KR7. 5 interactions.
MINTiMINT-1407590.
STRINGi9606.ENSP00000360054.

Structurei

3D structure databases

ProteinModelPortaliQ96KR7.
SMRiQ96KR7. Positions 403-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati93 – 11826RPEL 1Add
BLAST
Repeati401 – 42626RPEL 2Add
BLAST
Repeati439 – 46426RPEL 3Add
BLAST
Repeati477 – 50226RPEL 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni438 – 51881Required for PP1CA binding and inhibition of PP1 activityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili346 – 36924Sequence analysisAdd
BLAST
Coiled coili450 – 48637Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi217 – 23923Pro-richAdd
BLAST

Sequence similaritiesi

Contains 4 RPEL repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410IMQM. Eukaryota.
ENOG410YAYH. LUCA.
GeneTreeiENSGT00390000004420.
HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ96KR7.
KOiK17594.
OMAiDAESKTC.
OrthoDBiEOG7XWPN6.
PhylomeDBiQ96KR7.
TreeFamiTF316316.

Family and domain databases

InterProiIPR029990. Phactr3.
IPR004018. RPEL_repeat.
[Graphical view]
PANTHERiPTHR12751:SF7. PTHR12751:SF7. 1 hit.
PfamiPF02755. RPEL. 1 hit.
[Graphical view]
SMARTiSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEiPS51073. RPEL. 4 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96KR7-1) [UniParc]FASTAAdd to basket

Also known as: Scapinin 1B

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
MAASEDGSGC LVSRGRSQSD PSVLTDSSAT SSADAGENPD EMDQTPPARP
60 70 80 90 100
EYLVSGIRTP PVRRNSKLAT LGRIFKPWKW RKKKNEKLKQ TTSALEKKMA
110 120 130 140 150
GRQGREELIK KGLLEMMEQD AESKTCNPDG GPRSVQSEPP TPKSETLTSE
160 170 180 190 200
DAQPGSPLAT GTDQVSLDKP LSSAAHLDDA AKMPSASSGE EADAGSLLPT
210 220 230 240 250
TNELSQALAG ADSLDSPPRP LERSVGQLPS PPLLPTPPPK ASSKTTKNVT
260 270 280 290 300
GQATLFQASS MKSADPSLRG QLSTPTGSPH LTTVHRPLPP SRVIEELHRA
310 320 330 340 350
LATKHRQDSF QGRESKGSPK KRLDVRLSRT SSVERGKERE EAWSFDGALE
360 370 380 390 400
NKRTAAKESE ENKENLIINS ELKDDLLLYQ DEEALNDSII SGTLPRKCKK
410 420 430 440 450
ELLAVKLRNR PSKQELEDRN IFPRRTDEER QEIRQQIEMK LSKRLSQRPA
460 470 480 490 500
VEELERRNIL KQRNDQTEQE ERREIKQRLT RKLNQRPTVD ELRDRKILIR
510 520 530 540 550
FSDYVEVAKA QDYDRRADKP WTRLSAADKA AIRKELNEYK SNEMEVHASS

KHLTRFHRP
Length:559
Mass (Da):62,552
Last modified:December 1, 2001 - v1
Checksum:iE98182FBE3D25D37
GO
Isoform 2 (identifier: Q96KR7-2) [UniParc]FASTAAdd to basket

Also known as: Scapinin-L, Scapinin 1C

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Show »
Length:518
Mass (Da):58,525
Checksum:i9DE458851866A690
GO
Isoform 3 (identifier: Q96KR7-3) [UniParc]FASTAAdd to basket

Also known as: Scapinin-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.
     181-250: Missing.

Show »
Length:448
Mass (Da):51,479
Checksum:i2F9803B04D14228F
GO
Isoform 4 (identifier: Q96KR7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MAASEDGSGCLVSRGRSQSDPSVLTDSSATSSADAGENP → MRGRGGGRARCPAPLRSLLGAFGARDAAAAARDPAQ

Show »
Length:556
Mass (Da):62,373
Checksum:i347BA6104D0920FE
GO

Sequence cautioni

The sequence CAC67489.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621V → M in AK098788 (PubMed:14702039).Curated
Sequence conflicti118 – 1181E → G in AK098788 (PubMed:14702039).Curated
Sequence conflicti321 – 3211K → R in CAF04087 (Ref. 2) Curated
Sequence conflicti399 – 3991K → R in CAF04087 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541P → L.
Corresponds to variant rs2277759 [ dbSNP | Ensembl ].
VAR_021969

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 2 and isoform 3. 3 PublicationsVSP_009091Add
BLAST
Alternative sequencei1 – 3939MAASE…AGENP → MRGRGGGRARCPAPLRSLLG AFGARDAAAAARDPAQ in isoform 4. 1 PublicationVSP_044546Add
BLAST
Alternative sequencei181 – 25070Missing in isoform 3. 1 PublicationVSP_009092Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB098521 mRNA. Translation: BAC82348.1.
AB098522 mRNA. Translation: BAC82349.1.
AJ311122 mRNA. Translation: CAC67489.2. Different initiation.
AJ617581 mRNA. Translation: CAF04087.1.
AK098788 mRNA. No translation available.
AK314493 mRNA. Translation: BAG37093.1.
AK316047 mRNA. Translation: BAH14418.1.
AL121908, AL357503 Genomic DNA. Translation: CAI22517.1.
AL121908, AL357503 Genomic DNA. Translation: CAI22518.1.
AL357503, AL121908 Genomic DNA. Translation: CAI23227.1.
AL357503 Genomic DNA. Translation: CAI23228.2.
AL357503, AL121908 Genomic DNA. Translation: CAI23229.1.
AL357503 Genomic DNA. Translation: CAM28339.1.
CH471077 Genomic DNA. Translation: EAW75428.1.
CH471077 Genomic DNA. Translation: EAW75429.1.
CH471077 Genomic DNA. Translation: EAW75430.1.
BC108303 mRNA. Translation: AAI08304.1.
BC117362 mRNA. Translation: AAI17363.1.
BC117364 mRNA. Translation: AAI17365.1.
CCDSiCCDS13480.1. [Q96KR7-1]
CCDS13481.1. [Q96KR7-3]
CCDS42895.1. [Q96KR7-2]
CCDS56202.1. [Q96KR7-4]
RefSeqiNP_001186434.1. NM_001199505.1. [Q96KR7-4]
NP_001186435.1. NM_001199506.1. [Q96KR7-2]
NP_001268436.1. NM_001281507.1. [Q96KR7-2]
NP_542403.1. NM_080672.4. [Q96KR7-1]
NP_899067.1. NM_183244.1. [Q96KR7-2]
NP_899069.1. NM_183246.1. [Q96KR7-3]
XP_011526827.1. XM_011528525.1. [Q96KR7-2]
UniGeneiHs.473218.

Genome annotation databases

EnsembliENST00000355648; ENSP00000347866; ENSG00000087495. [Q96KR7-2]
ENST00000359926; ENSP00000353002; ENSG00000087495. [Q96KR7-4]
ENST00000361300; ENSP00000354555; ENSG00000087495. [Q96KR7-3]
ENST00000371015; ENSP00000360054; ENSG00000087495. [Q96KR7-1]
ENST00000395636; ENSP00000378998; ENSG00000087495. [Q96KR7-2]
ENST00000541461; ENSP00000442483; ENSG00000087495. [Q96KR7-2]
GeneIDi116154.
KEGGihsa:116154.
UCSCiuc002yat.3. human. [Q96KR7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB098521 mRNA. Translation: BAC82348.1.
AB098522 mRNA. Translation: BAC82349.1.
AJ311122 mRNA. Translation: CAC67489.2. Different initiation.
AJ617581 mRNA. Translation: CAF04087.1.
AK098788 mRNA. No translation available.
AK314493 mRNA. Translation: BAG37093.1.
AK316047 mRNA. Translation: BAH14418.1.
AL121908, AL357503 Genomic DNA. Translation: CAI22517.1.
AL121908, AL357503 Genomic DNA. Translation: CAI22518.1.
AL357503, AL121908 Genomic DNA. Translation: CAI23227.1.
AL357503 Genomic DNA. Translation: CAI23228.2.
AL357503, AL121908 Genomic DNA. Translation: CAI23229.1.
AL357503 Genomic DNA. Translation: CAM28339.1.
CH471077 Genomic DNA. Translation: EAW75428.1.
CH471077 Genomic DNA. Translation: EAW75429.1.
CH471077 Genomic DNA. Translation: EAW75430.1.
BC108303 mRNA. Translation: AAI08304.1.
BC117362 mRNA. Translation: AAI17363.1.
BC117364 mRNA. Translation: AAI17365.1.
CCDSiCCDS13480.1. [Q96KR7-1]
CCDS13481.1. [Q96KR7-3]
CCDS42895.1. [Q96KR7-2]
CCDS56202.1. [Q96KR7-4]
RefSeqiNP_001186434.1. NM_001199505.1. [Q96KR7-4]
NP_001186435.1. NM_001199506.1. [Q96KR7-2]
NP_001268436.1. NM_001281507.1. [Q96KR7-2]
NP_542403.1. NM_080672.4. [Q96KR7-1]
NP_899067.1. NM_183244.1. [Q96KR7-2]
NP_899069.1. NM_183246.1. [Q96KR7-3]
XP_011526827.1. XM_011528525.1. [Q96KR7-2]
UniGeneiHs.473218.

3D structure databases

ProteinModelPortaliQ96KR7.
SMRiQ96KR7. Positions 403-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125483. 4 interactions.
IntActiQ96KR7. 5 interactions.
MINTiMINT-1407590.
STRINGi9606.ENSP00000360054.

PTM databases

iPTMnetiQ96KR7.
PhosphoSiteiQ96KR7.

Polymorphism and mutation databases

BioMutaiPHACTR3.
DMDMi38605426.

Proteomic databases

EPDiQ96KR7.
PaxDbiQ96KR7.
PRIDEiQ96KR7.

Protocols and materials databases

DNASUi116154.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355648; ENSP00000347866; ENSG00000087495. [Q96KR7-2]
ENST00000359926; ENSP00000353002; ENSG00000087495. [Q96KR7-4]
ENST00000361300; ENSP00000354555; ENSG00000087495. [Q96KR7-3]
ENST00000371015; ENSP00000360054; ENSG00000087495. [Q96KR7-1]
ENST00000395636; ENSP00000378998; ENSG00000087495. [Q96KR7-2]
ENST00000541461; ENSP00000442483; ENSG00000087495. [Q96KR7-2]
GeneIDi116154.
KEGGihsa:116154.
UCSCiuc002yat.3. human. [Q96KR7-1]

Organism-specific databases

CTDi116154.
GeneCardsiPHACTR3.
HGNCiHGNC:15833. PHACTR3.
HPAiHPA051834.
HPA054847.
MIMi608725. gene.
neXtProtiNX_Q96KR7.
PharmGKBiPA128394750.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IMQM. Eukaryota.
ENOG410YAYH. LUCA.
GeneTreeiENSGT00390000004420.
HOGENOMiHOG000220879.
HOVERGENiHBG057352.
InParanoidiQ96KR7.
KOiK17594.
OMAiDAESKTC.
OrthoDBiEOG7XWPN6.
PhylomeDBiQ96KR7.
TreeFamiTF316316.

Miscellaneous databases

ChiTaRSiPHACTR3. human.
GeneWikiiPHACTR3.
GenomeRNAii116154.
NextBioi79802.
PROiQ96KR7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96KR7.
CleanExiHS_PHACTR3.
ExpressionAtlasiQ96KR7. baseline and differential.
GenevisibleiQ96KR7. HS.

Family and domain databases

InterProiIPR029990. Phactr3.
IPR004018. RPEL_repeat.
[Graphical view]
PANTHERiPTHR12751:SF7. PTHR12751:SF7. 1 hit.
PfamiPF02755. RPEL. 1 hit.
[Graphical view]
SMARTiSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEiPS51073. RPEL. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Scapinin, a putative protein phosphatase-1 regulatory subunit associated with the nuclear nonchromatin structure."
    Sagara J., Higuchi T., Hattori Y., Moriya M., Sarvotham H., Shima H., Shirato H., Kikuchi K., Taniguchi S.
    J. Biol. Chem. 278:45611-45619(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH PP1CA.
    Tissue: Promyelocytic leukemia.
  2. "Structure and expression of scapinin in mouse and human."
    Worch S., Kussmann S., Hansmann I., Schlote D.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  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] (ISOFORMS 1; 2 AND 4).
    Tissue: Brain, Hippocampus and Kidney.
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Tissue: Brain.
  7. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.

Entry informationi

Entry nameiPHAR3_HUMAN
AccessioniPrimary (citable) accession number: Q96KR7
Secondary accession number(s): B1AKX0
, B1AN68, B1AN69, B2RB46, Q32P33, Q707P6, Q9H4T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 131 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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.