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Q96KR7 (PHAR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatase and actin regulator 3
Alternative name(s):
Scaffold-associated PP1-inhibiting protein
Short name=Scapinin
Gene names
Name:PHACTR3
Synonyms:C20orf101, SCAPIN1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

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

Subcellular location

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

Tissue specificity

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 U937, GOTO and HL-60 leukemia cells.

Induction

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

Sequence similarities

Belongs to the phosphatase and actin regulator family.

Contains 4 RPEL repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandActin-binding
   Molecular functionProtein phosphatase inhibitor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentnuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein phosphatase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96KR7-1)

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.
Isoform 2 (identifier: Q96KR7-2)

Also known as: Scapinin-L; Scapinin 1C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.
Isoform 3 (identifier: Q96KR7-3)

Also known as: Scapinin-S;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Phosphatase and actin regulator 3
PRO_0000126638

Regions

Repeat93 – 11826RPEL 1
Repeat401 – 42626RPEL 2
Repeat439 – 46426RPEL 3
Repeat477 – 50226RPEL 4
Region438 – 51881Required for PP1CA binding and inhibition of PP1 activity
Coiled coil346 – 36924 Potential
Coiled coil450 – 48637 Potential
Compositional bias217 – 23923Pro-rich

Amino acid modifications

Modified residue701Phosphothreonine Ref.7

Natural variations

Alternative sequence1 – 4141Missing in isoform 2 and isoform 3.
VSP_009091
Alternative sequence181 – 25070Missing in isoform 3.
VSP_009092
Natural variant1541P → L.
Corresponds to variant rs2277759 [ dbSNP | Ensembl ].
VAR_021969

Experimental info

Sequence conflict3211K → R in CAF04087. Ref.2
Sequence conflict3991K → R in CAF04087. Ref.2

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: E98182FBE3D25D37

FASTA55962,552
        10         20         30         40         50         60 
MAASEDGSGC LVSRGRSQSD PSVLTDSSAT SSADAGENPD EMDQTPPARP EYLVSGIRTP 

        70         80         90        100        110        120 
PVRRNSKLAT LGRIFKPWKW RKKKNEKLKQ TTSALEKKMA GRQGREELIK KGLLEMMEQD 

       130        140        150        160        170        180 
AESKTCNPDG GPRSVQSEPP TPKSETLTSE DAQPGSPLAT GTDQVSLDKP LSSAAHLDDA 

       190        200        210        220        230        240 
AKMPSASSGE EADAGSLLPT TNELSQALAG ADSLDSPPRP LERSVGQLPS PPLLPTPPPK 

       250        260        270        280        290        300 
ASSKTTKNVT GQATLFQASS MKSADPSLRG QLSTPTGSPH LTTVHRPLPP SRVIEELHRA 

       310        320        330        340        350        360 
LATKHRQDSF QGRESKGSPK KRLDVRLSRT SSVERGKERE EAWSFDGALE NKRTAAKESE 

       370        380        390        400        410        420 
ENKENLIINS ELKDDLLLYQ DEEALNDSII SGTLPRKCKK ELLAVKLRNR PSKQELEDRN 

       430        440        450        460        470        480 
IFPRRTDEER QEIRQQIEMK LSKRLSQRPA VEELERRNIL KQRNDQTEQE ERREIKQRLT 

       490        500        510        520        530        540 
RKLNQRPTVD ELRDRKILIR FSDYVEVAKA QDYDRRADKP WTRLSAADKA AIRKELNEYK 

       550 
SNEMEVHASS KHLTRFHRP 

« Hide

Isoform 2 (Scapinin-L) (Scapinin 1C) [UniParc].

Checksum: 9DE458851866A690
Show »

FASTA51858,525
Isoform 3 (Scapinin-S) [UniParc].

Checksum: 2F9803B04D14228F
Show »

FASTA44851,479

References

« Hide 'large scale' references
[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: 12925532] [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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: 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. expand/collapse author list , 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: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 17693683] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB098521 mRNA. Translation: BAC82348.1.
AB098522 mRNA. Translation: BAC82349.1.
AJ311122 mRNA. Translation: CAC67489.2. Different initiation.
AJ617581 mRNA. Translation: CAF04087.1.
AK314493 mRNA. Translation: BAG37093.1.
AL121908, AL357503 Genomic DNA. Translation: CAI22518.1.
AL357503, AL121908 Genomic DNA. Translation: CAI23229.1.
AL357503 Genomic DNA. Translation: CAM28339.1.
CH471077 Genomic DNA. Translation: EAW75429.1.
BC108303 mRNA. Translation: AAI08304.1.
BC117362 mRNA. Translation: AAI17363.1.
BC117364 mRNA. Translation: AAI17365.1.
IPIIPI00064745.
IPI00377257.
IPI00793519.
RefSeqNP_001186434.1. NM_001199505.1.
NP_001186435.1. NM_001199506.1.
NP_542403.1. NM_080672.3.
NP_899067.1. NM_183244.1.
NP_899069.1. NM_183246.1.
UniGeneHs.473218.

3D structure databases

ProteinModelPortalQ96KR7.
SMRQ96KR7. Positions 395-498.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96KR7. 2 interactions.
MINTMINT-1407590.
STRINGQ96KR7.

PTM databases

PhosphoSiteQ96KR7.

Polymorphism databases

DMDM38605426.

Proteomic databases

PRIDEQ96KR7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371015; ENSP00000360054; ENSG00000087495.
GeneID116154.
KEGGhsa:116154.
UCSCuc002yat.1. human.
uc002yau.1. human.
uc002yax.1. human.

Organism-specific databases

CTD116154.
GeneCardsGC20P058152.
H-InvDBHIX0015963.
HGNCHGNC:15833. PHACTR3.
MIM608725. gene.
neXtProtNX_Q96KR7.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18326.
GeneTreeENSGT00390000004420.
HOGENOMHBG445206.
HOVERGENHBG057352.
InParanoidQ96KR7.
OMAAAKMPSA.
PhylomeDBQ96KR7.

Gene expression databases

ArrayExpressQ96KR7.
BgeeQ96KR7.
CleanExHS_PHACTR3.
GenevestigatorQ96KR7.
GermOnlineENSG00000087495. Homo sapiens.

Family and domain databases

InterProIPR004018. RPEL_repeat.
[Graphical view]
PfamPF02755. RPEL. 2 hits.
[Graphical view]
SMARTSM00707. RPEL. 4 hits.
[Graphical view]
PROSITEPS51073. RPEL. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio79802.
SOURCESearch...

Entry information

Entry namePHAR3_HUMAN
AccessionPrimary (citable) accession number: Q96KR7
Secondary accession number(s): B1AN69 expand/collapse secondary AC list , B2RB46, Q32P33, Q707P6, Q9H4T4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 90 of the entry and version 1 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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families