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Q8IZ21 (PHAR4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 4
Gene names
Name:PHACTR4
ORF Names:PRO2963
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway By similarity.

Subunit structure

Binds PPP1CA and actin By similarity.

Subcellular location

Cytoplasm By similarity. Cell projectionlamellipodium By similarity.

Sequence similarities

Belongs to the phosphatase and actin regulator family.

Contains 3 RPEL repeats.

Sequence caution

The sequence AAG35507.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH68508.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence BAB14483.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB15130.1 differs from that shown. Reason: Frameshift at position 51.

The sequence CAH18286.1 differs from that shown. Reason: Frameshift at position 53.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell projection
Cytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

closure of optic fissure

Inferred from sequence or structural similarity. Source: UniProtKB

enteric nervous system development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of integrin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neural crest cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionactin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase 1 binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase type 1 activator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IZ21-1)

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: Q8IZ21-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MEDPF → MGQADVSRPVNPDAV
Isoform 3 (identifier: Q8IZ21-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
Isoform 4 (identifier: Q8IZ21-4)

The sequence of this isoform differs from the canonical sequence as follows:
     6-6: E → DFSREPWNSRGSRPAHYRARHGPGQCGSRRHNTSYQKEEQVLRLWQDLQALEMEEKKK
     7-702: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 702702Phosphatase and actin regulator 4
PRO_0000287306

Regions

Repeat63 – 8826RPEL 1
Repeat583 – 60826RPEL 2
Repeat621 – 64626RPEL 3
Compositional bias227 – 433207Pro-rich
Compositional bias478 – 4825Poly-Glu
Compositional bias508 – 5136Poly-Glu

Amino acid modifications

Modified residue1181Phosphoserine Ref.14
Modified residue1311Phosphoserine Ref.9
Modified residue3421Phosphoserine Ref.9
Modified residue3441Phosphoserine Ref.9
Modified residue3581Phosphothreonine Ref.9
Modified residue4271Phosphoserine Ref.9
Modified residue4321Phosphothreonine Ref.9
Modified residue4431Phosphoserine By similarity
Modified residue4641Phosphoserine Ref.14
Modified residue6281Phosphoserine Ref.7 Ref.9 Ref.12 Ref.14

Natural variations

Alternative sequence1 – 1616Missing in isoform 3.
VSP_025436
Alternative sequence1 – 55MEDPF → MGQADVSRPVNPDAV in isoform 2.
VSP_025437
Alternative sequence61E → DFSREPWNSRGSRPAHYRAR HGPGQCGSRRHNTSYQKEEQ VLRLWQDLQALEMEEKKK in isoform 4.
VSP_039730
Alternative sequence7 – 702696Missing in isoform 4.
VSP_039731

Experimental info

Sequence conflict1831E → G in CAH18286. Ref.2
Sequence conflict4591L → P in BAB14483. Ref.1

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: 89AC6A1D08411948

FASTA70278,211
        10         20         30         40         50         60 
MEDPFEEADQ PTTEPGMVLD SVEAGDTTPP TKRKSKFSGF GKIFKPWKWR KKKSSDKFKE 

        70         80         90        100        110        120 
TSEVLERKIS MRKPREELVK RGVLLEDPEQ GGEDPGKPSD AMLKNGHTTP IGNARSSSPV 

       130        140        150        160        170        180 
QVEEEPVRLA SLRKAIPEED LKKRLGSTGS QPNSEAESVP ENVPKPPLLP PKRPLSSSHE 

       190        200        210        220        230        240 
ASEGQAKDAT SSGGTARFII STSITTAPAA TTAATSLAKT VNLSVTPSPA PRTLPAAPAS 

       250        260        270        280        290        300 
TNTTATPSLT HMVPAKQPPI PPPKPAHRNS NPVIAELSQA INSGTLLSKP SPPLPPKRGI 

       310        320        330        340        350        360 
PSTSVPTLES AAAITTKTPS DEREKSTCSM GSELLPMISP RSPSPPLPTH IPPEPPRTPP 

       370        380        390        400        410        420 
FPAKTFQVVP EIEFPPSLDL HQEIPQQEDQ KKEVPKRILD QNFGEPHIPS RLPPLPLHIR 

       430        440        450        460        470        480 
IQQALTSPLP MTPILEGSHR AHSLLFENSD SFSEDSSTLG RTRSLPITIE MLKVPDDEEE 

       490        500        510        520        530        540 
EEQTCPSTFS EEMTPTSVIP KLPQCLREEE EKESDSDSEG PIQYRDEEDE DESYQSALAN 

       550        560        570        580        590        600 
KVKRKDTLAM KLNHRPSEPE LNLNSWPCKS KEEWNEIRHQ IGNTLIRRLS QRPTPEELEQ 

       610        620        630        640        650        660 
RNILQPKNEA DRQAEKREIK RRLTRKLSQR PTVAELLARK ILRFNEYVEV TDAQDYDRRA 

       670        680        690        700 
DKPWTKLTPA DKAAIRKELN EFKSSEMEVH EESKHFTRYH RP 

« Hide

Isoform 2 [UniParc].

Checksum: 3F9C6DE318A7B2F0
Show »

FASTA71279,129
Isoform 3 [UniParc].

Checksum: D08F12D5D26DB362
Show »

FASTA68676,436
Isoform 4 [UniParc].

Checksum: C71BB87679575723
Show »

FASTA637,586

References

[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. 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 271-702 (ISOFORM 1).
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[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] (ISOFORMS 1; 2 AND 4).
Tissue: Adrenal cortex, Skin and Testis.
[6]"Functional prediction of the coding sequences of 75 new genes deduced by analysis of cDNA clones from human fetal liver."
Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W., Gao F., Liu M., He F.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 365-702 (ISOFORM 1).
Tissue: Fetal liver.
[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-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-342; SER-344; THR-358; SER-427; THR-432 AND SER-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"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 SER-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-464 AND SER-628, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK023233 mRNA. Translation: BAB14483.1. Different initiation.
AK025436 mRNA. Translation: BAB15130.1. Frameshift.
CR749449 mRNA. Translation: CAH18286.1. Frameshift.
AL670471, CR391992, AL360012 Genomic DNA. Translation: CAM12870.1.
CR589951, AL360012, CR391992 Genomic DNA. Translation: CAM12871.1.
CH471059 Genomic DNA. Translation: EAX07696.1.
CH471059 Genomic DNA. Translation: EAX07698.1.
BC021247 mRNA. Translation: AAH21247.3.
BC029266 mRNA. Translation: AAH29266.1.
BC068508 mRNA. Translation: AAH68508.1. Sequence problems.
AF130081 mRNA. Translation: AAG35507.1. Different initiation.
CCDSCCDS41293.1. [Q8IZ21-1]
CCDS41294.1. [Q8IZ21-2]
RefSeqNP_001041648.1. NM_001048183.1. [Q8IZ21-1]
NP_076412.3. NM_023923.3. [Q8IZ21-2]
UniGeneHs.225641.

3D structure databases

ProteinModelPortalQ8IZ21.
SMRQ8IZ21. Positions 544-650.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122429. 10 interactions.
DIPDIP-47323N.
IntActQ8IZ21. 1 interaction.

PTM databases

PhosphoSiteQ8IZ21.

Polymorphism databases

DMDM74728415.

Proteomic databases

MaxQBQ8IZ21.
PaxDbQ8IZ21.
PRIDEQ8IZ21.

Protocols and materials databases

DNASU65979.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373836; ENSP00000362942; ENSG00000204138. [Q8IZ21-2]
ENST00000373839; ENSP00000362945; ENSG00000204138. [Q8IZ21-1]
GeneID65979.
KEGGhsa:65979.
UCSCuc001bpw.3. human. [Q8IZ21-1]
uc001bpy.3. human. [Q8IZ21-2]

Organism-specific databases

CTD65979.
GeneCardsGC01P028696.
HGNCHGNC:25793. PHACTR4.
HPAHPA028985.
MIM608726. gene.
neXtProtNX_Q8IZ21.
PharmGKBPA134959472.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG275065.
HOVERGENHBG108247.
KOK17585.
OMAREKSTCS.
OrthoDBEOG7QG44R.
PhylomeDBQ8IZ21.
TreeFamTF316316.

Gene expression databases

BgeeQ8IZ21.
CleanExHS_PHACTR4.
GenevestigatorQ8IZ21.

Family and domain databases

InterProIPR004018. RPEL_repeat.
[Graphical view]
PfamPF02755. RPEL. 3 hits.
[Graphical view]
SMARTSM00707. RPEL. 3 hits.
[Graphical view]
PROSITEPS51073. RPEL. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHACTR4. human.
GenomeRNAi65979.
NextBio67423.
PMAP-CutDBQ8IZ21.
PROQ8IZ21.
SOURCESearch...

Entry information

Entry namePHAR4_HUMAN
AccessionPrimary (citable) accession number: Q8IZ21
Secondary accession number(s): A2APK6 expand/collapse secondary AC list , B9ZVW0, D3DPM3, Q68DD4, Q6NUN6, Q8N384, Q9H395, Q9H6X0, Q9H8W6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 95 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM