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Q6PGN9 (PSRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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:
Proline/serine-rich coiled-coil protein 1
Gene names
Name:PSRC1
Synonyms:DDA3
ORF Names:FP3214
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression. Ref.8 Ref.11

Subunit structure

Interacts with APC2 By similarity. Interacts with KIF2A. Ref.8

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Note: Detected at the mitotic spindle and spindle poles. Diffusely distributed throughout the cell during interphase. Ref.1 Ref.8 Ref.11

Tissue specificity

Widely expressed in adult and fetal tissues, with highest expression in the adult brain and fetal thymus. Not detected in adult skeletal muscle. Ref.1

Post-translational modification

Phosphorylated during mitosis. Ref.8

Sequence similarities

Belongs to the PSRC1 family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule bundle formation

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

mitotic metaphase plate congression

Inferred from direct assay Ref.8. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

positive regulation of cyclin-dependent protein kinase activity

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

positive regulation of microtubule polymerization

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

regulation of mitotic spindle organization

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

cytosol

Inferred from direct assay Ref.8. Source: UniProtKB

microtubule cytoskeleton

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

midbody

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

nucleus

Inferred from direct assay. Source: HPA

spindle

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmicrotubule binding

Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform C (identifier: Q6PGN9-1)

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 A (identifier: Q6PGN9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     213-242: Missing.
Note: Contains a phosphoserine at position 212. Contains a phosphothreonine at position 215.
Isoform B (identifier: Q6PGN9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     222-310: VSGSGEFVGL...RGALPPDSLS → ACQPNATHQP...KRSGQQARLQ
     311-363: Missing.
Isoform D (identifier: Q6PGN9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-170: Missing.
     213-242: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 42. Contains a phosphothreonine at position 45.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Proline/serine-rich coiled-coil protein 1
PRO_0000273728

Regions

Repeat38 – 4141
Repeat68 – 7142
Repeat238 – 24143
Repeat243 – 24644
Region103 – 2461444 X 4 AA repeats of P-X-X-P
Coiled coil70 – 9425 Potential
Compositional bias238 – 361124Pro/Ser-rich

Amino acid modifications

Modified residue221Phosphoserine Ref.14
Modified residue651Phosphoserine Ref.13
Modified residue701Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14
Modified residue981Phosphoserine Ref.13
Modified residue1451Phosphothreonine Ref.10
Modified residue1861Phosphoserine Ref.10 Ref.13
Modified residue1901Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 170170Missing in isoform D.
VSP_022602
Alternative sequence213 – 24230Missing in isoform A and isoform D.
VSP_022591
Alternative sequence222 – 31089VSGSG…PDSLS → ACQPNATHQPECATWQRCPT SGFSVNSKRASKTKHCRTQS AGKWTQGSCFPATKSSCHGC HSQQSAAPQESGSPRTYQVK RSGQQARLQ in isoform B.
VSP_022592
Alternative sequence311 – 36353Missing in isoform B.
VSP_022593
Natural variant3121R → Q.
Corresponds to variant rs34863121 [ dbSNP | Ensembl ].
VAR_051288

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 4B59C01EB74F3B72

FASTA36338,796
        10         20         30         40         50         60 
MEDLEEDVRF IVDETLDFGG LSPSDSREEE DITVLVTPEK PLRRGLSHRS DPNAVAPAPQ 

        70         80         90        100        110        120 
GVRLSLGPLS PEKLEEILDE ANRLAAQLEQ CALQDRESAG EGLGPRRVKP SPRRETFVLK 

       130        140        150        160        170        180 
DSPVRDLLPT VNSLTRSTPS PSSLTPRLRS NDRKGSVRAL RATSGKRPSN MKRESPTCNL 

       190        200        210        220        230        240 
FPASKSPASS PLTRSTPPVR GRAGPSGRAA ASEETRAAKL RVSGSGEFVG LTLKFLHPSP 

       250        260        270        280        290        300 
PGPPTPIRSV LAPQPSTSNS QRLPRPQGAA AKSSSQLPIP SAIPRPASRM PLTSRSVPPG 

       310        320        330        340        350        360 
RGALPPDSLS TRKGLPRPST AGHRVRESGH KVPVSQRLNL PVMGATRSNL QPPRKVAVPG 


PTR 

« Hide

Isoform A [UniParc].

Checksum: 75BC7DB6B0705E2E
Show »

FASTA33335,632
Isoform B [UniParc].

Checksum: 79C03FBF5111CBBA
Show »

FASTA31033,638
Isoform D [UniParc].

Checksum: 3B72DF56B3BC730E
Show »

FASTA16316,981

References

« Hide 'large scale' references
[1]"Cloning and characterization of human and mouse DDA3 genes."
Lo P.-K., Wang F.-F.
Biochim. Biophys. Acta 1579:214-218(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"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 B).
Tissue: Cerebellum.
[3]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
[4]"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] (ISOFORMS A AND B).
[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 (JUL-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
Tissue: Skin.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-215 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-45 (ISOFORM D), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"DDA3 recruits microtubule depolymerase Kif2a to spindle poles and controls spindle dynamics and mitotic chromosome movement."
Jang C.Y., Wong J., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
J. Cell Biol. 181:255-267(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH KIF2A, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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 THR-145; SER-186 AND SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"The N-terminal domain of DDA3 regulates the spindle-association of the microtubule depolymerase Kif2a and controls the mitotic function of DDA3."
Jang C.Y., Fang G.
Cell Cycle 8:3165-3171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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-65; SER-70; SER-98 AND SER-186, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-215 (ISOFORM A), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-45 (ISOFORM D), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-22 AND SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF223000 mRNA. Translation: AAN73431.1.
AF322891 Genomic DNA. Translation: AAN73434.1.
AK126567 mRNA. Translation: BAC86599.1.
AF447874 mRNA. Translation: AAQ04649.1.
AL390252 Genomic DNA. Translation: CAI13172.1.
AL390252 Genomic DNA. Translation: CAI13173.1.
AL390252 Genomic DNA. Translation: CAI13174.2.
CH471122 Genomic DNA. Translation: EAW56373.1.
BC056909 mRNA. Translation: AAH56909.1.
RefSeqNP_001005290.1. NM_001005290.3.
NP_001027462.1. NM_001032291.2.
NP_116025.1. NM_032636.7.
XP_005271339.1. XM_005271282.1.
XP_005271340.1. XM_005271283.1.
UniGeneHs.405925.

3D structure databases

ProteinModelPortalQ6PGN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124224. 9 interactions.
IntActQ6PGN9. 1 interaction.
STRING9606.ENSP00000358925.

PTM databases

PhosphoSiteQ6PGN9.

Polymorphism databases

DMDM74737651.

Proteomic databases

PaxDbQ6PGN9.
PRIDEQ6PGN9.

Protocols and materials databases

DNASU84722.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369903; ENSP00000358919; ENSG00000134222. [Q6PGN9-2]
ENST00000369904; ENSP00000358920; ENSG00000134222. [Q6PGN9-3]
ENST00000369907; ENSP00000358923; ENSG00000134222. [Q6PGN9-2]
ENST00000369909; ENSP00000358925; ENSG00000134222. [Q6PGN9-2]
ENST00000409138; ENSP00000474667; ENSG00000134222. [Q6PGN9-1]
ENST00000409267; ENSP00000386323; ENSG00000134222. [Q6PGN9-2]
ENST00000438534; ENSP00000413591; ENSG00000134222. [Q6PGN9-1]
GeneID84722.
KEGGhsa:84722.
UCSCuc001dxb.3. human. [Q6PGN9-4]
uc001dxc.3. human. [Q6PGN9-2]
uc001dxf.3. human. [Q6PGN9-3]
uc001dxj.3. human. [Q6PGN9-1]

Organism-specific databases

CTD84722.
GeneCardsGC01M109822.
HGNCHGNC:24472. PSRC1.
HPAHPA049315.
HPA056561.
MIM613126. gene.
neXtProtNX_Q6PGN9.
PharmGKBPA142671120.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39428.
HOGENOMHOG000231348.
HOVERGENHBG080237.
InParanoidQ6PGN9.
OMASPTCNLF.
OrthoDBEOG7T4MKW.
PhylomeDBQ6PGN9.
TreeFamTF338374.

Gene expression databases

ArrayExpressQ6PGN9.
BgeeQ6PGN9.
CleanExHS_PSRC1.
GenevestigatorQ6PGN9.

Family and domain databases

InterProIPR026658. DDA3.
IPR026657. DDA3/GTSE-1.
[Graphical view]
PANTHERPTHR21584. PTHR21584. 1 hit.
PTHR21584:SF1. PTHR21584:SF1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPSRC1. human.
GeneWikiPSRC1.
GenomeRNAi84722.
NextBio74828.
PROQ6PGN9.
SOURCESearch...

Entry information

Entry namePSRC1_HUMAN
AccessionPrimary (citable) accession number: Q6PGN9
Secondary accession number(s): Q5T2Z3 expand/collapse secondary AC list , Q6ZTI8, Q71MG3, Q9BV77
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 78 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 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 1

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