Q6PGN9 (PSRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline/serine-rich coiled-coil protein 1

Gene names

Name:	PSRC1
Synonyms:	DDA3
ORF Names:	FP3214

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle 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 process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW microtubule 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 microtubule polymerization Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL positive regulation of transcription, DNA-dependent 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_component	cytosol Inferred from direct assay Ref.8. Source: UniProtKB midbody Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL spindle Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	microtubule 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	Proline/serine-rich coiled-coil protein 1		PRO_0000273728
Regions
	Repeat	38 – 41	4	1
	Repeat	68 – 71	4	2
	Repeat	238 – 241	4	3
	Repeat	243 – 246	4	4
	Region	103 – 246	144	4 X 4 AA repeats of P-X-X-P
	Coiled coil	70 – 94	25	Potential
	Compositional bias	238 – 361	124	Pro/Ser-rich
Amino acid modifications
	Modified residue	22	1	Phosphoserine Ref.14
	Modified residue	65	1	Phosphoserine Ref.13
	Modified residue	70	1	Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14
	Modified residue	98	1	Phosphoserine Ref.13
	Modified residue	145	1	Phosphothreonine Ref.10
	Modified residue	186	1	Phosphoserine Ref.10 Ref.13
	Modified residue	190	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 170	170	Missing in isoform D.		VSP_022602
	Alternative sequence	213 – 242	30	Missing in isoform A and isoform D.		VSP_022591
	Alternative sequence	222 – 310	89	VSGSG…PDSLS → ACQPNATHQPECATWQRCPT SGFSVNSKRASKTKHCRTQS AGKWTQGSCFPATKSSCHGC HSQQSAAPQESGSPRTYQVK RSGQQARLQ in isoform B.		VSP_022592
	Alternative sequence	311 – 363	53	Missing in isoform B.		VSP_022593
	Natural variant	312	1	R → Q. Corresponds to variant rs34863121 [ dbSNP | Ensembl ].		VAR_051288

Sequences

	Sequence		Length	Mass (Da)
	Isoform C [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4B59C01EB74F3B72	FASTA	363	38,796
	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
	Isoform A [UniParc]. Checksum: 75BC7DB6B0705E2E	FASTA	333	35,632
	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 ASPPTPIRSV LAPQPSTSNS QRLPRPQGAA 250 260 270 280 290 300 AKSSSQLPIP SAIPRPASRM PLTSRSVPPG RGALPPDSLS TRKGLPRPST AGHRVRESGH 310 320 330 KVPVSQRLNL PVMGATRSNL QPPRKVAVPG PTR
	Isoform B [UniParc]. Checksum: 79C03FBF5111CBBA	FASTA	310	33,638
	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 RACQPNATHQ PECATWQRCP 250 260 270 280 290 300 TSGFSVNSKR ASKTKHCRTQ SAGKWTQGSC FPATKSSCHG CHSQQSAAPQ ESGSPRTYQV 310 KRSGQQARLQ
	Isoform D [UniParc]. Checksum: 3B72DF56B3BC730E	FASTA	163	16,981
	10 20 30 40 50 60 MKRESPTCNL FPASKSPASS PLTRSTPPVR GRAGPSGRAA ASPPTPIRSV LAPQPSTSNS 70 80 90 100 110 120 QRLPRPQGAA AKSSSQLPIP SAIPRPASRM PLTSRSVPPG RGALPPDSLS TRKGLPRPST 130 140 150 160 AGHRVRESGH KVPVSQRLNL PVMGATRSNL QPPRKVAVPG PTR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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), MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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), MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00027963. IPI00445113. IPI00448173. IPI00828052.
RefSeq	NP_001005290.1. NM_001005290.3. NP_001027462.1. NM_001032291.2. NP_116025.1. NM_032636.7.
UniGene	Hs.405925.
3D structure databases
ProteinModelPortal	Q6PGN9.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000358925.
PTM databases
PhosphoSite	Q6PGN9.
Polymorphism databases
DMDM	74737651.
Proteomic databases
PaxDb	Q6PGN9.
PRIDE	Q6PGN9.
Protocols and materials databases
DNASU	84722.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369903; ENSP00000358919; ENSG00000134222. ENST00000369904; ENSP00000358920; ENSG00000134222. ENST00000369907; ENSP00000358923; ENSG00000134222. ENST00000369909; ENSP00000358925; ENSG00000134222. ENST00000409267; ENSP00000386323; ENSG00000134222. ENST00000438534; ENSP00000413591; ENSG00000134222.
GeneID	84722.
KEGG	hsa:84722.
UCSC	uc001dxb.3. human. uc001dxc.3. human. uc001dxf.3. human. uc001dxj.3. human.
Organism-specific databases
CTD	84722.
GeneCards	GC01M109822.
HGNC	HGNC:24472. PSRC1.
HPA	HPA049315.
MIM	613126. gene.
neXtProt	NX_Q6PGN9.
PharmGKB	PA142671120.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG39428.
HOGENOM	HOG000231348.
HOVERGEN	HBG080237.
InParanoid	Q6PGN9.
OMA	KRESPTC.
Gene expression databases
ArrayExpress	Q6PGN9.
Bgee	Q6PGN9.
CleanEx	HS_PSRC1.
Genevestigator	Q6PGN9.
Family and domain databases
InterPro	IPR026658. DDA3. IPR026657. DDA3/GTSE-1. [Graphical view]
PANTHER	PTHR21584. PTHR21584. 1 hit. PTHR21584:SF1. PTHR21584:SF1. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PSRC1. human.
GenomeRNAi	84722.
NextBio	74828.
SOURCE	Search...

Entry information

Entry name

PSRC1_HUMAN

Accession

Primary (citable) accession number: Q6PGN9
Secondary accession number(s): Q5T2Z3 , Q6ZTI8, Q71MG3, Q9BV77

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.