Q8N3V7 (SYNPO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Synaptopodin

Gene names

Name:	SYNPO
Synonyms:	KIAA1029

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	929 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin-associated protein that may play a role in modulating actin-based shape and motility of dendritic spines and renal podocyte foot processes. Seems to be essential for the formation of spine apparatuses in spines of telencephalic neurons, which is involved in synaptic plasticity By similarity.
Subunit structure	Interacts with BAIAP1. Interacts with actin By similarity. Interacts (via PPxY motifs) with WWC1 (via WW domains). Ref.8 Ref.11
Subcellular location	Cytoplasm › cytoskeleton By similarity. Cell junction › tight junction By similarity. Perikaryon By similarity. Cell projection › dendritic spine By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Cell junction › synapse By similarity. Note: Localized at the tight junction of cells. In brain, localized to the postsynaptic densities and in the perikarya. Associated with dendritic spines of a subset of synapses By similarity. Ref.8
Tissue specificity	Expressed in cerebral cortex. Ref.1
Post-translational modification	O-glycosylated By similarity. Isoform 2 is phosphorylated on Ser-826, Thr-836, Ser-840 and Ser-871.
Sequence similarities	Belongs to the synaptopodin family.
Sequence caution	The sequence BAA82981.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Postsynaptic cell membrane Synapse Tight junction
Coding sequence diversity	Alternative splicing
Ligand	Actin-binding
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of actin filament bundle assembly Inferred from electronic annotation. Source: Compara regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara
Cellular_component	actin cytoskeleton Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW dendritic spine Traceable author statement PubMed 15841212. Source: UniProtKB perikaryon Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW stress fiber Inferred from electronic annotation. Source: Compara tight junction Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N3V7-1)

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: Q8N3V7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.
     921-929: VWKPSFCFK → DRRESLPTSP...SLPAEASCTT

Note: Contains a phosphoserine at position 871. Contains a phosphoserine at position 826. Contains a phosphoserine at position 894. Contains a phosphoserine at position 854.

Isoform 3 (identifier: Q8N3V7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 929	929	Synaptopodin		PRO_0000187670
Regions
	Motif	562 – 565	4	PPxY motif
	Motif	581 – 584	4	PPxY motif
	Compositional bias	753 – 908	156	Pro-rich
Amino acid modifications
	Modified residue	263	1	Phosphoserine Ref.13 Ref.15
	Modified residue	501	1	Phosphoserine By similarity
	Modified residue	525	1	Phosphoserine Ref.13
	Modified residue	548	1	Phosphoserine By similarity
	Modified residue	580	1	Phosphoserine Ref.13 Ref.15
	Modified residue	685	1	Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
	Modified residue	702	1	Phosphoserine Ref.13
	Modified residue	746	1	Phosphothreonine Ref.13 Ref.15
	Modified residue	754	1	Phosphoserine Ref.13
	Modified residue	833	1	Phosphoserine Ref.13 Ref.15
	Modified residue	882	1	Phosphoserine By similarity
	Glycosylation	330	1	N-linked (GlcNAc...) Ref.14
Natural variations
	Alternative sequence	1 – 244	244	Missing in isoform 2 and isoform 3.		VSP_010476
	Alternative sequence	921 – 929	9	VWKPSFCFK → DRRESLPTSPPWTPGASRPP SSLDGWVSPGPWEPGRGSSM SSPPPLPPPPPMSPSWSERS VSPLRPETEARPPSRQLQAL LARNIINAARRKSASPRSAG AENPRPFSPPRAPPPPPPPP PPPPRMRSPQPARPGSAAVP GAAFAPIPRSPLPAGPSSCT SPRSPLPAPPRPFLYRRSPT DSDVSLDSEDSGAKSPGILG YNICPRGWNGSLRLKRGSLP AEASCTT in isoform 2.		VSP_010477
Experimental info
	Sequence conflict	95	1	Q → R in CAD38532. Ref.5
	Sequence conflict	417	1	E → G Ref.4
	Sequence conflict	428	1	A → V in CAA71955. Ref.1
	Sequence conflict	744	1	S → G in CAA71955. Ref.1
	Sequence conflict	836	1	K → R Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: 38723B6FDD046F15	FASTA	929	99,463
	10 20 30 40 50 60 MLGPHLPPPP LAPSEGRPTP CAFQIPDGSY RCLALEAEES SGEEGLQGEV GPTDLEEDEG 70 80 90 100 110 120 VSRSGDDSAC RVTQGTPQLP KALGIQPPSC SREEQGASQH DDRASQDWDV VKAGQMMTAS 130 140 150 160 170 180 PSPGPGPRVA QKPALGRSTS LTEKDLKEAK ARSQQIAAQL TTPPSSNSRG VQLFNRRRQR 190 200 210 220 230 240 VNEFTLESHG QRGQKPSQES LRVLPSSLPG HAPGLSLSST SLPEPGPPRH PSPQSPDRGV 250 260 270 280 290 300 PGHSMEGYSE EASLLRHLEK VASEEEEVPL VVYLKENAAL LTANGLHLSQ NREAQQSSPA 310 320 330 340 350 360 PPPAEVHSPA ADVNQNLASP SATLTTPTSN SSHNPPATDV NQNPPATVVP QSLPLSSIQQ 370 380 390 400 410 420 NSSEAQLPSN GTGPASKPST LCADGQPQAP AEEVRCSTLL IDKVSTPATT TSTFSREATL 430 440 450 460 470 480 IPSSRPPASD FMSSSLLIDI QPNTLVVSAD QEMSGRAAAT TPTKVYSEVH FTLAKPPSVV 490 500 510 520 530 540 NRTARPFGIQ APGGTSQMER SPMLERRHFG EKAPAPQPPS LPDRSPRPQR HIMSRSPMVE 550 560 570 580 590 600 RRMMGQRSPA SERRPLGNFT APPTYTETLS TAPLASWVRS PPSYSVLYPS SDPKSSHLKG 610 620 630 640 650 660 QAVPASKTGI LEESMARRGS RKSMFTFVEK PKVTPNPDLL DLVQTADEKR RQRDQGEVGV 670 680 690 700 710 720 EEEPFALGAE ASNFQQEPAP RDRASPAAAE EVVPEWASCL KSPRIQAKPK PKPNQNLSEA 730 740 750 760 770 780 SGKGAELYAR RQSRMEKYVI ESSSHTPELA RCPSPTMSLP SSWKYPTNAP GAFRVASRSP 790 800 810 820 830 840 ARTPPASLYH GYLPENGVLR PEPTKQPPYQ LRPSLFVLSP IKEPAKVSPR AASPAKPSSL 850 860 870 880 890 900 DLVPNLPKGA LPPSPALPRP SRSSPGLYTS PGQDSLQPTA VSPPYGGDIS PVSPSRAWSP 910 920 RAKQAPRPSF STRNAGIEAQ VWKPSFCFK
	Isoform 2 [UniParc]. Checksum: 5F0C0A39635750E4	FASTA	903	96,397
	10 20 30 40 50 60 MEGYSEEASL LRHLEKVASE EEEVPLVVYL KENAALLTAN GLHLSQNREA QQSSPAPPPA 70 80 90 100 110 120 EVHSPAADVN QNLASPSATL TTPTSNSSHN PPATDVNQNP PATVVPQSLP LSSIQQNSSE 130 140 150 160 170 180 AQLPSNGTGP ASKPSTLCAD GQPQAPAEEV RCSTLLIDKV STPATTTSTF SREATLIPSS 190 200 210 220 230 240 RPPASDFMSS SLLIDIQPNT LVVSADQEMS GRAAATTPTK VYSEVHFTLA KPPSVVNRTA 250 260 270 280 290 300 RPFGIQAPGG TSQMERSPML ERRHFGEKAP APQPPSLPDR SPRPQRHIMS RSPMVERRMM 310 320 330 340 350 360 GQRSPASERR PLGNFTAPPT YTETLSTAPL ASWVRSPPSY SVLYPSSDPK SSHLKGQAVP 370 380 390 400 410 420 ASKTGILEES MARRGSRKSM FTFVEKPKVT PNPDLLDLVQ TADEKRRQRD QGEVGVEEEP 430 440 450 460 470 480 FALGAEASNF QQEPAPRDRA SPAAAEEVVP EWASCLKSPR IQAKPKPKPN QNLSEASGKG 490 500 510 520 530 540 AELYARRQSR MEKYVIESSS HTPELARCPS PTMSLPSSWK YPTNAPGAFR VASRSPARTP 550 560 570 580 590 600 PASLYHGYLP ENGVLRPEPT KQPPYQLRPS LFVLSPIKEP AKVSPRAASP AKPSSLDLVP 610 620 630 640 650 660 NLPKGALPPS PALPRPSRSS PGLYTSPGQD SLQPTAVSPP YGGDISPVSP SRAWSPRAKQ 670 680 690 700 710 720 APRPSFSTRN AGIEAQDRRE SLPTSPPWTP GASRPPSSLD GWVSPGPWEP GRGSSMSSPP 730 740 750 760 770 780 PLPPPPPMSP SWSERSVSPL RPETEARPPS RQLQALLARN IINAARRKSA SPRSAGAENP 790 800 810 820 830 840 RPFSPPRAPP PPPPPPPPPP RMRSPQPARP GSAAVPGAAF APIPRSPLPA GPSSCTSPRS 850 860 870 880 890 900 PLPAPPRPFL YRRSPTDSDV SLDSEDSGAK SPGILGYNIC PRGWNGSLRL KRGSLPAEAS CTT
	Isoform 3 [UniParc]. Checksum: BE102B27B2C0BCC8	FASTA	685	73,667
	10 20 30 40 50 60 MEGYSEEASL LRHLEKVASE EEEVPLVVYL KENAALLTAN GLHLSQNREA QQSSPAPPPA 70 80 90 100 110 120 EVHSPAADVN QNLASPSATL TTPTSNSSHN PPATDVNQNP PATVVPQSLP LSSIQQNSSE 130 140 150 160 170 180 AQLPSNGTGP ASKPSTLCAD GQPQAPAEEV RCSTLLIDKV STPATTTSTF SREATLIPSS 190 200 210 220 230 240 RPPASDFMSS SLLIDIQPNT LVVSADQEMS GRAAATTPTK VYSEVHFTLA KPPSVVNRTA 250 260 270 280 290 300 RPFGIQAPGG TSQMERSPML ERRHFGEKAP APQPPSLPDR SPRPQRHIMS RSPMVERRMM 310 320 330 340 350 360 GQRSPASERR PLGNFTAPPT YTETLSTAPL ASWVRSPPSY SVLYPSSDPK SSHLKGQAVP 370 380 390 400 410 420 ASKTGILEES MARRGSRKSM FTFVEKPKVT PNPDLLDLVQ TADEKRRQRD QGEVGVEEEP 430 440 450 460 470 480 FALGAEASNF QQEPAPRDRA SPAAAEEVVP EWASCLKSPR IQAKPKPKPN QNLSEASGKG 490 500 510 520 530 540 AELYARRQSR MEKYVIESSS HTPELARCPS PTMSLPSSWK YPTNAPGAFR VASRSPARTP 550 560 570 580 590 600 PASLYHGYLP ENGVLRPEPT KQPPYQLRPS LFVLSPIKEP AKVSPRAASP AKPSSLDLVP 610 620 630 640 650 660 NLPKGALPPS PALPRPSRSS PGLYTSPGQD SLQPTAVSPP YGGDISPVSP SRAWSPRAKQ 670 680 APRPSFSTRN AGIEAQVWKP SFCFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Synaptopodin: an actin-associated protein in telencephalic dendrites and renal podocytes." Mundel P., Heid H.W., Mundel T.M., Krueger M., Reiser J., Kriz W. J. Cell Biol. 139:193-204(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY. Tissue: Brain.
[2]	"Loss of spine apparatus associated protein synaptopodin in Alzheimer's disease." Reddy P.H., Gutala R. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain and Kidney.
[3]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"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 AND 3). Tissue: Thalamus.
[5]	"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: Skeletal muscle.
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 3).
[8]	"Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1." Patrie K.M., Drescher A.J., Welihinda A., Mundel P., Margolis B. J. Biol. Chem. 277:30183-30190(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAIAP1, SUBCELLULAR LOCATION.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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-685, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"KIBRA modulates directional migration of podocytes." Duning K., Schurek E.M., Schlueter M., Bayer M., Reinhardt H.C., Schwab A., Schaefer L., Benzing T., Schermer B., Saleem M.A., Huber T.B., Bachmann S., Kremerskothen J., Weide T., Pavenstaedt H. J. Am. Soc. Nephrol. 19:1891-1903(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWC1.
[12]	"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-685, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-263; SER-525; SER-580; SER-685; SER-702; THR-746; SER-754 AND SER-833, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND SER-894 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-330, MASS SPECTROMETRY. Tissue: Liver.
[15]	"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-263; SER-580; SER-685; THR-746 AND SER-833, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854 AND SER-871 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11072 mRNA. Translation: CAA71955.1. AF499136 mRNA. Translation: AAQ07402.1. AF499137 mRNA. Translation: AAQ07403.1. AB028952 mRNA. Translation: BAA82981.2. Different initiation. AK127049 mRNA. No translation available. AK290178 mRNA. Translation: BAF82867.1. AL831818 mRNA. Translation: CAD38532.1. CH471062 Genomic DNA. Translation: EAW61715.1. CH471062 Genomic DNA. Translation: EAW61716.1. BC142683 mRNA. Translation: AAI42684.1. BC146665 mRNA. Translation: AAI46666.1.
IPI	IPI00027258. IPI00413058. IPI00413060.
RefSeq	NP_001103444.1. NM_001109974.2. NP_001159680.1. NM_001166208.1. NP_001159681.1. NM_001166209.1. NP_009217.3. NM_007286.5.
UniGene	Hs.435228.
3D structure databases
ProteinModelPortal	Q8N3V7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N3V7. 5 interactions.
STRING	9606.ENSP00000302139.
PTM databases
PhosphoSite	Q8N3V7.
Polymorphism databases
DMDM	48428650.
Proteomic databases
PaxDb	Q8N3V7.
PRIDE	Q8N3V7.
Protocols and materials databases
DNASU	11346.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307662; ENSP00000302139; ENSG00000171992. ENST00000394243; ENSP00000377789; ENSG00000171992. ENST00000519664; ENSP00000429268; ENSG00000171992. ENST00000522122; ENSP00000428378; ENSG00000171992.
GeneID	11346.
KEGG	hsa:11346.
UCSC	uc003lsn.3. human. uc003lsp.3. human.
Organism-specific databases
CTD	11346.
GeneCards	GC05P149960.
H-InvDB	HIX0164291.
HGNC	HGNC:30672. SYNPO.
HPA	HPA034631.
MIM	608155. gene.
neXtProt	NX_Q8N3V7.
PharmGKB	PA134863299.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG43259.
HOGENOM	HOG000132998.
HOVERGEN	HBG056954.
InParanoid	Q8N3V7.
OMA	YSTNAPG.
OrthoDB	EOG4933H7.
PhylomeDB	Q8N3V7.
Gene expression databases
ArrayExpress	Q8N3V7.
Bgee	Q8N3V7.
CleanEx	HS_SYNPO.
Genevestigator	Q8N3V7.
GermOnline	ENSG00000171992. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
ChiTaRS	SYNPO. human.
GenomeRNAi	11346.
NextBio	43120.
SOURCE	Search...

Entry information

Entry name

SYNPO_HUMAN

Accession

Primary (citable) accession number: Q8N3V7
Secondary accession number(s): A5PKZ8 , D3DQG8, O15271, Q9UPX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	April 3, 2013
This is version 99 of the entry and version 2 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.