Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8N3V7 (SYNPO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. 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:
Synaptopodin
Gene names
Name:SYNPO
Synonyms:KIAA1029
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length929 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytoskeleton By similarity. Cell junctiontight junction By similarity. Perikaryon By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity. Cell junctionsynapse 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929929Synaptopodin
PRO_0000187670

Regions

Motif562 – 5654PPxY motif
Motif581 – 5844PPxY motif
Compositional bias753 – 908156Pro-rich

Amino acid modifications

Modified residue2631Phosphoserine Ref.13 Ref.15
Modified residue5251Phosphoserine Ref.13
Modified residue5801Phosphoserine Ref.13 Ref.15
Modified residue6851Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
Modified residue7021Phosphoserine Ref.13
Modified residue7461Phosphothreonine Ref.13 Ref.15
Modified residue7541Phosphoserine Ref.13
Modified residue8331Phosphoserine Ref.13 Ref.15
Glycosylation3301N-linked (GlcNAc...) Ref.14

Natural variations

Alternative sequence1 – 244244Missing in isoform 2 and isoform 3.
VSP_010476
Alternative sequence921 – 9299VWKPSFCFK → DRRESLPTSPPWTPGASRPP SSLDGWVSPGPWEPGRGSSM SSPPPLPPPPPMSPSWSERS VSPLRPETEARPPSRQLQAL LARNIINAARRKSASPRSAG AENPRPFSPPRAPPPPPPPP PPPPRMRSPQPARPGSAAVP GAAFAPIPRSPLPAGPSSCT SPRSPLPAPPRPFLYRRSPT DSDVSLDSEDSGAKSPGILG YNICPRGWNGSLRLKRGSLP AEASCTT in isoform 2.
VSP_010477

Experimental info

Sequence conflict951Q → R in CAD38532. Ref.5
Sequence conflict4171E → G Ref.4
Sequence conflict4281A → V in CAA71955. Ref.1
Sequence conflict7441S → G in CAA71955. Ref.1
Sequence conflict8361K → R Ref.4

Sequences

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

Last modified June 7, 2004. Version 2.
Checksum: 38723B6FDD046F15

FASTA92999,463
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5F0C0A39635750E4
Show »

FASTA90396,397
Isoform 3 [UniParc].

Checksum: BE102B27B2C0BCC8
Show »

FASTA68573,667

References

« Hide '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. 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] (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. 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].
[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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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
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.
CCDSCCDS4308.1. [Q8N3V7-2]
CCDS54937.1. [Q8N3V7-1]
CCDS54938.1. [Q8N3V7-3]
RefSeqNP_001103444.1. NM_001109974.2. [Q8N3V7-3]
NP_001159680.1. NM_001166208.1. [Q8N3V7-1]
NP_001159681.1. NM_001166209.1. [Q8N3V7-1]
NP_009217.3. NM_007286.5. [Q8N3V7-2]
XP_005268426.1. XM_005268369.1. [Q8N3V7-2]
XP_005268427.1. XM_005268370.1. [Q8N3V7-2]
XP_005268428.1. XM_005268371.1. [Q8N3V7-2]
UniGeneHs.435228.

3D structure databases

ProteinModelPortalQ8N3V7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116474. 8 interactions.
IntActQ8N3V7. 5 interactions.
MINTMINT-4136464.
STRING9606.ENSP00000302139.

PTM databases

PhosphoSiteQ8N3V7.

Polymorphism databases

DMDM48428650.

Proteomic databases

MaxQBQ8N3V7.
PaxDbQ8N3V7.
PRIDEQ8N3V7.

Protocols and materials databases

DNASU11346.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307662; ENSP00000302139; ENSG00000171992. [Q8N3V7-2]
ENST00000394243; ENSP00000377789; ENSG00000171992. [Q8N3V7-1]
ENST00000519664; ENSP00000429268; ENSG00000171992. [Q8N3V7-3]
ENST00000522122; ENSP00000428378; ENSG00000171992. [Q8N3V7-1]
GeneID11346.
KEGGhsa:11346.
UCSCuc003lsn.3. human. [Q8N3V7-1]
uc003lsp.3. human. [Q8N3V7-2]

Organism-specific databases

CTD11346.
GeneCardsGC05P149960.
H-InvDBHIX0164291.
HGNCHGNC:30672. SYNPO.
HPAHPA034631.
MIM608155. gene.
neXtProtNX_Q8N3V7.
PharmGKBPA134863299.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43259.
HOGENOMHOG000132998.
HOVERGENHBG056954.
InParanoidQ8N3V7.
OMASWKYSTN.
OrthoDBEOG7GN2PF.
PhylomeDBQ8N3V7.
TreeFamTF330867.

Gene expression databases

ArrayExpressQ8N3V7.
BgeeQ8N3V7.
CleanExHS_SYNPO.
GenevestigatorQ8N3V7.

Family and domain databases

InterProIPR028753. Synpo.
[Graphical view]
PANTHERPTHR24217:SF11. PTHR24217:SF11. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSYNPO. human.
GeneWikiSYNPO.
GenomeRNAi11346.
NextBio43120.
PROQ8N3V7.
SOURCESearch...

Entry information

Entry nameSYNPO_HUMAN
AccessionPrimary (citable) accession number: Q8N3V7
Secondary accession number(s): A5PKZ8 expand/collapse secondary AC list , D3DQG8, O15271, Q9UPX1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 2 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 5

Human chromosome 5: entries, gene names and cross-references to MIM