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Q8N3V7

- SYNPO_HUMAN

UniProt

Q8N3V7 - SYNPO_HUMAN

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Protein

Synaptopodin

Gene

SYNPO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. actin binding Source: UniProtKB

GO - Biological processi

  1. positive regulation of actin filament bundle assembly Source: InterPro
  2. regulation of stress fiber assembly Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptopodin
Gene namesi
Name:SYNPO
Synonyms:KIAA1029
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:30672. SYNPO.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. dendritic spine Source: UniProtKB
  4. postsynaptic membrane Source: UniProtKB-KW
  5. stress fiber Source: Ensembl
  6. tight junction Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse, Tight junction

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134863299.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929SynaptopodinPRO_0000187670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei263 – 2631Phosphoserine2 Publications
Glycosylationi330 – 3301N-linked (GlcNAc...)1 Publication
Modified residuei525 – 5251Phosphoserine1 Publication
Modified residuei580 – 5801Phosphoserine2 Publications
Modified residuei685 – 6851Phosphoserine4 Publications
Modified residuei702 – 7021Phosphoserine1 Publication
Modified residuei746 – 7461Phosphothreonine2 Publications
Modified residuei754 – 7541Phosphoserine1 Publication
Modified residuei833 – 8331Phosphoserine2 Publications

Post-translational modificationi

O-glycosylated.By similarity
Isoform 2 is phosphorylated on Ser-826, Thr-836, Ser-840 and Ser-871.4 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8N3V7.
PaxDbiQ8N3V7.
PRIDEiQ8N3V7.

PTM databases

PhosphoSiteiQ8N3V7.

Expressioni

Tissue specificityi

Expressed in cerebral cortex.1 Publication

Gene expression databases

BgeeiQ8N3V7.
CleanExiHS_SYNPO.
ExpressionAtlasiQ8N3V7. baseline and differential.
GenevestigatoriQ8N3V7.

Organism-specific databases

HPAiHPA034631.

Interactioni

Subunit structurei

Interacts with BAIAP1. Interacts with actin (By similarity). Interacts (via PPxY motifs) with WWC1 (via WW domains).By similarity2 Publications

Protein-protein interaction databases

BioGridi116474. 8 interactions.
IntActiQ8N3V7. 5 interactions.
MINTiMINT-4136464.
STRINGi9606.ENSP00000302139.

Structurei

3D structure databases

ProteinModelPortaliQ8N3V7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi562 – 5654PPxY motif
Motifi581 – 5844PPxY motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi753 – 908156Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the synaptopodin family.Curated

Phylogenomic databases

eggNOGiNOG43259.
GeneTreeiENSGT00530000063754.
HOGENOMiHOG000132998.
HOVERGENiHBG056954.
InParanoidiQ8N3V7.
OMAiSWKYSTN.
OrthoDBiEOG7GN2PF.
PhylomeDBiQ8N3V7.
TreeFamiTF330867.

Family and domain databases

InterProiIPR028753. Synpo.
[Graphical view]
PANTHERiPTHR24217:SF11. PTHR24217:SF11. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8N3V7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLGPHLPPPP LAPSEGRPTP CAFQIPDGSY RCLALEAEES SGEEGLQGEV
60 70 80 90 100
GPTDLEEDEG VSRSGDDSAC RVTQGTPQLP KALGIQPPSC SREEQGASQH
110 120 130 140 150
DDRASQDWDV VKAGQMMTAS PSPGPGPRVA QKPALGRSTS LTEKDLKEAK
160 170 180 190 200
ARSQQIAAQL TTPPSSNSRG VQLFNRRRQR VNEFTLESHG QRGQKPSQES
210 220 230 240 250
LRVLPSSLPG HAPGLSLSST SLPEPGPPRH PSPQSPDRGV PGHSMEGYSE
260 270 280 290 300
EASLLRHLEK VASEEEEVPL VVYLKENAAL LTANGLHLSQ NREAQQSSPA
310 320 330 340 350
PPPAEVHSPA ADVNQNLASP SATLTTPTSN SSHNPPATDV NQNPPATVVP
360 370 380 390 400
QSLPLSSIQQ NSSEAQLPSN GTGPASKPST LCADGQPQAP AEEVRCSTLL
410 420 430 440 450
IDKVSTPATT TSTFSREATL IPSSRPPASD FMSSSLLIDI QPNTLVVSAD
460 470 480 490 500
QEMSGRAAAT TPTKVYSEVH FTLAKPPSVV NRTARPFGIQ APGGTSQMER
510 520 530 540 550
SPMLERRHFG EKAPAPQPPS LPDRSPRPQR HIMSRSPMVE RRMMGQRSPA
560 570 580 590 600
SERRPLGNFT APPTYTETLS TAPLASWVRS PPSYSVLYPS SDPKSSHLKG
610 620 630 640 650
QAVPASKTGI LEESMARRGS RKSMFTFVEK PKVTPNPDLL DLVQTADEKR
660 670 680 690 700
RQRDQGEVGV EEEPFALGAE ASNFQQEPAP RDRASPAAAE EVVPEWASCL
710 720 730 740 750
KSPRIQAKPK PKPNQNLSEA SGKGAELYAR RQSRMEKYVI ESSSHTPELA
760 770 780 790 800
RCPSPTMSLP SSWKYPTNAP GAFRVASRSP ARTPPASLYH GYLPENGVLR
810 820 830 840 850
PEPTKQPPYQ LRPSLFVLSP IKEPAKVSPR AASPAKPSSL DLVPNLPKGA
860 870 880 890 900
LPPSPALPRP SRSSPGLYTS PGQDSLQPTA VSPPYGGDIS PVSPSRAWSP
910 920
RAKQAPRPSF STRNAGIEAQ VWKPSFCFK
Length:929
Mass (Da):99,463
Last modified:June 7, 2004 - v2
Checksum:i38723B6FDD046F15
GO
Isoform 2 (identifier: Q8N3V7-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:903
Mass (Da):96,397
Checksum:i5F0C0A39635750E4
GO
Isoform 3 (identifier: Q8N3V7-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:685
Mass (Da):73,667
Checksum:iBE102B27B2C0BCC8
GO

Sequence cautioni

The sequence BAA82981.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951Q → R in CAD38532. (PubMed:17974005)Curated
Sequence conflicti417 – 4171E → G(PubMed:14702039)Curated
Sequence conflicti428 – 4281A → V in CAA71955. (PubMed:9314539)Curated
Sequence conflicti744 – 7441S → G in CAA71955. (PubMed:9314539)Curated
Sequence conflicti836 – 8361K → R(PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 244244Missing in isoform 2 and isoform 3. 5 PublicationsVSP_010476Add
BLAST
Alternative sequencei921 – 9299VWKPSFCFK → DRRESLPTSPPWTPGASRPP SSLDGWVSPGPWEPGRGSSM SSPPPLPPPPPMSPSWSERS VSPLRPETEARPPSRQLQAL LARNIINAARRKSASPRSAG AENPRPFSPPRAPPPPPPPP PPPPRMRSPQPARPGSAAVP GAAFAPIPRSPLPAGPSSCT SPRSPLPAPPRPFLYRRSPT DSDVSLDSEDSGAKSPGILG YNICPRGWNGSLRLKRGSLP AEASCTT in isoform 2. 2 PublicationsVSP_010477

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4308.1. [Q8N3V7-2]
CCDS54937.1. [Q8N3V7-1]
CCDS54938.1. [Q8N3V7-3]
RefSeqiNP_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]
UniGeneiHs.435228.

Genome annotation databases

EnsembliENST00000307662; ENSP00000302139; ENSG00000171992. [Q8N3V7-2]
ENST00000394243; ENSP00000377789; ENSG00000171992. [Q8N3V7-1]
ENST00000519664; ENSP00000429268; ENSG00000171992. [Q8N3V7-3]
ENST00000522122; ENSP00000428378; ENSG00000171992. [Q8N3V7-1]
GeneIDi11346.
KEGGihsa:11346.
UCSCiuc003lsn.3. human. [Q8N3V7-1]
uc003lsp.3. human. [Q8N3V7-2]

Polymorphism databases

DMDMi48428650.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4308.1. [Q8N3V7-2 ]
CCDS54937.1. [Q8N3V7-1 ]
CCDS54938.1. [Q8N3V7-3 ]
RefSeqi NP_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 ]
UniGenei Hs.435228.

3D structure databases

ProteinModelPortali Q8N3V7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116474. 8 interactions.
IntActi Q8N3V7. 5 interactions.
MINTi MINT-4136464.
STRINGi 9606.ENSP00000302139.

PTM databases

PhosphoSitei Q8N3V7.

Polymorphism databases

DMDMi 48428650.

Proteomic databases

MaxQBi Q8N3V7.
PaxDbi Q8N3V7.
PRIDEi Q8N3V7.

Protocols and materials databases

DNASUi 11346.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307662 ; ENSP00000302139 ; ENSG00000171992 . [Q8N3V7-2 ]
ENST00000394243 ; ENSP00000377789 ; ENSG00000171992 . [Q8N3V7-1 ]
ENST00000519664 ; ENSP00000429268 ; ENSG00000171992 . [Q8N3V7-3 ]
ENST00000522122 ; ENSP00000428378 ; ENSG00000171992 . [Q8N3V7-1 ]
GeneIDi 11346.
KEGGi hsa:11346.
UCSCi uc003lsn.3. human. [Q8N3V7-1 ]
uc003lsp.3. human. [Q8N3V7-2 ]

Organism-specific databases

CTDi 11346.
GeneCardsi GC05P149960.
H-InvDB HIX0164291.
HGNCi HGNC:30672. SYNPO.
HPAi HPA034631.
MIMi 608155. gene.
neXtProti NX_Q8N3V7.
PharmGKBi PA134863299.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43259.
GeneTreei ENSGT00530000063754.
HOGENOMi HOG000132998.
HOVERGENi HBG056954.
InParanoidi Q8N3V7.
OMAi SWKYSTN.
OrthoDBi EOG7GN2PF.
PhylomeDBi Q8N3V7.
TreeFami TF330867.

Miscellaneous databases

ChiTaRSi SYNPO. human.
GeneWikii SYNPO.
GenomeRNAii 11346.
NextBioi 43120.
PROi Q8N3V7.
SOURCEi Search...

Gene expression databases

Bgeei Q8N3V7.
CleanExi HS_SYNPO.
ExpressionAtlasi Q8N3V7. baseline and differential.
Genevestigatori Q8N3V7.

Family and domain databases

InterProi IPR028753. Synpo.
[Graphical view ]
PANTHERi PTHR24217:SF11. PTHR24217:SF11. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  6. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYNPO_HUMAN
AccessioniPrimary (citable) accession number: Q8N3V7
Secondary accession number(s): A5PKZ8
, D3DQG8, O15271, Q9UPX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: October 29, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3