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Protein

Synaptopodin-2

Gene

SYNPO2

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

Functioni

Has an actin-binding and actin-bundling activity.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptopodin-2
Alternative name(s):
Genethonin-2
Myopodin
Gene namesi
Name:SYNPO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:17732. SYNPO2.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Shuttles between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. Localizes to the Z-disk in mature striated muscle. The nuclear export is XPO1-dependent (By similarity). Localized in a fiber-like pattern. partly overlapping with filamentous actin.By similarity1 Publication

GO - Cellular componenti

  • actin cytoskeleton Source: LIFEdb
  • focal adhesion Source: UniProtKB
  • nucleus Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38244.

Polymorphism and mutation databases

BioMutaiSYNPO2.
DMDMi51702160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10931093Synaptopodin-2PRO_0000187673Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei274 – 2741PhosphoserineCombined sources
Modified residuei310 – 3101PhosphoserineBy similarity
Modified residuei549 – 5491PhosphoserineBy similarity
Modified residuei551 – 5511PhosphoserineBy similarity
Modified residuei604 – 6041PhosphoserineBy similarity
Modified residuei610 – 6101PhosphothreonineCombined sources
Modified residuei611 – 6111PhosphoserineCombined sources
Modified residuei622 – 6221PhosphotyrosineCombined sources
Modified residuei626 – 6261PhosphothreonineCombined sources
Modified residuei729 – 7291PhosphoserineCombined sources
Modified residuei755 – 7551PhosphothreonineCombined sources
Modified residuei774 – 7741PhosphothreonineCombined sources
Modified residuei777 – 7771PhosphoserineCombined sources
Modified residuei781 – 7811PhosphoserineBy similarity
Modified residuei902 – 9021PhosphoserineCombined sources
Modified residuei906 – 9061PhosphoserineCombined sources
Modified residuei1056 – 10561PhosphoserineCombined sources
Isoform 4 (identifier: Q9UMS6-4)
Modified residuei1107 – 11071PhosphoserineCombined sources
Isoform 2 (identifier: Q9UMS6-2)
Modified residuei1138 – 11381PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UMS6.
MaxQBiQ9UMS6.
PaxDbiQ9UMS6.
PeptideAtlasiQ9UMS6.
PRIDEiQ9UMS6.

PTM databases

iPTMnetiQ9UMS6.
PhosphoSiteiQ9UMS6.

Expressioni

Tissue specificityi

Skeletal muscle specific.1 Publication

Inductioni

Down-regulated in muscle cell lines derived from patients with Duchenne muscular dystrophy (DMD).1 Publication

Gene expression databases

BgeeiQ9UMS6.
CleanExiHS_SYNPO2.
ExpressionAtlasiQ9UMS6. baseline and differential.
GenevisibleiQ9UMS6. HS.

Organism-specific databases

HPAiHPA030665.

Interactioni

Subunit structurei

Interacts with actin.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ILKQ134186EBI-3453434,EBI-747644

GO - Molecular functioni

Protein-protein interaction databases

BioGridi128105. 20 interactions.
DIPiDIP-47311N.
IntActiQ9UMS6. 7 interactions.
MINTiMINT-4541802.
STRINGi9606.ENSP00000306015.

Structurei

3D structure databases

ProteinModelPortaliQ9UMS6.
SMRiQ9UMS6. Positions 9-88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8883PDZPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi400 – 4056Poly-Arg
Compositional biasi423 – 4264Poly-Glu
Compositional biasi591 – 65868Pro-richAdd
BLAST
Compositional biasi756 – 81863Pro-richAdd
BLAST
Compositional biasi767 – 7704Poly-Ser

Sequence similaritiesi

Belongs to the synaptopodin family.Curated
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IIQE. Eukaryota.
ENOG410ZJ02. LUCA.
GeneTreeiENSGT00530000063754.
HOGENOMiHOG000261625.
HOVERGENiHBG079226.
InParanoidiQ9UMS6.
OMAiYNPHPRG.
OrthoDBiEOG7NGQDS.
PhylomeDBiQ9UMS6.
TreeFamiTF330867.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UMS6-1) [UniParc]FASTAAdd to basket

Also known as: Myo1

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
MGTGDFICIS MTGGAPWGFR LQGGKEQKQP LQVAKIRNQS KASGSGLCEG
60 70 80 90 100
DEVVSINGNP CADLTYPEVI KLMESITDSL QMLIKRPSSG ISEALISENE
110 120 130 140 150
NKNLEHLTHG GYVESTTLQI RPATKTQCTE FFLAPVKTEV PLAENQRSGP
160 170 180 190 200
DCAGSLKEET GPSYQRAPQM PDSQRGRVAE ELILREKVEA VQPGPVVELQ
210 220 230 240 250
LSLSQERHKG ASGPLVALPG AEKSKSPDPD PNLSHDRIVH INSIPTNEKA
260 270 280 290 300
DPFLRSSKII QISSGRELRV IQESEAGDAG LPRVEVILDC SDRQKTEGCR
310 320 330 340 350
LQAGKECVDS PVEGGQSEAP PSLVSFAVSS EGTEQGEDPR SEKDHSRPHK
360 370 380 390 400
HRARHARLRR SESLSEKQVK EAKSKCKSIA LLLTDAPNPN SKGVLMFKKR
410 420 430 440 450
RRRARKYTLV SYGTGELERE ADEEEEGDKE DTCEVAFLGA SESEVDEELL
460 470 480 490 500
SDVDDNTQVV NFDWDSGLVD IEKKLNRGDK MEMLPDTTGK GALMFAKRRE
510 520 530 540 550
RMDQITAQKE EDKVGGTPSR EQDAAQTDGL RTTTSYQRKE EESVRTQSSV
560 570 580 590 600
SKSYIEVSHG LGHVPQQNGF SGTSETANIQ RMVPMNRTAK PFPGSVNQPA
610 620 630 640 650
TPFSPTRNMT SPIADFPAPP PYSAVTPPPD AFSRGVSSPI AGPAQPPPWP
660 670 680 690 700
QPAPWSQPAF YDSSERIASR DERISVPAKR TGILQEAKRR STTKPMFTFK
710 720 730 740 750
EPKVSPNPEL LSLLQNSEGK RGTGAGGDSG PEEDYLSLGA EACNFMQSSS
760 770 780 790 800
AKQKTPPPVA PKPAVKSSSS QPVTPVSPVW SPGVAPTQPP AFPTSNPSKG
810 820 830 840 850
TVVSSIKIAQ PSYPPARPAS TLNVAGPFKG PQAAVASQNY TPKPTVSTPT
860 870 880 890 900
VNAVQPGAVG PSNELPGMSG RGAQLFAKRQ SRMEKYVVDS DTVQAHAARA
910 920 930 940 950
QSPTPSLPAS WKYSSNVRAP PPVAYNPIHS PSYPLAALKS QPSAAQPSKM
960 970 980 990 1000
GKKKGKKPLN ALDVMKHQPY QLNASLFTFQ PPDAKDGLPQ KSSVKVNSAL
1010 1020 1030 1040 1050
AMKQALPPRP VNAASPTNVQ ASSVYSVPAY TSPPSFFAEA SSPVSASPVP
1060 1070 1080 1090
VGIPTSPKQE SASSSYFVAP RPKFSAKKSG VTIQVWKPSV VEE
Length:1,093
Mass (Da):117,514
Last modified:August 31, 2004 - v2
Checksum:i8DF6F4D2823B444D
GO
Isoform 2 (identifier: Q9UMS6-2) [UniParc]FASTAAdd to basket

Also known as: Myo3

The sequence of this isoform differs from the canonical sequence as follows:
     1085-1093: VWKPSVVEE → ESGRSLSLPG...PHPRGWRRQT

Show »
Length:1,261
Mass (Da):136,342
Checksum:iE38B72200E742404
GO
Isoform 3 (identifier: Q9UMS6-3) [UniParc]FASTAAdd to basket

Also known as: Myo2

The sequence of this isoform differs from the canonical sequence as follows:
     1086-1093: WKPSVVEE → KCKSGIHSQDIIRTYFPAYLSSST

Show »
Length:1,109
Mass (Da):119,244
Checksum:i1AECA76771126803
GO
Isoform 4 (identifier: Q9UMS6-4) [UniParc]FASTAAdd to basket

Also known as: Myo4

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MGTGDFICISMTGGAPWGFRLQGGKEQKQPLQVAK → MVTQ
     1085-1093: VWKPSVVEE → ESGRSLSLPG...PHPRGWRRQT

Show »
Length:1,230
Mass (Da):133,081
Checksum:iC54DF3CE60B6BAEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611C → R in AL832031 (PubMed:17974005).Curated
Sequence conflicti147 – 1471Missing in AL832031 (PubMed:17974005).Curated
Sequence conflicti263 – 2664SSGR → IRHE in CAB51856 (PubMed:11673475).Curated
Sequence conflicti508 – 5081Q → P in AGS94404 (PubMed:22915763).Curated
Sequence conflicti667 – 6671I → M in AL832031 (PubMed:17974005).Curated
Sequence conflicti969 – 9691P → L in AAI50630 (PubMed:15489334).Curated
Sequence conflicti987 – 9871G → V in AAI50630 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541G → A.1 Publication
Corresponds to variant rs12645298 [ dbSNP | Ensembl ].
VAR_057256
Natural varianti174 – 1741Q → H.
Corresponds to variant rs17263971 [ dbSNP | Ensembl ].
VAR_057257
Natural varianti179 – 1791A → T.
Corresponds to variant rs17050152 [ dbSNP | Ensembl ].
VAR_057258
Natural varianti573 – 5731T → A.5 Publications
Corresponds to variant rs7698598 [ dbSNP | Ensembl ].
VAR_019670

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535MGTGD…LQVAK → MVTQ in isoform 4. 1 PublicationVSP_053771Add
BLAST
Alternative sequencei1085 – 10939VWKPSVVEE → ESGRSLSLPGRSVPPPISTS PWVYQPTYSYSSKPTDGLEK ANKRPTPWEAAAKSPLGLVD DAFQPRNIQESIVANVVSAA RRKVLPGPPEDWNERLSYIP QTQKAYMGSCGRQEYNVTAN NNMSTTSQYGSQLPYAYYRQ ASRNDSAIMSMETRSDYCLP VADYNYNPHPRGWRRQT in isoform 2 and isoform 4. 2 PublicationsVSP_041222
Alternative sequencei1086 – 10938WKPSVVEE → KCKSGIHSQDIIRTYFPAYL SSST in isoform 3. 1 PublicationVSP_041223

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU481975 mRNA. Translation: ACC93875.1.
KF147165 mRNA. Translation: AGS94404.1.
AL832031 mRNA. No translation available.
AL833294 mRNA. No translation available.
AC096745 Genomic DNA. No translation available.
AC107048 Genomic DNA. No translation available.
AC108030 Genomic DNA. No translation available.
BC150629 mRNA. Translation: AAI50630.1.
AJ010482 mRNA. Translation: CAB51856.1.
AF177291 mRNA. Translation: AAD55264.1.
CCDSiCCDS34054.1. [Q9UMS6-2]
CCDS47128.1. [Q9UMS6-3]
CCDS47129.1. [Q9UMS6-1]
CCDS75185.1. [Q9UMS6-4]
RefSeqiNP_001122405.1. NM_001128933.2. [Q9UMS6-1]
NP_001122406.1. NM_001128934.2. [Q9UMS6-3]
NP_001273683.1. NM_001286754.1. [Q9UMS6-4]
NP_597734.2. NM_133477.2. [Q9UMS6-2]
UniGeneiHs.655519.

Genome annotation databases

EnsembliENST00000307142; ENSP00000306015; ENSG00000172403. [Q9UMS6-2]
ENST00000429713; ENSP00000395143; ENSG00000172403. [Q9UMS6-1]
ENST00000434046; ENSP00000390965; ENSG00000172403. [Q9UMS6-3]
ENST00000610556; ENSP00000484885; ENSG00000172403. [Q9UMS6-4]
GeneIDi171024.
KEGGihsa:171024.
UCSCiuc003icm.6. human. [Q9UMS6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU481975 mRNA. Translation: ACC93875.1.
KF147165 mRNA. Translation: AGS94404.1.
AL832031 mRNA. No translation available.
AL833294 mRNA. No translation available.
AC096745 Genomic DNA. No translation available.
AC107048 Genomic DNA. No translation available.
AC108030 Genomic DNA. No translation available.
BC150629 mRNA. Translation: AAI50630.1.
AJ010482 mRNA. Translation: CAB51856.1.
AF177291 mRNA. Translation: AAD55264.1.
CCDSiCCDS34054.1. [Q9UMS6-2]
CCDS47128.1. [Q9UMS6-3]
CCDS47129.1. [Q9UMS6-1]
CCDS75185.1. [Q9UMS6-4]
RefSeqiNP_001122405.1. NM_001128933.2. [Q9UMS6-1]
NP_001122406.1. NM_001128934.2. [Q9UMS6-3]
NP_001273683.1. NM_001286754.1. [Q9UMS6-4]
NP_597734.2. NM_133477.2. [Q9UMS6-2]
UniGeneiHs.655519.

3D structure databases

ProteinModelPortaliQ9UMS6.
SMRiQ9UMS6. Positions 9-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128105. 20 interactions.
DIPiDIP-47311N.
IntActiQ9UMS6. 7 interactions.
MINTiMINT-4541802.
STRINGi9606.ENSP00000306015.

PTM databases

iPTMnetiQ9UMS6.
PhosphoSiteiQ9UMS6.

Polymorphism and mutation databases

BioMutaiSYNPO2.
DMDMi51702160.

Proteomic databases

EPDiQ9UMS6.
MaxQBiQ9UMS6.
PaxDbiQ9UMS6.
PeptideAtlasiQ9UMS6.
PRIDEiQ9UMS6.

Protocols and materials databases

DNASUi171024.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307142; ENSP00000306015; ENSG00000172403. [Q9UMS6-2]
ENST00000429713; ENSP00000395143; ENSG00000172403. [Q9UMS6-1]
ENST00000434046; ENSP00000390965; ENSG00000172403. [Q9UMS6-3]
ENST00000610556; ENSP00000484885; ENSG00000172403. [Q9UMS6-4]
GeneIDi171024.
KEGGihsa:171024.
UCSCiuc003icm.6. human. [Q9UMS6-1]

Organism-specific databases

CTDi171024.
GeneCardsiSYNPO2.
HGNCiHGNC:17732. SYNPO2.
HPAiHPA030665.
neXtProtiNX_Q9UMS6.
PharmGKBiPA38244.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIQE. Eukaryota.
ENOG410ZJ02. LUCA.
GeneTreeiENSGT00530000063754.
HOGENOMiHOG000261625.
HOVERGENiHBG079226.
InParanoidiQ9UMS6.
OMAiYNPHPRG.
OrthoDBiEOG7NGQDS.
PhylomeDBiQ9UMS6.
TreeFamiTF330867.

Miscellaneous databases

ChiTaRSiSYNPO2. human.
GeneWikiiSYNPO2.
GenomeRNAii171024.
PROiQ9UMS6.

Gene expression databases

BgeeiQ9UMS6.
CleanExiHS_SYNPO2.
ExpressionAtlasiQ9UMS6. baseline and differential.
GenevisibleiQ9UMS6. HS.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple isoforms of the tumor suppressor myopodin are simultaneously transcribed in cancer cells."
    De Ganck A., De Corte V., Staes A., Gevaert K., Vandekerckhove J., Gettemans J.
    Biochem. Biophys. Res. Commun. 370:269-273(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, VARIANT ALA-573.
  2. "Myopodin isoforms alter the chemokinetic response of PC3 cells in response to different migration stimuli via differential effects on Rho-ROCK signaling pathways."
    Kai F., Tanner K., King C., Duncan R.
    Carcinogenesis 33:2100-2107(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT ALA-573.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ALA-154 AND ALA-573.
    Tissue: Skeletal muscle.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2), VARIANT ALA-573.
  6. "Differentiation and stress-dependent nuclear-cytoplasmic redistribution of myopodin, a novel actin bundling protein."
    Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P.
    J. Cell Biol. 155:393-404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 263-1093 (ISOFORM 1), VARIANT ALA-573.
  7. "Identification of altered gene expression in skeletal muscles from Duchenne muscular dystrophy patients."
    Tkatchenko A.V., Pietu G., Cros N., Gannoun-Zaki L., Auffray C., Leger J.J., Dechesne C.A.
    Neuromuscul. Disord. 11:269-277(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 961-1093 (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; THR-610; SER-611; TYR-622; THR-626; SER-729; THR-755; THR-774; SER-777; SER-902; SER-906 AND SER-1056, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSYNP2_HUMAN
AccessioniPrimary (citable) accession number: Q9UMS6
Secondary accession number(s): B2RWP6
, B2Y8J9, Q9UK89, S5XAM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 6, 2016
This is version 130 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.