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Q92797

- SYMPK_HUMAN

UniProt

Q92797 - SYMPK_HUMAN

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Protein

Symplekin

Gene

SYMPK

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

Functioni

Scaffold protein that functions as a component of a multimolecular complex involved in histone mRNA 3'-end processing. Specific component of the tight junction (TJ) plaque, but might not be an exclusively junctional component. May have a house-keeping rule. Is involved in pre-mRNA polyadenylation. Enhances SSU72 phosphatase activity.2 Publications

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. mRNA polyadenylation Source: UniProtKB
  3. positive regulation of protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, mRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Symplekin
Gene namesi
Name:SYMPK
Synonyms:SPK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:22935. SYMPK.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctiontight junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Nucleusnucleoplasm
Note: Cytoplasmic face of adhesion plaques (major) and nucleoplasm (minor) (in cells with TJ). Nucleoplasm (in cells without TJ). Nuclear bodies of heat-stressed cells.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: HPA
  5. plasma membrane Source: HPA
  6. tight junction Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi185 – 1851K → A: Abolishes stimulation of SSU72 phosphatase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134896920.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12741274SymplekinPRO_0000072385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei494 – 4941Phosphoserine1 Publication
Modified residuei1243 – 12431Phosphoserine2 Publications
Modified residuei1257 – 12571Phosphothreonine1 Publication
Modified residuei1259 – 12591Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92797.
PaxDbiQ92797.
PRIDEiQ92797.

PTM databases

PhosphoSiteiQ92797.

Expressioni

Tissue specificityi

In testis, expressed in polar epithelia and Sertoli cells but not in vascular endothelia. The protein is detected in stomach, duodenum, pancreas, liver, fetal brain, carcinomas, lens-forming cells, fibroblasts, lymphocytes, lymphoma cells, erythroleukemia cells but not in endothelium of vessels, epidermis, intercalated disks, Purkinje fiber cells of the heart and lymph node.1 Publication

Gene expression databases

BgeeiQ92797.
CleanExiHS_SYMPK.
ExpressionAtlasiQ92797. baseline and differential.
GenevestigatoriQ92797.

Organism-specific databases

HPAiHPA041756.
HPA055661.

Interactioni

Subunit structurei

Found in a heat-sensitive complex at least composed of several cleavage and polyadenylation specific and cleavage stimulation factors. Interacts with CPSF2, CPSF3 and CSTF2. Interacts with HSF1 in heat-stressed cells. Interacts with SSU72.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CPSF2Q9P2I02EBI-1051992,EBI-1043224

Protein-protein interaction databases

BioGridi113833. 24 interactions.
DIPiDIP-42506N.
IntActiQ92797. 5 interactions.
MINTiMINT-1537611.
STRINGi9606.ENSP00000245934.

Structurei

Secondary structure

1
1274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 4514Combined sources
Helixi50 – 6314Combined sources
Helixi67 – 737Combined sources
Helixi74 – 785Combined sources
Helixi79 – 824Combined sources
Helixi86 – 10217Combined sources
Helixi104 – 1063Combined sources
Helixi107 – 11812Combined sources
Helixi123 – 14624Combined sources
Helixi152 – 17019Combined sources
Helixi171 – 1733Combined sources
Helixi177 – 19317Combined sources
Helixi205 – 2073Combined sources
Helixi213 – 2153Combined sources
Beta strandi221 – 2233Combined sources
Helixi225 – 24218Combined sources
Helixi250 – 26617Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28313Combined sources
Helixi287 – 2893Combined sources
Helixi291 – 2933Combined sources
Helixi294 – 30916Combined sources
Helixi312 – 3176Combined sources
Helixi318 – 32710Combined sources
Helixi332 – 3376Combined sources
Helixi342 – 3454Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3O2QX-ray2.40A/D30-360[»]
3O2SX-ray2.50A30-360[»]
3O2TX-ray1.40A30-395[»]
3ODRX-ray2.20A1-395[»]
3ODSX-ray1.90A1-395[»]
4H3HX-ray2.20A/D30-360[»]
4H3KX-ray2.00A/D30-360[»]
ProteinModelPortaliQ92797.
SMRiQ92797. Positions 30-349.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92797.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati31 – 6434HEAT 1Add
BLAST
Repeati67 – 10135HEAT 2Add
BLAST
Repeati104 – 14643HEAT 3Add
BLAST
Repeati153 – 19240HEAT 4Add
BLAST
Repeati227 – 26640HEAT 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 124124Interaction with HSF1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi345 – 36016Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1168 – 11758Poly-Ser

Domaini

The HEAT repeats have been determined based on 3D-structure analysis of the D.melanogaster ortholog and are not detected by sequence-based prediction programs.

Sequence similaritiesi

Belongs to the Symplekin family.Curated
Contains 5 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG273943.
GeneTreeiENSGT00390000017045.
HOGENOMiHOG000046745.
HOVERGENiHBG062441.
InParanoidiQ92797.
KOiK06100.
OMAiEACKRDN.
OrthoDBiEOG7RZ5PC.
PhylomeDBiQ92797.
TreeFamiTF312860.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021850. Symplekin/Pta1.
IPR022075. Symplekin_C.
[Graphical view]
PANTHERiPTHR15245:SF20. PTHR15245:SF20. 1 hit.
PfamiPF12295. Symplekin_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q92797-1) [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
MASGSGDSVT RRSVASQFFT QEEGPGIDGM TTSERVVDLL NQAALITNDS
60 70 80 90 100
KITVLKQVQE LIINKDPTLL DNFLDEIIAF QADKSIEVRK FVIGFIEEAC
110 120 130 140 150
KRDIELLLKL IANLNMLLRD ENVNVVKKAI LTMTQLYKVA LQWMVKSRVI
160 170 180 190 200
SELQEACWDM VSAMAGDIIL LLDSDNDGIR THAIKFVEGL IVTLSPRMAD
210 220 230 240 250
SEIPRRQEHD ISLDRIPRDH PYIQYNVLWE EGKAALEQLL KFMVHPAISS
260 270 280 290 300
INLTTALGSL ANIARQRPMF MSEVIQAYET LHANLPPTLA KSQVSSVRKN
310 320 330 340 350
LKLHLLSVLK HPASLEFQAQ ITTLLVDLGT PQAEIARNMP SSKDTRKRPR
360 370 380 390 400
DDSDSTLKKM KLEPNLGEDD EDKDLEPGPS GTSKASAQIS GQSDTDITAE
410 420 430 440 450
FLQPLLTPDN VANLVLISMV YLPEAMPASF QAIYTPVESA GTEAQIKHLA
460 470 480 490 500
RLMATQMTAA GLGPGVEQTK QCKEEPKEEK VVKTESVLIK RRLSAQGQAI
510 520 530 540 550
SVVGSLSSMS PLEEEAPQAK RRPEPIIPVT QPRLAGAGGR KKIFRLSDVL
560 570 580 590 600
KPLTDAQVEA MKLGAVKRIL RAEKAVACSG AAQVRIKILA SLVTQFNSGL
610 620 630 640 650
KAEVLSFILE DVRARLDLAF AWLYQEYNAY LAAGASGSLD KYEDCLIRLL
660 670 680 690 700
SGLQEKPDQK DGIFTKVVLE APLITESALE VVRKYCEDES RTYLGMSTLR
710 720 730 740 750
DLIFKRPSRQ FQYLHVLLDL SSHEKDKVRS QALLFIKRMY EKEQLREYVE
760 770 780 790 800
KFALNYLQLL VHPNPPSVLF GADKDTEVAA PWTEETVKQC LYLYLALLPQ
810 820 830 840 850
NHKLIHELAA VYTEAIADIK RTVLRVIEQP IRGMGMNSPE LLLLVENCPK
860 870 880 890 900
GAETLVTRCL HSLTDKVPPS PELVKRVRDL YHKRLPDVRF LIPVLNGLEK
910 920 930 940 950
KEVIQALPKL IKLNPIVVKE VFNRLLGTQH GEGNSALSPL NPGELLIALH
960 970 980 990 1000
NIDSVKCDMK SIIKATNLCF AERNVYTSEV LAVVMQQLME QSPLPMLLMR
1010 1020 1030 1040 1050
TVIQSLTMYP RLGGFVMNIL SRLIMKQVWK YPKVWEGFIK CCQRTKPQSF
1060 1070 1080 1090 1100
QVILQLPPQQ LGAVFDKCPE LREPLLAHVR SFTPHQQAHI PNSIMTILEA
1110 1120 1130 1140 1150
SGKQEPEAKE APAGPLEEDD LEPLTLAPAP APRPPQDLIG LRLAQEKALK
1160 1170 1180 1190 1200
RQLEEEQKLK PGGVGAPSSS SPSPSPSARP GPPPSEEAMD FREEGPECET
1210 1220 1230 1240 1250
PGIFISMDDD SGLTEAALLD SSLEGPLPKE TAAGGLTLKE ERSPQTLAPV
1260 1270
GEDAMKTPSP AAEDAREPEA KGNS
Length:1,274
Mass (Da):141,148
Last modified:July 19, 2005 - v2
Checksum:iD8AD9ABB0B25A688
GO
Isoform 2 (identifier: Q92797-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     637-672: GSLDKYEDCLIRLLSGLQEKPDQKDGIFTKVVLEAP → PRLCWRRHSSQRVPWRWSASTARMRVAPIWACPHFET
     673-1274: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Show »
Length:673
Mass (Da):74,523
Checksum:iE5939FC7FFDAA3AA
GO

Sequence cautioni

The sequence AAC50667.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH30214.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAD92261.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA71861.1 differs from that shown. Reason: Frameshift at position 67. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei637 – 67236GSLDK…VLEAP → PRLCWRRHSSQRVPWRWSAS TARMRVAPIWACPHFET in isoform 2. 1 PublicationVSP_014842Add
BLAST
Alternative sequencei673 – 1274602Missing in isoform 2. 1 PublicationVSP_014843Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10931 mRNA. Translation: CAA71861.1. Frameshift.
AB209024 mRNA. Translation: BAD92261.1. Different initiation.
U88726 mRNA. Translation: AAB58578.1.
BC006536 mRNA. Translation: AAH06536.2.
BC006567 mRNA. Translation: AAH06567.2.
BC030214 mRNA. Translation: AAH30214.1. Sequence problems.
U49240 mRNA. Translation: AAC50667.1. Different initiation.
DB328640 mRNA. No translation available.
CCDSiCCDS12676.2. [Q92797-1]
RefSeqiNP_004810.2. NM_004819.2. [Q92797-1]
XP_005259343.1. XM_005259286.1. [Q92797-1]
UniGeneiHs.515475.

Genome annotation databases

EnsembliENST00000245934; ENSP00000245934; ENSG00000125755. [Q92797-1]
GeneIDi8189.
KEGGihsa:8189.
UCSCiuc002pdn.3. human. [Q92797-1]
uc002pdq.2. human. [Q92797-2]

Polymorphism databases

DMDMi71153180.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10931 mRNA. Translation: CAA71861.1 . Frameshift.
AB209024 mRNA. Translation: BAD92261.1 . Different initiation.
U88726 mRNA. Translation: AAB58578.1 .
BC006536 mRNA. Translation: AAH06536.2 .
BC006567 mRNA. Translation: AAH06567.2 .
BC030214 mRNA. Translation: AAH30214.1 . Sequence problems.
U49240 mRNA. Translation: AAC50667.1 . Different initiation.
DB328640 mRNA. No translation available.
CCDSi CCDS12676.2. [Q92797-1 ]
RefSeqi NP_004810.2. NM_004819.2. [Q92797-1 ]
XP_005259343.1. XM_005259286.1. [Q92797-1 ]
UniGenei Hs.515475.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3O2Q X-ray 2.40 A/D 30-360 [» ]
3O2S X-ray 2.50 A 30-360 [» ]
3O2T X-ray 1.40 A 30-395 [» ]
3ODR X-ray 2.20 A 1-395 [» ]
3ODS X-ray 1.90 A 1-395 [» ]
4H3H X-ray 2.20 A/D 30-360 [» ]
4H3K X-ray 2.00 A/D 30-360 [» ]
ProteinModelPortali Q92797.
SMRi Q92797. Positions 30-349.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113833. 24 interactions.
DIPi DIP-42506N.
IntActi Q92797. 5 interactions.
MINTi MINT-1537611.
STRINGi 9606.ENSP00000245934.

PTM databases

PhosphoSitei Q92797.

Polymorphism databases

DMDMi 71153180.

Proteomic databases

MaxQBi Q92797.
PaxDbi Q92797.
PRIDEi Q92797.

Protocols and materials databases

DNASUi 8189.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000245934 ; ENSP00000245934 ; ENSG00000125755 . [Q92797-1 ]
GeneIDi 8189.
KEGGi hsa:8189.
UCSCi uc002pdn.3. human. [Q92797-1 ]
uc002pdq.2. human. [Q92797-2 ]

Organism-specific databases

CTDi 8189.
GeneCardsi GC19M046318.
H-InvDB HIX0015243.
HGNCi HGNC:22935. SYMPK.
HPAi HPA041756.
HPA055661.
MIMi 602388. gene.
neXtProti NX_Q92797.
PharmGKBi PA134896920.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG273943.
GeneTreei ENSGT00390000017045.
HOGENOMi HOG000046745.
HOVERGENi HBG062441.
InParanoidi Q92797.
KOi K06100.
OMAi EACKRDN.
OrthoDBi EOG7RZ5PC.
PhylomeDBi Q92797.
TreeFami TF312860.

Miscellaneous databases

ChiTaRSi SYMPK. human.
EvolutionaryTracei Q92797.
GeneWikii SYMPK.
GenomeRNAii 8189.
NextBioi 30878.
PROi Q92797.
SOURCEi Search...

Gene expression databases

Bgeei Q92797.
CleanExi HS_SYMPK.
ExpressionAtlasi Q92797. baseline and differential.
Genevestigatori Q92797.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR021850. Symplekin/Pta1.
IPR022075. Symplekin_C.
[Graphical view ]
PANTHERi PTHR15245:SF20. PTHR15245:SF20. 1 hit.
Pfami PF12295. Symplekin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 3 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Six transcripts map within 200 kilobases of the myotonic dystrophy expanded repeat."
    Alwazzan M., Hamshere M.G., Lennon G.G., Brook J.D.
    Mamm. Genome 9:485-487(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Muscle.
  2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "Chromosomal localization to 19q13.3, partial genomic structure and 5' cDNA sequence of the human symplekin gene."
    Ueki K., Ramaswamy S., Billings S.J., Mohrenweiser H.W., Louis D.N.
    Somat. Cell Mol. Genet. 23:229-231(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-155 (ISOFORM 1).
  4. "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] OF 17-1274 (ISOFORM 1).
    Tissue: Kidney and Lung.
  5. "Symplekin, a novel type of tight junction plaque protein."
    Keon B.H., Schaefer S., Kuhn C., Grund C., Franke W.W.
    J. Cell Biol. 134:1003-1018(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 97-1274 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Colon carcinoma.
  6. "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] OF 426-533 (ISOFORM 1).
  7. "Complex protein interactions within the human polyadenylation machinery identify a novel component."
    Takagaki Y., Manley J.L.
    Mol. Cell. Biol. 20:1515-1525(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSTF2.
  8. "Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes."
    Hofmann I., Schnoelzer M., Kaufmann I., Franke W.W.
    Mol. Biol. Cell 13:1665-1676(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin."
    Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.
    J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSF1, SUBCELLULAR LOCATION.
  10. "Symplekin and multiple other polyadenylation factors participate in 3'-end maturation of histone mRNAs."
    Kolev N.G., Steitz J.A.
    Genes Dev. 19:2583-2592(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A HEAT-SENSITIVE COMPLEX.
  11. "Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation."
    Kolev N.G., Yario T.A., Benson E., Steitz J.A.
    EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CPSF2 AND CPSF3.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1243; THR-1257 AND SER-1259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-1243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure of the human symplekin-Ssu72-CTD phosphopeptide complex."
    Xiang K., Nagaike T., Xiang S., Kilic T., Beh M.M., Manley J.L., Tong L.
    Nature 467:729-733(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-395 IN COMPLEX WITH SSU72, FUNCTION, MUTAGENESIS OF LYS-185, INTERACTION WITH SSU72.
  17. "An unexpected binding mode for a Pol II CTD peptide phosphorylated at Ser7 in the active site of the CTD phosphatase Ssu72."
    Xiang K., Manley J.L., Tong L.
    Genes Dev. 26:2265-2270(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-360 IN COMPLEX WITH SSU72, INTERACTION WITH SSU72.

Entry informationi

Entry nameiSYMPK_HUMAN
AccessioniPrimary (citable) accession number: Q92797
Secondary accession number(s): O00521
, O00689, O00733, Q59GT5, Q8N2U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 19, 2005
Last modified: November 26, 2014
This is version 132 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

Miscellaneous

Could be used as a differentiation marker in the differential diagnosis of tumors.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3