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Protein

SNF1-like protein kinase ssp2

Gene

ssp2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631ATPPROSITE-ProRule annotation
Active sitei156 – 1561Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • polyubiquitin binding Source: PomBase
  • protein kinase activity Source: PomBase
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 5613.
ReactomeiR-SPO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SPO-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SPO-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Names & Taxonomyi

Protein namesi
Recommended name:
SNF1-like protein kinase ssp2 (EC:2.7.11.1)
Gene namesi
Name:ssp2
ORF Names:SPCC74.03c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC74.03c.
PomBaseiSPCC74.03c. ssp2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • nucleotide-activated protein kinase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576SNF1-like protein kinase ssp2PRO_0000086669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei442 – 4421Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74536.

PTM databases

iPTMnetiO74536.

Interactioni

GO - Molecular functioni

  • polyubiquitin binding Source: PomBase

Protein-protein interaction databases

BioGridi275681. 222 interactions.
DIPiDIP-29520N.
IntActiO74536. 1 interaction.
MINTiMINT-4679856.

Structurei

Secondary structure

1
576
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 313Combined sources
Beta strandi34 – 4310Combined sources
Beta strandi46 – 538Combined sources
Turni54 – 563Combined sources
Beta strandi59 – 668Combined sources
Helixi67 – 726Combined sources
Helixi77 – 8610Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi104 – 1118Combined sources
Helixi118 – 1258Combined sources
Helixi130 – 14920Combined sources
Turni159 – 1613Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi170 – 1723Combined sources
Turni178 – 1836Combined sources
Turni194 – 1963Combined sources
Helixi199 – 2013Combined sources
Helixi206 – 2083Combined sources
Helixi210 – 22617Combined sources
Beta strandi230 – 2323Combined sources
Beta strandi234 – 2363Combined sources
Helixi256 – 2638Combined sources
Helixi270 – 2723Combined sources
Helixi276 – 2794Combined sources
Helixi283 – 2864Combined sources
Helixi291 – 2933Combined sources
Helixi306 – 3149Combined sources
Helixi320 – 3267Combined sources
Beta strandi329 – 3313Combined sources
Helixi338 – 35114Combined sources
Beta strandi453 – 4608Combined sources
Helixi462 – 47615Combined sources
Beta strandi486 – 4894Combined sources
Helixi492 – 4954Combined sources
Beta strandi496 – 5027Combined sources
Helixi504 – 5085Combined sources
Beta strandi513 – 52513Combined sources
Beta strandi528 – 54114Combined sources
Turni545 – 5473Combined sources
Helixi562 – 57514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOXX-ray2.60A/C440-576[»]
2OOYX-ray2.88A/C440-576[»]
2QR1X-ray2.70A/C440-576[»]
2QRCX-ray2.70A/C440-576[»]
2QRDX-ray2.41A/C440-576[»]
2QREX-ray3.01A/C440-576[»]
3H4JX-ray2.80A/B25-351[»]
ProteinModelPortaliO74536.
SMRiO74536. Positions 30-295, 447-575.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO74536.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 285252Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini304 – 34542UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000233016.
InParanoidiO74536.
KOiK12761.
OMAiTIDSNIC.
OrthoDBiEOG793BK1.
PhylomeDBiO74536.

Family and domain databases

InterProiIPR032270. AMPK_C.
IPR028375. KA1/Ssp2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
IPR013896. Ubiquitin-assoc_dom.
[Graphical view]
PfamiPF16579. AdenylateSensor. 1 hit.
PF00069. Pkinase. 1 hit.
PF08587. UBA_2. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74536-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPQEVDLME NSTMRNGARV LPPEAISKRH IGPYIIRETL GEGSFGKVKL
60 70 80 90 100
ATHYKTQQKV ALKFISRQLL KKSDMHMRVE REISYLKLLR HPHIIKLYDV
110 120 130 140 150
ITTPTDIVMV IEYAGGELFD YIVEKKRMTE DEGRRFFQQI ICAIEYCHRH
160 170 180 190 200
KIVHRDLKPE NLLLDDNLNV KIADFGLSNI MTDGNFLKTS CGSPNYAAPE
210 220 230 240 250
VINGKLYAGP EVDVWSCGIV LYVMLVGRLP FDDEFIPNLF KKVNSCVYVM
260 270 280 290 300
PDFLSPGAQS LIRRMIVADP MQRITIQEIR RDPWFNVNLP DYLRPMEEVQ
310 320 330 340 350
GSYADSRIVS KLGEAMGFSE DYIVEALRSD ENNEVKEAYN LLHENQVIQE
360 370 380 390 400
KSHLSKSKRV DSFLSVSPPA FSEYTSELQK KSKQELIDPT LEGPRWTVSD
410 420 430 440 450
PPTYAKQTID SNICVLVPTA EKNKLEMRTL ADAASAVDTS QSTRKKSRRN
460 470 480 490 500
KWHFGVRCRG DAPEILLAVY RALQRAGAQF TVPKPVNGKY RSDMYTIKSR
510 520 530 540 550
WEIPHCKREG KNTYAYIELQ LYEVMPGCFM LDVKSNGYKD IYSHPERTAD
560 570
HGMDDLKSSF PFLDLCAMLV CKLFSA
Length:576
Mass (Da):65,996
Last modified:November 1, 1998 - v1
Checksum:iE5857E8F171E7B50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20833.1.
PIRiT41587.
RefSeqiNP_588376.1. NM_001023367.2.

Genome annotation databases

EnsemblFungiiSPCC74.03c.1; SPCC74.03c.1:pep; SPCC74.03c.
GeneIDi2539109.
KEGGispo:SPCC74.03c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA20833.1.
PIRiT41587.
RefSeqiNP_588376.1. NM_001023367.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOXX-ray2.60A/C440-576[»]
2OOYX-ray2.88A/C440-576[»]
2QR1X-ray2.70A/C440-576[»]
2QRCX-ray2.70A/C440-576[»]
2QRDX-ray2.41A/C440-576[»]
2QREX-ray3.01A/C440-576[»]
3H4JX-ray2.80A/B25-351[»]
ProteinModelPortaliO74536.
SMRiO74536. Positions 30-295, 447-575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275681. 222 interactions.
DIPiDIP-29520N.
IntActiO74536. 1 interaction.
MINTiMINT-4679856.

PTM databases

iPTMnetiO74536.

Proteomic databases

MaxQBiO74536.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC74.03c.1; SPCC74.03c.1:pep; SPCC74.03c.
GeneIDi2539109.
KEGGispo:SPCC74.03c.

Organism-specific databases

EuPathDBiFungiDB:SPCC74.03c.
PomBaseiSPCC74.03c. ssp2.

Phylogenomic databases

HOGENOMiHOG000233016.
InParanoidiO74536.
KOiK12761.
OMAiTIDSNIC.
OrthoDBiEOG793BK1.
PhylomeDBiO74536.

Enzyme and pathway databases

BRENDAi2.7.11.1. 5613.
ReactomeiR-SPO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SPO-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SPO-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Miscellaneous databases

EvolutionaryTraceiO74536.
PROiO74536.

Family and domain databases

InterProiIPR032270. AMPK_C.
IPR028375. KA1/Ssp2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR015940. UBA.
IPR013896. Ubiquitin-assoc_dom.
[Graphical view]
PfamiPF16579. AdenylateSensor. 1 hit.
PF00069. Pkinase. 1 hit.
PF08587. UBA_2. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSNF1_SCHPO
AccessioniPrimary (citable) accession number: O74536
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.