wanglab/gogpt-training-data huggingface dataset:
Protein: At2g20940 (Expressed protein) (Transmembrane protein, putative (DUF1279)) (Q9SKR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATRLKEIVKKYGKVALGVHFSVSGVSISGFYIAIKNNVDVESLLEKYQIPWFSSKENPNPSLDLKLEEQGSVTSDNKTKQLAKSAGGALALAVLCNKALFPIRVPITMALTPPIARFLRQRKILKTGQ
Protein: Putative pentatricopeptide repeat-containing protein At2g02150 (P0C894)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cytosolic sulfotransferase 5
- Protein THYLAKOID ASSEMBLY 8, chloroplastic
- Cytosolic sulfotransferase 1
- DEAD-box ATP-dependent RNA helicase 58, chloroplastic
Sequence:
MFCSLRNFLHVNRRFPRHVSPSSSSLSQIQSPLCFPLSSPSPSQSSFISCPFVWFTSFLCIIRYPFVTKSGTSTYSEDFDRDWIRKVVHNDLWDDPGLEKLFDLTLAPIWVPRVLVELKEDPKLAFKFFKWSMTRNGFKHSVESYCIVAHILFCARMYYDANSVLKEMVLSKADCDVFDVLWSTRNVCVPGFGVFDALFSVLIDLGMLEEAIQCFSKMKRFRVFPKTRSCNGLLHRFAKLGKTDDVKRFFKDMIGAGARPTVFTYNIMIDCMCKEGDVEAARGLFEEMKFRGLVPDTVTYNSMIDGFGKVGRLDDTVCFFEEMKDMCCEPDVITYNALINCFCKFGKLPIGLEFYREMKGNGLKPNVVSYSTLVDAFCKEGMMQQAIKFYVDMRRVGLVPNEYTYTSLIDANCKIGNLSDAFRLGNEMLQVGVEWNVVTYTALIDGLCDAERMKEAEELFGKMDTAGVIPNLASYNALIHGFVKAKNMDRALELLNELKGRGIKPDLLLYGTFIWGLCSLEKIEAAKVVMNEMKECGIKANSLIYTTLMDAYFKSGNPTEGLHLLDEMKELDIEVTVVTFCVLIDGLCKNKLVSKAVDYFNRISNDFGLQANAAIFTAMIDGLCKDNQVEAATTLFEQMVQKGLVPDRTAYTSLMDGNFKQGNVLEALALRDKMAEIGMKLDLLAYTSLVWGLSHCNQLQKARSFLEEMIGEGIHPDEVLCISVLKKHYELGCIDEAVELQSYLMKHQLLTSDNDNALPNM
Protein: Uncharacterized protein (Q38E52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSPRSLYVTGKGVLSLVGGFTAGWCGLGFVEDKGLISEANLRALHVGTLKLHLFLQEWILPVSFSEKYGYKKEVLEEIIERYGSGSAAEARWTFEQLLGECEVPGQISWLEEHISEDIPYFYIADLFDSWCNLHRNLFVCSADAHETAKRSDDRFESELLCKGVIEKAISGVLPYDTAVRALCILAIGCRTNTQFMLKTIKPDFIINRYKLYTDDLAQPIDGNTDVTPLAEVNAATIGLLNALNTELQEQEKLKLWKSSTARKLPLLMQLNATPWCDSVDSLRRGLKGITSNNAATLLEEATQYFRCSELSK
Protein: Neuropeptide Y (A4D158)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000256|ARBA:ARBA00037849}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW
Protein: BRISC and BRCA1-A complex member 2 (F8W733)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368019}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368019}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000256|RuleBase:RU368019}.
Interaction partners:
Sequence:
MSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVKELVQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEQLSLSPCHTDFLLTRFLPAPLWGSEVSVPSGPFHLLIILPQPLSGLVRPCLLFSQPCS
Protein: Rhoptry-associated membrane antigen (C0H4M0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Rhoptry neck protein 3
Sequence:
MNVLLLSLLVVQNIVTYLEQIKNGISGHYTEDHNIKNNNCISFSDYERSIKNFSISSHAENNYDNIINEYKKIKDINNNINILSSVHRKGRILYDSFLEINKLENDKKEKHEKEDEYEDNDESFLETEEYEDNEDEKYNKDEDDYAESFIETDEYEDNEDDKYNKDEDDYSESFIETDEYDDNEEEQYNKDEDDYTDSFIETDHYENNDDKNEEEEEYNDQDNDYGYNFLETDEYDDSEEYDYDDKEYGESFLEKEEGEEMKDEEMKDEEMKDVEMKDEEMKDEEMKYDEMKNEEMKYDEMKDEVMKDEEMKDEVMKDEEMKDEQMKYEEFKNEESKNEESKNEESKNEESKNEEFKNEESKNEEFKNEEFKNEDMSYDEYMGYKKKEEDESYNTFNGTKKNNTSNSFLEKDLQGDSDDELHSTFYSKNVDKENYDDKNIFYGYSDNDDESFLETDSYEEYEDEDKDVEDEYEESFLQNDEKKMVFYDLYKPEENESYYEKKQKKEEKEEKEEKEQSLNKQNDMEDQEDNEEYKFEEENKEDLLDVQQDEELPSEGKQKVKGKSFDNEHLNEIQNVSDVHAFIQKDMKYLDDLIDEEQTIKDAVKKSAYKGNKKLGNNKKSQMILEEEPEENFEEDADEELNKLMEQEKNIVDKEIKNSKANKSNKKLQFNNTNKQNKMYMKNEYNNKTKNNKNNKFEQQNYDESYMDDDYEQNEEFNDNNQSEDMKETNELDKINDELLTDQGPNEDTLLENNNKIFDNKFVAHKKREKSISPHSYQKVSTKVQNKEDMENKEEKQLINDEAAMTAEELVELENTEDVNTPTMVETEEIDSDENGNKSSSSISYISSIVFLMVTLLYFMN
Protein: Transcription factor GTE3, chloroplastic (Bromodomain-containing protein GTE3) (Protein GLOBAL TRANSCRIPTION FACTOR GROUP E3) (Q9S7T1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that binds to acetylated histone H3.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- At1g61215
- E3 SUMO-protein ligase SIZ1
- E4 SUMO-protein ligase PIAL1
- PHD finger protein ING2
- E4 SUMO-protein ligase PIAL2
- Protein MIZU-KUSSEI 1
Sequence:
MASGPIAGGGVSKTKHKWSDSGNKSQKRSKPTVANSNSLGLEDNHQMMKISLSSISKLEVRNLKRKLQAELEEVRSLIKRLEPQGNNFAPVPNKKLKTANGGKKGGVHGAAADKGTVQILKSCNNLLTKLMKHKSGWIFNTPVDVVTLGLHDYHNIIKEPMDLGTVKTRLSKSLYKSPLEFAEDVRLTFNNAMLYNPVGHDVYHMAEILLNLFEEKWVPLETQYELLIRKQQPVRDIDFHAPVSTNTHNVEALPLPAPTPSLSPPPPPKVVENRTLERAESMTNPVKPAVLPVVPEKLVEEASANRDLTFDEKRQLSEDLQDLPYDKLEAVVQIIKKRTPELSQQDDEIELDIDSLDLETLWELFRFVTEYKESLSKKKEEQGLDSERDAESFHNSVHESNTLVTGLESSKVTELGHVASTVRQEVNVGGSSSSNSSSSGSGSGSSGSDSDSSGHESDTGN
Protein: Histone chaperone ASF1 (Anti-silencing function protein 1) (yASF1) (P32447)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for RTT109-dependent acetylation of histone H3 on 'Lys-9' and 'Lys-56'. Promotion of RTT109-mediated histone H3 'Lys-56' acetylation is dependent on interactions with histone H3 pre-acetylated on 'Lys-14'.
Subcellular location: Nucleus {ECO:0000269|PubMed:11404324, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16020781}.
Interaction partners:
- Protein HIR2
- Serine/threonine-protein kinase RAD53
- Histone H3
- Histone H4
- Protein HIR1
- Histone acetyltransferase RTT109
- Chromatin assembly factor 1 subunit B
- HAT1-interacting factor 1
- Histone transcription regulator 3
- Chromatin assembly factor 1 subunit A
Sequence:
MSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGVDDEEEEDDEEEDDDEDDEDDEDDDQEDGEGEAEEAAEEEEEEEEKTEDNETNLEEEEEDIENSDGDEEEGEEEVGSVDKNEDGNDKKRRKIEGGSTDIESTPKDAARSTN
Protein: Trihelix transcription factor GT-1 (Trihelix DNA-binding protein GT-1) (Q9FX53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that binds specifically to the core DNA sequence 5'-GGTTAA-3'. May act as a molecular switch in response to light signals.
Subcellular location: Nucleus {ECO:0000269|PubMed:7866025}.
Interaction partners:
- E3 ubiquitin-protein ligase SP1
- Protein HOTHEAD
- ABC transporter F family member 4
- Probable xyloglucan 6-xylosyltransferase 3
- Trihelix transcription factor ASIL1
- Probable xyloglucan 6-xylosyltransferase 5
- Trihelix transcription factor ASIL2
- At5g63780
- Probable xyloglucan galactosyltransferase GT20
- Transcription factor AS1
Sequence:
MFISDKSRPTDFYKDDHHNSSTTSTTRDMMIDVLTTTNESVDLQSHHHHNHHNHHLHQSQPQQQILLGESSGEDHEVKAPKKRAETWVQDETRSLIMFRRGMDGLFNTSKSNKHLWEQISSKMREKGFDRSPTMCTDKWRNLLKEFKKAKHHDRGNGSAKMSYYKEIEDILRERSKKVTPPQYNKSPNTPPTSAKVDSFMQFTDKGFDDTSISFGSVEANGRPALNLERRLDHDGHPLAITTAVDAVAANGVTPWNWRETPGNGDDSHGQPFGGRVITVKFGDYTRRIGVDGSAEAIKEVIRSAFGLRTRRAFWLEDEDQIIRCLDRDMPLGNYLLRLDDGLAIRVCHYDESNQLPVHSEEKIFYTEEDYREFLARQGWSSLQVDGFRNIENMDDLQPGAVYRGVR
Protein: Tetratricopeptide repeat protein 4 (TPR repeat protein 4) (Q8R3H9)
Organism: Mus musculus (Mouse)
Function: May act as a co-chaperone for HSP90AB1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17335777, ECO:0000269|PubMed:19390865, ECO:0000269|PubMed:24913909}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:O95801}. Cytoplasm {ECO:0000269|PubMed:19390865}. Note=Predominantly nuclear in the G1 and S phases of cell cycle and is evenly distributed between the nucleus and cytoplasm in the G2 phase (PubMed:19390865). MSL1 can promote its nuclear localization (PubMed:19390865, PubMed:24913909). {ECO:0000269|PubMed:19390865, ECO:0000269|PubMed:24913909}.
Interaction partners:
- Protein HGH1 homolog
- Small ribosomal subunit protein eS7
- Male-specific lethal 1 homolog
- Tetratricopeptide repeat protein 5
- Hsp90 co-chaperone Cdc37
- Tetratricopeptide repeat protein 9C
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
Sequence:
MESSEPEPTEDASMDAFLEKFQSQPYRGGFREDQWEEEFDKIPLFMKKAPSEIDPEEFPDLACLQSMIFDDDRYPEEQAKTYKDEGNDYFKEKDYKKAVLSYSEGLKKKCADPDLNAVLYTNRAAAQYYLGNVRSSLNDVLAAKKLKPGHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEIRAKADKLKRMEERDLRKAKLKEKKEQHQNEALLQAIKARNIRLVSESAGEDEDSASNGPAEILLDGLSSENPYGARLSIDDQGRLSWPVLFLYPEYAQSDFISAFHEDTRFIDHLMAMFSEAPSWDSEHKYHPENLEVYFEDEDRAELYQVSPDSTLLQVLQHPRCCVKALTPAFLVCVGSSPFCRNYLQGKKVHR
Protein: Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (EC 3.1.3.16) (Phosphatase PP2A-like catalytic subunit PPH3) (P32345)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms the histone H2A phosphatase complex in association with the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. PPH3 is directly involved in the dephosphorylation and activation of the transcription factor GLN3 in response to nutrient availability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Type 2A phosphatase-associated protein 42
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Protein phosphatase PP2A regulatory subunit A
- Cell cycle serine/threonine-protein kinase CDC5/MSD2
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase 2A activator 1
- Protein phosphatase 2C homolog 2
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator 2
Sequence:
MMDLDKIIASLRDGKHIPEETVFRLCLNSQELLMNEGNVTQVDTPVTICGDIHGQLHDLLTLFEKSGGVEKTRYIFLGDFVDRGFYSLESFLLLLCYKLRYPDRITLIRGNHETRQITKVYGFYDEVVRKYGNSNVWRYCCEVFDYLSLGAIINNSIFCVHGGLSPDMTTVDEIRTIDRKQEVPHEGAMCDLLWSDPEDVDTWSLSPRGAGFLFGKREVDQFLEKNNVELIARAHQLVMEGYKEMFDGGLVTVWSAPNYCYRCGNVAAVLKIDDDLNREYTIFEAVQAQNEVGNAIIPTKKSQMDYFL
Protein: Apoptosis-stimulating of p53 protein 2 (Tumor suppressor p53-binding protein 2) (53BP2) (p53-binding protein 2) (p53BP2) (Q8CG79)
Organism: Mus musculus (Mouse)
Function: Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions with proteins such as TP53 (By similarity). Regulates p53/TP53 by enhancing the DNA binding and transactivation function of p53/TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42 (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. {ECO:0000250}.
Interaction partners:
- Cellular tumor antigen p53
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
- Tumor protein p73
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Apoptosis regulator Bcl-2
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Tumor protein 63
- Protein S100-A8
Sequence:
MMPMFLTVYLSNSEQHFTEVPVTPETICRDVVDLCKEPGENDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPNRDIVSGPRSQDPSVKRNGVKVPGEHRRKENGVNSPRLDLTLAELQEMASRQQQQIEAQQQMLATKEQRLKFLKQQDQRQQQQAAEQEKLKRLREIAESQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNSLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDGHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVSELRDRLWKKKAALQQKENLPVSPDGNLPQQAVSAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLLMQSAEGPMKIQTLPNMRSGAASQSKGSKAHPASPDWNPSNADLLPSQGSSVPQSAGTALDQVDDGEIAVREKEKKVRPFSMFDTVDQCAAPPSFGTLRKNQSSEDILRDAQAVNKNVAKVPPPVPTKPKQIHLPYFGQTAQSPSDMKPDGNAQQLPIAATSVGAKLKPAGPQARMLLSPGAPSGGQDQVLSPASKQESPPAAAVRPFTPQPSKDTFPPAFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTQPRGPHFSSVYGKPVIAAAQNPQQHPENIYSCSQGKPGSPEPETETVSSVHESHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSHPSKSPGSVTVNPESSVEIPNPYLHVEPEKEVGSLVPEPLSPEDMGSASTENSDVPAPSAGLEYVSEGVTDSSTNLQNNVEETNPEAPHLLEVYLEEYPPYPPPPYPSGEPEVSEEDSARMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQHDDELLMKEGDCMTVIRREDEEEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA
Protein: CRA domain-containing protein, putative (Q8IBD0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKNKLSTLFFITIFLILIFIDSAKGDERKNFWKSRFTAGRGNITNKPTEVNHPIKKEGENFLSVGKGDHDESRVMLLKELYQKDNELNIVRKKHKKYKSITVALASIIGMMLLRNIGSLLYDTVTRLNQKSNRVWML
Protein: Cysteine-rich receptor-like protein kinase 45 (Cysteine-rich RLK45) (EC 2.7.11.1) (ABA- and osmotic stress-inducible receptor-like cytosolic kinase 1) (Q8GY82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms a complex with CRK36 that may negatively control abscisic acid (ABA) and osmotic stress signal transduction. Involved in plant response to ABA during seed germination, early seedling growth and responses to abiotic stresses by inducing the expression of ABA-responsive genes and stress-inducible genes. Acts as positive regulator in disease resistance, downstream of NPR1 and WRKY70.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22225700}. Note=Interacts with CRK36 at the cell surface. {ECO:0000269|PubMed:22225700}.
Interaction partners:
- Cysteine-rich receptor-like protein kinase 36
- Phospholipase like protein family protein)
- Protein RALF-like 27
Sequence:
MAVTSLLDTVFRRRKKKSTEFISFFEFDLDTIKAATNDFSELVGRGGFGFVYKGRLQNGQEIAVKILSTSSIRTERQFHNELIILSKLKHKNLINLLGFCTKRDQHGLVYEFMPNSSLDCFILDPHRAAQLNWEMCRNIIDGIARGLRYLHEESGLWVVHRDIKPGNILLDSDLKPKIVGFELARTMQQGENAAETTEIVGTVGYLDPEYIRSGRVSVKSDVYAFGVTILTIISRRKAWSVDGDSLIKYVRRCWNRGEAIDVIHEVMREEEREYSISEILRYIHIALLCVDENAERRPNIDKVLHWFSCFSTPLPDPTFGNRFLVEEETNWPWSPSLSPGHSSVTSPISSR
Protein: DNA-binding protein (DBP) (Early 2A protein) (Early E2A DNA-binding protein) (P03265)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its relese from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04054}. Note=Accumulates in infected cells. {ECO:0000255|HAMAP-Rule:MF_04054}.
Interaction partners:
Sequence:
MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSKKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF
Protein: Probable sigma-70 factor, ECF subfamily (Q9HYJ5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transmembrane sensor
- Sigma factor regulator, FemR
- Probable transmembrane sensor
- Probable transmembrane sensor
- Probable transmembrane sensor
- Probable transmembrane sensor
- Probable transmembrane sensor
- Anti-sigma factor FoxR
- Probable transmembrane sensor
- Sigma factor regulator, VreR
Sequence:
MDAPLAEQDLKALFLRHARQLQSYLLRKTRDPHLAADLAQESFLRLAEQRHKEPIEHVDAYLYRTAHNLTIDHYRQERRRRTETQPNDDLAGFVADQPGPEESAVDADALARLREIVAELPPRTREIFRLNRLEGLTHAEVARRLEISDSSVQKHLARTLAHVMQALEDSR
Protein: L-threonine kinase (EC 2.7.1.177) (Propanediol utilization protein PduX) (Q9XDM4)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: L-threonine kinase that catalyzes the conversion of L-threonine to L-threonine-O-3-phosphate. Involved in the de novo synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of cobyric acid. Uses ATP; the activity with CTP, GTP or UTP is 6, 11, and 3% of the activity with ATP, respectively.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Threonine-phosphate decarboxylase
- Cobalt-precorrin-5A hydrolase
- Corrinoid adenosyltransferase PduO
- 1-propanol dehydrogenase PduQ
- Cobyric acid synthase
- Bacterial microcompartment shell protein PduK
- Cobalt-precorrin-6A reductase
- Propanal dehydrogenase
- Cobalt-precorrin-5B C
- Probable cobalt-factor III C
Sequence:
MRAHYSYLKGDNVAVAQCPASCGELIQGWILGSEKLVSCPVDWYSTVAVTAAPPLINERPLSRAMVERVLAHWQYPAHWSNEIRVDVRSSIPVAKGMASSTADIAATAVATAHHLGHSLDETTLAQLCVSIEPTDSTVFHQLTLFDHNNAATQIACEPPPPIDLLVLESPVTLRTQDYHRLPRQQKLIASSATLQQAWNLVQEACITQNPLRLGEAATLSAIASQTLLPKPGFTALLSLVEECDLYGLNVAHSGSVVGLMLDRKRHDIARLKGKLAEKKLTRHWPKQHLLKMVTGGVKLQ
Protein: Flagella synthesis protein FlgN (P43533)
Organism: Escherichia coli (strain K12)
Function: Required for the efficient initiation of filament assembly.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Negative regulator of flagellin synthesis
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein 3
- Flagella basal body P-ring formation protein FlgA
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 2
- Flagellar basal body rod protein FlgB
- RNA polymerase sigma factor FliA
- Basal-body rod modification protein FlgD
- Flagellar hook protein FlgE
Sequence:
MTRLAEILDQMSAVLNDLKTVMDQEQQHLSMGQINGSQLQWITEQKSSLLATLDYLEQLRRKEPNTANSVDISQRWQEITVKTQQLRQMNQHNGWLLEGQIERNQQALEMLKPHQEPTLYGANGQTSTTHRGGKKISI
Protein: Docking protein 5 (Downstream of tyrosine kinase 5) (Q91ZM9)
Organism: Mus musculus (Mouse)
Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK5 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway. Putative link with downstream effectors of RET in neuronal differentiation.
Interaction partners:
Sequence:
MASNFNDIVKQGYVRIRSRRLGIYQRCWLVFKKASSKGPKRLEKFSDERAAYFRCYHKVTELNNVKNVARLPKSTKKHAIGIYFNDDTSKTFACESDLEADEWCKVLQMECVGTRINDISLGEPDLLATGVEREQSERFNVYLMPSPNLDVHGECALQITYEYICLWDVQNPRVKLISWPLSALRRYGRDTTWFTFEAGRMCETGEGLFIFQTRDGEAIYQKVHSAALAIAEQHERLLQSVKNSMLQMKKSERAASLSTVVPLPRSAYWQHITRQHSTGQLYHLQDVTSPLKLHRTETFPTYRSEH
Protein: Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta) (eIF2-beta) (P20042)
Organism: Homo sapiens (Human)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 2 subunit 3
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 5
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 1
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit B
Sequence:
MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDTQTEETQPSETKEVEPEPTEDKDLEADEEDTRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEGVKDLKIESDVQEPTEPEDDLDIMLGNKKKKKKNVKFPDEDEILEKDEALEDEDNKKDDGISFSNQTGPAWAGSERDYTYEELLNRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFLLAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFLQCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN
Protein: Axin-1 (Axis inhibition protein 1) (rAxin) (O70239)
Organism: Rattus norvegicus (Rat)
Function: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects; down-regulates beta-catenin to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (By similarity). Also facilitates the phosphorylation of APC by GSK3B (By similarity). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (By similarity). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15169}. Nucleus {ECO:0000250|UniProtKB:O15169}. Cell membrane {ECO:0000269|PubMed:16815997}. Membrane {ECO:0000250|UniProtKB:O35625}. Note=On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its translocation to cell membrane (By similarity). {ECO:0000250|UniProtKB:O15169, ECO:0000250|UniProtKB:O35625}.
Interaction partners:
Sequence:
MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDSVPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHAPKLGLKLDSAGLHHHRHVHHHVHHNSARPKEQMEAEAARRVQSSFSWGPETHGHAKPRSYSESTGTNPSAGDLAFGGKASAPSKRNTKKAESGKNASAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGMRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRTKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAILPVFEEKIIGKVEKVD