wanglab/gogpt-training-data huggingface dataset:
Protein: Protein arginine N-methyltransferase HSL7 (EC 2.1.1.320) (Histone synthetic lethal protein 7) (Type II protein arginine N-methyltransferase) (Type II PRMT) (P38274)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that can catalyze both the mono- and symmetric (type II) dimethylation of the guanidino nitrogens of arginine residues in target proteins. Involved in the control of the cell cycle at the G2/M (mitosis) transition. Cooperates with HSL1 to hyperphosphorylate SWE1, thereby targeting SWE1 for polyubiquitination and subsequent degradation. Acts as a negative regulator of the filamentous growth-signaling pathway through inhibition of STE20.
Subcellular location: Bud neck {ECO:0000269|PubMed:10490648}. Note=Associates with the septin ring of the bud neck during cell division. {ECO:0000269|PubMed:10490648}.
Interaction partners:
- Mitosis inhibitor protein kinase SWE1
- Probable serine/threonine-protein kinase HSL1
- Protein LOT5
- Polyadenylation factor subunit 2
- Serine/threonine-protein kinase RIO1
- Mitogen-activated protein kinase HOG1
- Protein arginine N-methyltransferase 2
- M-phase inducer phosphatase
- Protein arginine N-methyltransferase 1
- G2/mitotic-specific cyclin-2
Sequence:
MHSNVFVGVKPGFNHKQHSKKSRFLENVSSHSPELPSNYDYVLLPITTPRYKEIVGQVFKDFQRQSIQNWKPLQIPEPQLQDICIPPFNVKKLDNDDTPSYIGLLSSWLELESRDPNVRDLGLKVLLNECKYARFVGINKLILAPPRDLSNLQLYGQMIYRLLQNRIVFAAPALTISISLPLYEDSDPLATWELWNTVRKQCEYHPSLTISLALPRTRTPSYVLNRWLAEPVSCLLVSSSIFASNQYDYPVLHKFNQNLILKFQKVNGDSQILGNELCVILHGMEKYANNVKGGESAYLEYINYLLKKGDKVLNSNSNHQFLLQEDSRIMPPLKPHSDNLLNSTYLTFEKDLVKYDLYESAILEALQDLAPRASAKRPLVILVAGAGRGPLVDRTFKIISMLFMDSKVSIIAIEKNPQAYLYLQKRNFDCWDNRVKLIKEDMTKWQINEPSEKRIQIDLCISELLGSFGCNELSPECLWSIEKYHSHNDTIFIPRSYSSYIAPISSPLFYQKLSQTNRSLEAPWIVHRVPYCILSSRVNEVWRFEHPMAQKDTVQDEDDFTVEFSQSSLNEFKIKHRGEIHGFIGFFSANLYNNIFLSTLPNDSTVRLKFSEETLMNTRREENLIKKCDHTPNMTSWSPIIFPLKQPISFIDDSELSVLMSRIHSDTEQKVWYEWSLESFIYLMLSNYTSAVTAASMTIPRSIVTDDTKTLAHNRHYSATTNQKLDNQIDLDQDIENEEEQGFLSNLETGWQSVQDIHGLSETAKPDHLDSINKPMFDLKSTKALEPSNELPRHEDLEEDVPEVHVRVKTSVSTLHNVCGRAFSLPL
Protein: ribonuclease H (EC 3.1.26.4) (Q09633)
Organism: Caenorhabditis elegans
Interaction partners:
- Ribonuclease H2 subunit A
- Ribonuclease H1
- SERPIN domain-containing protein
- Protein-tyrosine phosphatase
- Protein-tyrosine phosphatase
- Protein kinase domain-containing protein
- DUF4091 domain-containing protein
- PDZ domain-containing protein
- Protein kinase domain-containing protein
- Protein kinase domain-containing protein
Sequence:
MIRWFRNFGALFKKPRGAGLMKNEQTHNLQRVVQNDITCPEEQRSTGGKGGGGGSHGGHGGSHGGSHGGHGSHGGSYGGHSGHGRSFSTSSGSSGYRGLSSGSTNTSYSKSTPRTNSGYSTGKTTKTASSSRNYSNTSSTRSTTKPSKSSYSKRSTKSTKSLNYSSSSLGSKSIEKSRRSSRKSGSRQDSVASRRQLRSVSSKPQKKYVATDMPSTVSTGRSRGRSVYRRNNVNADVSQRQSRSMSVSRGRSRNRSQNRERSPSIEKSTRSQHVSRKDAFNSHDVLSPTNRSGSVHRSHSAHHERTFEERHKTPNGVWNEMFPKGTLVMYTDGSYLKRPPTSGIGIFVGPGHELNRSQRIRGPIQDNNYAEFIAVRTALQNALKNENYRDQKVVIRTDCLNVIEALQGTRPTAFVDVKSQVEFLSKQFPKGVHFQHVYAHAGDPGNEMADLFAGQASSKSQNSFGGGQRTRSASTARGRSRERNRLRSKSNDPSFIRSRSHSIHSRK
Protein: Tubulin alpha chain (A9PL15)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRECISVHIGQAGIQVGNACWELYCLEHGIQPDGQMPSDKTVGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAESGEGDEEDEDEY
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Q9VPW4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mitochondrial transcription factor A, isoform B
- Dimethyladenosine transferase 1, mitochondrial dimethyltransferase 1)
- Single-stranded DNA-binding protein, mitochondrial
- RE67859p
- Probable dimethyladenosine transferase-N
- Dimethyladenosine transferase 2, mitochondrial dimethyltransferase 2)
- DNA polymerase subunit gamma-1, mitochondrial
- Transcription termination factor 3, mitochondrial
- DNA-directed RNA polymerase I subunit RPA2
- GM03767p
Sequence:
MYRLLSANRAAAVQKALRVPPTAHPTTTTATTTTVCCGCGIAPSNFVHYQQYYQMLYRQMPAGAITAKTTTTTTRTQTTTPTQTDAVAQAKKKRLRKPRYAKYVELLEVTEQAISERRSRVKRLKSKKLADFIHKAQQQILERRAREDRKDKKTKCVLDLAQRQPVEYQKIDMEALDGSILESGVYDDRPMLFFGKDEYTKQVIANPEEVQNILKSFQNFRDIIESMENDQHEADFGLSTTKVHPEEHEMLDPFEAIEPYISPLDKSKRSVTTVAVPNASAVTTKSKKRFKSKVHVNEEQERLAKQRALHINLNTYLNVCVSANMLNRALSTIIAYRGKVRKSSLPHMSEGLITIDLYNILLHGYAGKGSFDRAQEVFKLIEEDGLSFNEQTYAAIFECLGRLEPDEENHQYISEYVSKAEKEGFSLNQIMDRSKFVADQRDIALDAIRRLRPDFKPVYVPPQLGYDNELLDHLNEHVIPVGAKKEPGKADYAIMNSKRGYTAAQLEQLAREQLKIELDGSITIKSIEKSKEFANSEKCRELLKELEDTWRKQISAAIVRDLNTLRAQVRFKPHGFMNYYTYLKTLDASHFADILIKELYKLAEGSETFSPTVGQLYKELGQKVQQRYQIEQKKHNGTLEKIGEIYSSYCELWGSGMSQDNTRQAWQRLVYEQRESGPSMDLLEVPWPSNVLTGVGRFLYNILMRDIKIDAHIMRQKSKSKAAAQPQNLLPAFYTLFRNQGRFVKEEVKPHPVLSRLFRASRQQTLTFDSNLVPMLCPPQPWSTPHNGGYLLNKTELIRLPHQAIQQWDRIMASNPQHLYPALDSLNQLASVPWRVNTQLLDVIIKVFQNGGDVKLDVPQPPSSLPPLPTLPAKDAEGNATSSEDRAKQFRDKLGHRRKQAEMYSLWCDALYRLSLAQHYRDKVFWLPHNMDFRGRVYPVPPHLNHLGSDLARSMLIFDQAQPLGVDGLSWLKLHCINLTGLKKRDSVRERLLYAEEIMPDILDSADNPLTGRMWWSKSDEPWQTLACCMEIANVHRCPDPAAYLSRFPIHQDGSCNGLQHYAALGRDEAGARSVNLAPSAIPQDVYSAVAALVEKSRKADAQNGLHVAEALAGFVRRKVIKQTVMTTVYGVTRYGARLQIARQLKDIDDFPKDWVWPASTYLTTKTFESLREMFTSTREIQDWFTECARLISGVCSQNVEWVTPLGLPVVQPYNRQEMKHSPRSGFKVSANMPMDLYERPNILKQKNAFPPNFIHSLDSSHMMLTSLHCERQGITFVSVHDCFWTHANTVPELNRMCREQFVALHSQPILEQLSEFMRHTYSFKDSDFINDGSVEDLSKRQLNRILKQMPQKGDFDLRNVLDSVYFFS
Protein: Melanoma-associated antigen 3 (Antigen MZ2-D) (Cancer/testis antigen 1.3) (CT1.3) (MAGE-3 antigen) (P43357)
Organism: Homo sapiens (Human)
Function: Activator of ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases that acts as a as repressor of autophagy. May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. May play a role in embryonal development and tumor transformation or aspects of tumor progression. In vitro promotes cell viability in melanoma cell lines. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes.
Interaction partners:
- Melanoma-associated antigen 6
- Melanoma-associated antigen 12
- Transcription intermediary factor 1-beta
- Chondrosarcoma-associated gene 1 protein
- Cancer/testis antigen 1
- G antigen 2A
- demerged
- Cancer/testis antigen 2
- Tyrosinase
- Melanocyte protein PMEL
Sequence:
MPLEQRSQHCKPEEGLEARGEALGLVGAQAPATEEQEAASSSSTLVEVTLGEVPAAESPDPPQSPQGASSLPTTMNYPLWSQSYEDSSNQEEEGPSTFPDLESEFQAALSRKVAELVHFLLLKYRAREPVTKAEMLGSVVGNWQYFFPVIFSKASSSLQLVFGIELMEVDPIGHLYIFATCLGLSYDGLLGDNQIMPKAGLLIIVLAIIAREGDCAPEEKIWEELSVLEVFEGREDSILGDPKKLLTQHFVQENYLEYRQVPGSDPACYEFLWGPRALVETSYVKVLHHMVKISGGPHISYPPLHEWVLREGEE
Protein: Kazal-like domain-containing protein (Q3TRK5)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKTATVPMLLTLAFYLTQDAAGEKGNQDPCMKFQAQMKNGTLTCPKGNNSSQSLNDIIFQSECILCKRALEQGAPTKIMNVKVLSRANRATDPAKLNCESFKQRRKDGDFICPSDTSSVCGTDGKTYRSRCELCAENAKSQNHVDVKSEGECGSSHLETDMCSDFRAYVQDGRLGCTRESDPILGPDGRTHGNRCAMCAELFLKEAKENATRNRESRIRRDAEKELCKEFENQVRNGRLFCTRESDPIRGPDGKMHGNKCALCAEIFMRQFTEEKGKAEKNQKDAEERAKAKMEIQKRCSEFQDRARNGTLFCTRENDPIRGLDGKTHGNLCSMCQAFFKTEAEEKKAEAGSRNRRGSEESETYAKLCDEYRKARKNGQLYCTRENAPIRGPDGKIHGNTCSMCQAFFIQEDKARAKVKREAAKEMCSEFRNQARNGMLMCTRENDPVVGPDGKRHSNKCAMCASVFLLEEEEKKKDDKTEKVDAGKAKKEAVQELCRKYHTQLRNGPLRCTRRNNPIEGLDGKMYKNACFMCWAFFQQEAKKSGAGFRPKVKREVKVDCSEYLALSKRGEIFCTRENDPVRGPDGKTHGNKCAMCKAVF
Protein: Tumor protein p53-inducible protein 11 (p53-induced gene 11 protein) (O14683)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Thioredoxin-like protein 1
Sequence:
MAAKQPPPLMKKHSQTDLVSRLKTRKILGVGGEDDDGEVHRSKISQVLGNEIKFTIREPLGLRVWQFVSAVLFSGIAIMALAFPDQLYDAVFDGAQVTSKTPIRLYGGALLSISLIMWNALYTAEKVIIRWTLLTEACYFGVQFLVVTATLAETGLMSLGILLLLVSRLLFVVISIYYYYQVGRRPKKA
Protein: Prostaglandin E synthase 2 (EC 5.3.99.3) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form] (Q9N0A4)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro). The biological function and the GSH-dependent property of PTGES2 is still under debate. In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H7Z7}.; SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region. {ECO:0000250|UniProtKB:Q9H7Z7}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin E synthase
- Hematopoietic prostaglandin D synthase
- Prostaglandin-H2 D-isomerase
- Prostaglandin-endoperoxide synthase 1.
- Prostaglandin-endoperoxide synthase 2.
- Prostacyclin synthase
- Carbonyl reductase 1])
- carbonyl reductase
- Peroxiredoxin like 2B.
Sequence:
MAPATRVVRALWTGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGQGPVAAARKGSPRLLGAAALALGGALGLYHTARWHLHAQDLHAERSAVQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVLRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNDQGKEVTEFGNKYWLMLNEKEAQQVYSGKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH
Protein: Mast cell protease 2 isoform X2 (Si:ch211-212d10.1) (A0A2R8QQC0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Carbonyl reductase family member 4
- Large ribosomal subunit protein uL16m
Sequence:
MSIIWQTTSLLLLLRCCAPGFCMRDGIVGGKVSIPHSRPYMVYIKDSNSKLACGGFLIREDFVLTAAHCKRSHLKVYLGVNDTHILPHGIEVEATPHPKFNNAPGDDIMLLKLKTPATLNKTVNIITWPECENKEISKDCMVLGWGWQDYVDGCPSSVLKEANVTLIDFKKCGTNYTLCTNGSIGPAKGDSGGPLVCGDAAQGIVSFYTESSGVYLTRYTRISHYHQWIDHIMNKTYQQQLKTWRGKLYELI
Protein: SKP1-like protein 14 (AtSK14) (O81057)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-like protein 3
- Cullin-2
- Putative cullin-like protein 1
- Putative cullin-like protein 2
- RING-box protein 1a
- F-box protein DOR
- RING-box protein 1b
- F-box protein 7
- Elongin-C
Sequence:
MSSNKIVLSSSDGESFEVEEAVARKLKIVEHMIEDDCVVTEVPLQNVTGKILSIVVEYCKKHVVDEESDEFKTWDEEFMKKFDQPTVFQLLLAANYLNIKGLLDLSAQTVADRIKDKTPEEIREIFNIENDFTPEEEAAVRKENAWAFE
Protein: Cytochrome c oxidase-assembly factor COX23, mitochondrial (P38824)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the assembly of cytochrome c oxidase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15145942}. Mitochondrion intermembrane space {ECO:0000269|PubMed:15145942, ECO:0000269|PubMed:22984289}.
Interaction partners:
- Cytochrome c oxidase copper chaperone
- Cytochrome c oxidase assembly protein COX11
- Mitochondrial protein PET191
- Cytochrome c oxidase assembly protein COX19
- COX assembly mitochondrial protein 2
- Cytochrome c oxidase subunit 12, mitochondrial
- Protein SCO2
- mRNA-binding protein PUF3
- Cytochrome c oxidase assembly factor 6
- Mitochondrial intermembrane space import and assembly protein 40
Sequence:
MEKPSPTRRQTSSLSTISNGMTMTNDNRDTTNTNSGSTSSNNSQPSSSSTPPAASGPVTDRTKVNYVPKSDDPSSFQYYPDDPENPVNKYKFALKADSQYYDPCEESSKLSFQCLERNDYDRSKCQEYFDAYRECKKQWLTARRKNRQQWE
Protein: Integrin subunit alpha 4 (A0A8I5Y1L1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MAAEAMCRPRPRGVALQEAVMLLLYFGVHFRVPTGHSYNLDPESALLYQGPSGTLFGYSVVLHSHGTKRWLIVGAPTASWLANASVVNPGAIYRCRIGKNPNQICEQLQLGSPSGEPCGKTCLEERDNQWLGVTISRQPGENGSIVTCGHRWKNIFYMKNNNKLPTGVCYGMPSDLRTELSKRMAPCYQDFVRKFGENFASCQAGISSFYTQDLIVMGAPGSSYWTGSVFVYNITTNKYKAFVDRQNQVKFGSYLGYSVGAGHFRNPHTTEVVGGAPQHEQIGKAYIFSIDESELTIVYEMKGKKLGSYFGASVCAVDLNADGFSDLLVGAPMQSTIREEGRVFVYINSGMGAVMVEMERVLVGSDKYAARFGESMANLGDIDNDGFEDIAIGAPQEDDLRGAVYIYNGRVDGISSTYSQRIEGRQISQSLRMFGQSISGQIDADNNGYVDVAVGAFQSDSAVLLRTRPVVIVEASLSHPESVNRTKFDCTENGLLSVCVDLKLCFSYKGKEVPGYIVLFYNVSLDVHRKAESPSRFYFFSNGTSDMITRSIRVSSSGEKCRTHQAFMRKDVRDILTPIQVEATYHLGHHVITKRNTEEFPPLQPILQQKKEKDIIRKTINFARFCAYENCSADLQVSAKVGFLKPYENKTYLAVGSMKTIMLNVSLFNAGDDAYETTLNVQLPTGLYFIKILDLEEKQINCDVTESSGVVKLACSLGYIYVDRLSRVSIQHFHLLVGMCENEGKLDQVKDNRVTLVIPLRYEVMLAVHGFVTPTSFVYGSSEENEPEMCMAEKLNLTFHVINTGISMAPNVSVKIMVPNSFLPRNDKLFNVLDVQATMGQCQFEHYGRECALAQQKGIAGTLTDLVKFLSKTDKRLLYCMKADRHCLDFLCNFGKMESGKEASVHIQLEGRPSILEMDETSSLKFEIKATAFPEPHPKVIELNKDENIAHVYLEGLHHQRPKRHFTIVIVTISLLLGLIVLLLISCVMWKAGFFKRQYKSILQEENRRDSWSYVNSKSNDD
Protein: Guanylate-binding family protein (F4I2I5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Purple acid phosphatase 3
Sequence:
MRNPTDESGRAVQLVYVDENGKLKTDPEAIGALQKLKGPVAVVSLFGKALQGKSFIWNQLLSRSIGFEVQTLHRPCNGDIWMWIEPVKRISEDGTEYSLVLLDVELEDAKSIPATHNSQIFSLAILLSSVFIYGPTLGLNDIALDLSRLLEIRKQDHVGEAKDNTFFELGQFSPMFVQLMMDINSETVEGGEDVTQNSKLKKLRPLLLYGVDALMKFVSERVRPKQRGDTIVTGPPLAGFTKAFSENVNNNIVPKISSLWQTVEELEGRRARDTATEVYMSSLERSETPDESMLLEAHNKAVVEALTAFCESSIGNVEVKQKYKRDLWSFFAKALEDHKRVANVEAYSRCCNAIEDMGKKLWALPCSQDANIGDMIKALDTAVAEYEASINGPMKWQKLSSFLRESVQDILVHRRGNQMDELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYESAIDDICKLSDQFKNRINDLESKCKSIHDEHSNLMEVLGSTRLEASEWKRKYEGTLDENGVSNIRVGVDASITRCSNKLIDWKIKYENTVSEQKAVTEKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEELEKVCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAKSRIEGLERDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAKQNEEEVTKWQRIINAEKSKNIRENLMEKEDSFMVWDEATPMQRVKRLKVEAAVTCSGSDFAQETEEDSVSQESRKVRTMTPRRCTSSEAGATSSSTGTGHSKYTMKKLRTEILEHGFGAELVGLKNPRKRDLVQLYERTVLRK
Protein: Uncharacterized protein orf152 (Q2F970)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MWPSLQAHIWIWSTLFHPILIYFIPAIDSNSLFSNCTLKAKAKKDHINYSPNCRISHRIQMEDRKRRQFKPNGQTLRIQDRKTYSHKRITREQKQLHILLACLSDLLSNCHGSTTEDWLLRPSTRSWAIPDRQADGMDSLYMDGRNASTAEP
Protein: Endoplasmic reticulum transmembrane protein (Q8L702)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367026}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367026}.
Interaction partners:
Sequence:
MQQLLFAVVLFEVVVIMALSFKTPIRKLLIMSLDRSKRGRGPVVIQTVSATVIVLLVTSVYNMMGIQKRWIEDGVVNPTDEVIMAKHLLESTLMGGFLFLGLMIDRLHHYMRELRIRRKNMEVIKKEGALLEGVKARGLDEVKNLMEEITSLRKRQEQLDSELEARSKEIRTEKTSAVALQKQSEGFLIEFNRLLEENQVLRDQLHTVDSKLSRSSSKKNT
Protein: Lipopolysaccharide export system ATP-binding protein LptB (EC 7.5.2.-) (P0A9V1)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}; Cytoplasmic side {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Lipopolysaccharide export system permease protein LptF
- Lipopolysaccharide export system protein LptC
- Lipopolysaccharide export system permease protein LptG
- Lipopolysaccharide export system protein LptA
- LPS-assembly protein LptD
- LPS-assembly lipoprotein LptE
- Probable multidrug ABC transporter permease YbhS
- 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
- High-affinity branched-chain amino acid transport system permease protein LivM
- Arabinose 5-phosphate isomerase KdsD
Sequence:
MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDDDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFRL
Protein: Myb-like transcription factor 2 (Q8H266)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
NKGSWTAEEDRRLAKYIEIHGAKRWKTIAIKSGLNRCGKSCRLRWLNYLRPNIKRGNISDEEEDLIIRLHKLLGNRWSLIAGRLPGRTDNEIKNYWNSHLSKKMINHDVRTEQTSSSEQIVPHKAWETVQMEEEEVVKGSDEIENSEFSIDVDEFFD
Protein: MKIAA0897 protein (Q69ZW5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GPPHGADAEANFEQLMVNMLDEREKLLESLRESQETLVATQSRLQDALHERDQLQRHLNSALPQEFATLTRELSMCREQLLEREEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRAALERVTTLEEQLAGAHQQVSALQQGAGIRDGVAEEEGTVDLGPKRLWKDDTGRVEELQGLLEKQNYELSQARERLVTLSATVTELEEDLREALAQKEDMEERITTLEKRYLAAQREATSIHDLNDKLENELANKESLHRQCEEKARHLQELLEVAEQKLQQTMRKAETLPEVEAELSQRIAALTKAEERHGNIEEHLRQLEGQLEEKNQELARVRQREKMNEDHNKRLSDTVDRLLSESNERLQLHLKERMAALEEKGRLSEEIEKLRQEVDQLKGRGGPFVDGIHSRSHVGSAADVRFSLSTATHAPPGLHRRYSALRDESAKDWKPSPLPGVLGATTPAFDSDPEISDVDEDEPGGLVGTQVDVISPGGHSDAQTLAMMLQEQLDAINQEIRMIQEEKESTELRAEEIETRVTSGSMEALNLTQLRKRGSIPTSLTALSLASASPPLSGRSTPKLTSRSAAQDLDRMGVMTLPSDLRKHRRKLLSPVSREENREDKATIKCETSPPSSPRTLRLEKLGHPGLSQEEGKSALEGQDSNPSSSNSSQDSLHKGAKRKGIKSSIGRLFGKKEKGRLIQLSRDATGHVLLTDSELSLQEPMVPAKLGTQAEKDRRLKKKHQLLEDARRKGMPFAQWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNALHRLKLRLAIQEMVSLTSPSAPPTSRTSSGNVWVTHEEMETLATSTKTTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELEKRREESQHEIKDVLVWTNDQVVHWVQSIGLRDYAGNLHESGVHGALLALDENFDHNTLALVLQIPTQSTQARQVMEREFNNLLALGTDRKLDDGEEKVFRRAPSWRKRFRPRDHHSGGMLGTSAETLPAGFRVSTLGPLQPPPAPPKKIMPEAHSHYLYGHMLSAFRD
Protein: Fanconi anemia complementation group G isoform 1 (Fanconi anemia, complementation group G) (cDNA, FLJ93448, Homo sapiens Fanconi anemia, complementation group G (FANCG), mRNA) (Q53XM5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRQTTSVGSSCLDLWREKNDRLVRQAKVAQNSGLTLRRQQLAQDALEGLRGLLHSLQGLPAAVPVLPLELTVTCNFIILRASLAQGFTEDQAQDIQRSLERVLETQEQQGPRLEQGLRELWDSVLRASCLLPELLSALHRLVGLQAALWLSADRLGDLALLLETLNGSQSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQFLIEVELLLPPPDLASPLHCGTQSQTKHILASRCLQTGRAGDAAEHYLDLLALLLDSSEPRFSPPPSPPGPCMPEVFLEAAVALIQAGRAQDALTLCEELLSRTSSLLPKMSRLWEDARKGTKELPYCPLWVSATHLLQGQAWVQLGAQKVAISEFSRCLELLFRATPEEKEQGAAFNCEQGCKSDAALQQLRAAALISRGLEWVASGQDTKALQDFLLSVQMCPGNRDTYFHLLQTLKRLDRRDEATALWWRLEAQTKGSHEDALWSLPLYLESYLSWIRPSDRDAFLEEFRTSLPKSCDL
Protein: Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A (PP6-ARS-A) (Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A) (Ankyrin repeat domain-containing protein 28) (Phosphatase interactor targeting protein hnRNP K) (PITK) (O15084)
Organism: Homo sapiens (Human)
Function: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK phosphorylation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:16564677}. Note=Seems to be excluded from nucleoli.
Interaction partners:
- Serine/threonine-protein phosphatase 6 catalytic subunit
- Serine/threonine-protein phosphatase 6 regulatory subunit 3
- Serine/threonine-protein phosphatase 6 regulatory subunit 1
- Serine/threonine-protein phosphatase 6 regulatory subunit 2
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B
- Dedicator of cytokinesis protein 1
- Ubiquitin carboxyl-terminal hydrolase 10
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Sequence:
MAFLKLRDQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILATMMPVSSSSPLSSLTFNAINRYTNTSKTVSFEALPIMRNEPSSYCSFNNIGGEQEYLYTDVDELNDSDSETY
Protein: Voltage-dependent calcium channel gamma-1 subunit (Dihydropyridine-sensitive L-type, skeletal muscle calcium channel subunit gamma) (O70578)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics.
Subcellular location: Cell membrane, sarcolemma {ECO:0000305|PubMed:10799530, ECO:0000305|PubMed:9504716}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19518}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent calcium channel gamma-4 subunit
- Voltage-dependent calcium channel gamma-7 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent calcium channel subunit alpha-2/delta-4
- Voltage-dependent L-type calcium channel subunit alpha-1F
Sequence:
MSQTKTAKVRVTLFFILVGGVLAMVAVVTDHWAVLSPHLEHHNETCEAAHFGLWRICTARVAVHNKDKSCEHVTPSGEKNCSYFRHFNPGESSEIFEFTTQKEYSISAAAIAIFSLGFIIVGSICAFLSFGNKRDYLLRPASMFYAFAGLCLIVSVEVMRQSVKRMIDSEDTVWIEHYYSWSFACACAAFILLFLGGLFLLLFSLPRMPQNPWESCMDAEPEH