wanglab/gogpt-training-data huggingface dataset:
Protein: Toll-like receptor 9 (CD antigen CD289) (Q5I2M5)
Organism: Bos taurus (Bovine)
Function: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Upon CpG stimulation, induces B-cell proliferation, activation, survival and antibody production (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9EQU3}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9EQU3}. Endosome {ECO:0000250|UniProtKB:Q9EQU3}. Lysosome {ECO:0000250|UniProtKB:Q9EQU3}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9EQU3}. Note=Relocalizes from endoplasmic reticulum to endosome and lysosome upon stimulation with agonist. Exit from the ER requires UNC93B1. Endolysosomal localization is required for proteolytic cleavage and subsequent activation. Intracellular localization of the active receptor may prevent from responding to self nucleic acid. {ECO:0000250|UniProtKB:Q9EQU3}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- TIR domain containing adaptor protein
- High mobility group protein B1
- Toll-like receptor 4
- Toll-like receptor 2
- TIR domain-containing adapter molecule 2
- Toll-like receptor 9
- Unc-93 homolog B1, TLR signaling regulator
- Interleukin-1 beta
- Interferon gamma
Sequence:
MGPYCAPHPLSLLVQAAALAAALAEGTLPAFLPCELQPHGQVDCNWLFLKSVPHFSAGAPRANVTSLSLISNRIHHLHDSDFVHLSNLRVLNLKWNCPPAGLSPMHFPCRMTIEPNTFLAVPTLEELNLSYNGITTVPALPSSLVSLSLSHTSILVLGPTHFTGLHALRFLYMDGNCYYMNPCPRALEVAPGALLGLGNLTHLSLKYNNLTEVPRRLPPSLDTLLLSYNHIVTLAPEDLANLTALRVLDVGGNCRRCDHARNPCRECPKNFPKLHPDTFSHLSRLEGLVLKDSSLYKLEKDWFRGLGRLQVLDLSENFLYDYITKTTIFNDLTQLRRLNLSFNYHKKVSFAHLHLASSFGSLVSLEKLDMHGIFFRSLTNITLQSLTRLPKLQSLHLQLNFINQAQLSIFGAFPSLLFVDLSDNRISGAATPAAALGEVDSRVEVWRLPRGLAPGPLDAVSSKDFMPSCNLNFTLDLSRNNLVTIQQEMFTRLSRLQCLRLSHNSISQAVNGSQFVPLTSLRVLDLSHNKLDLYHGRSFTELPQLEALDLSYNSQPFSMQGVGHNLSFVAQLPSLRYLSLAHNGIHSRVSQKLSSASLRALDFSGNSLSQMWAEGDLYLCFFKGLRNLVQLDLSENHLHTLLPRHLDNLPKSLRQLRLRDNNLAFFNWSSLTVLPRLEALDLAGNQLKALSNGSLPPGIRLQKLDVSSNSIGFVIPGFFVRATRLIELNLSANALKTVDPSWFGSLAGTLKILDVSANPLHCACGAAFVDFLLERQEAVPGLSRRVTCGSPGQLQGRSIFTQDLRLCLDETLSLDCFGLSLLMVALGLAVPMLHHLCGWDLWYCFHLCLAHLPRRRRQRGEDTLLYDAVVVFDKVQSAVADWVYNELRVQLEERRGRRALRLCLEERDWLPGKTLFENLWASVYSSRKTMFVLDHTDRVSGLLRASFLLAQQRLLEDRKDVVVLVILRPAAYRSRYVRLRQRLCRQSVLLWPHQPSGQGSFWANLGIALTRDNRHFYNRNFCRGPTTAE
Protein: phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC 3.1.3.95) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (A0A8I5Y8V2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MGEEGPPSLEYIQAKDLFPPKELVKEEENLQVPFTVLQGEGVEFLGRAADALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHIACKDSKVVRCHFSTFKQCQEWLSRLSRATARPAKPEDLFAFAYHAWCLGLTEEDQHTHLCQPGEHIRCRQEAELARMGFDLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIAKACALDPGTRASGGSLSAGTNDASEACDTDFDSSLTACSGVESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVVFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENAEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVLHPVCHVRALHLWTAVYLPASSPCTLGEENMDLYLSPVAQSQEFSGRSLDRLPKTRSMDDLLSACDTSSPLTRTSSDPNLNNHCQEVRVSLEPWHSNPEGAEAVIESGVGSPQLTVGDVGLPPPLPSSQKDYLSNKPFKGHKSCSLSYKLLNTSVSWEMKNTSEIKVLEETEALAPGPPAREEQSRTSDGLGKPPEQCPEKEATSSLSNVSSKCGGACDFPGEPPQDSFTGTPQQPHLDSMQAVPIRCTPDHGQGSLCNPPSAASQTLQEPNTDLISQDPPGSMAGISYQEQPSSVSDLIYKKEDAGKRGSKNGQLVENPRFGKMPLELARKPISQSQISEFSFLGSNWDSFQGMMTSFPSGETTPRRLLAYGCCSKRPSNKHIRAAAPCFGGQWAQREGMKSPVCSSHSNGHCTGPGGKNNRMWFSSHPKQVSSTKPSLLSCPSPVPPLYLDDDGLPFPTDVIQHRLRQIEAGYKQEVEQLRRQVRELQMRLDIRHCCAPPAEPPMDYEDDFTCLKESDGSDTEDFGSDHSEDCLSEASWEPVDKKETEVTRWVPDHMASHCYNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHIQVSRARELMSQHLKKPIATASS
Protein: Isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Q6FXL1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- NAD-specific glutamate dehydrogenase
- Glutamate synthase
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- Glutamate dehydrogenase
- Aspartate aminotransferase
Sequence:
MSKVKVVNPIVEMDGDEQTRIIWHLIREKLILPFLDVDLKYYDLSIEYRDETNDKVTEDSALATLKYGVAVKCATITPDEARVEEFNLKEMWKSPNGTIRNILGGTVFREPIVIPRIPKLVPQWKEPIIIGRHAFGDQYRATDVVIPDEGEVRLVYKSKDGKTDIDIPVYNFPKEGGVAMMMYNTTESIRGFARASFNMALEHEMPLYSTTKNTILKKYDGKFKDTFESMYEAEYKEQFEAKGIWYEHRLIDDMVAQMLKSKGGFIIAMKNYDGDVESDIVAQGFGSLGLMTSVLISPDGKTFESEAAHGTVTRHYRQHQQGKETSTNSIASIFAWTRGIIQRGKLDETADVVKFGELLERATVDTVQEDGIMTKDLALILGKTDRSAYVTTEEFIDAVENRIKSEFQKNF
Protein: Serine/threonine-protein kinase 33 (EC 2.7.11.1) (Q924X7)
Organism: Mus musculus (Mouse)
Function: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29155043}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29155043}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16176263}. Note=Colocalizes with the caudal end of the manchette, a transient structure that guides tail elongation in elongating spermatids. {ECO:0000269|PubMed:29155043}.
Interaction partners:
Sequence:
MADPSLNDNPTACPHCASSQAGLLCVCPAGKSPVLVVEMSQTSSIGSTEFFASQERKKERNTSRESSLKDLSIRTSNVERKPQAQWSRSNVTVGKIPHIRMDDGAGIEEFYTFGRILGQGSFGMVFEAIDKETGAKWAIKKVNKEKAGSSAMKLLEREVSILKTVNHQHIIHLEQVFESPQKMYLVMELCEDGELKAVMDQRGHFSENETRLIIQSLASAIAYLHNKDIVHRDLKLENIMVKSSFIDDNNEMNLNIKVTDFGLSVQKHGSRSEGMMQTTCGTPIYMAPEVINAHDYSQQCDIWSIGVIMFILLCGEPPFLANSEEKLYELIKKGELRFENPVWESVSDSAKNTLKQLMKVDPAHRITAKELLDNQWLTGNTLSSARPTNVLEMMKEWKNNPESDEETNTDEETEQSAVYSPSANTAKQPTNAAKKPAAESVGMTSSNSSSSKLLSAESKAEPEKSSETVGHASVAKTTLKSTTLFRGKKRL
Protein: Interferon gamma 2 (B6UQB7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDVLSRAVMCFCLMGWMTLGWSNAAQYTSINMKRNIDKLKVHYKISKDQLFNGNPVFPKDTFEDSEQRVLMSVVLDVYLSIFSQMLNQTGDQEVRERLDQVKGKVQETQKHYFLGRVPELRTHLQNLWAIKTSDTTVQGKALSEFITIYEKASKLAHEIHLKKDNRRKRRQAQRLKSHIM
Protein: Angiogenin-4 (EC 3.1.27.-) (Q3TMQ6)
Organism: Mus musculus (Mouse)
Function: Has bactericidal activity against E.faecalis and L.monocytogenes, but not against L.innocua and E.coli. Promotes angiogenesis (in vitro). Has low ribonuclease activity (in vitro). Promotes proliferation of melanoma cells, but not of endothelial cells or fibroblasts (in vitro).
Subcellular location: Secreted {ECO:0000269|PubMed:12548285}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:12548285}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P03950}. Note=Exposure to bacterial lipopolysaccharide (LPS) triggers secretion from intestinal epithelium cells (PubMed:12548285). Rapidly endocytosed by target cells and translocated to the nucleus where it accumulates in the nucleolus and binds to DNA (By similarity). {ECO:0000250|UniProtKB:P03950, ECO:0000269|PubMed:12548285}.
Interaction partners:
- Angiogenin-2
- Angiogenin ribonuclease 6
- Regenerating islet-derived protein 3-gamma
Sequence:
MTMSPCPLLLVFVLGLVVIPPTLAQNERYEKFLRQHYDAKPNGRDDRYCESMMKERKLTSPCKDVNTFIHGTKKNIRAICGKKGSPYGENFRISNSPFQITTCTHSGASPRPPCGYRAFKDFRYIVIACEDGWPVHFDESFISP
Protein: HORMA domain-containing protein 2 (Q8N7B1)
Organism: Homo sapiens (Human)
Function: Essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes. Required for the DNA double-strand break-independent, BRCA1-dependent activation of ATR on the sex chromosomes that is essential for normal sex body formation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:22893617}. Chromosome {ECO:0000250}. Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the male and female prophase I stage of meiosis. TRIP13 is required for depletion from synapsed chromosomes (By similarity). {ECO:0000250}.
Interaction partners:
- Synaptonemal complex protein 3
- MutS protein homolog 4
- Meiotic recombination protein SPO11
- Meiotic recombination protein REC8 homolog
- Synaptonemal complex protein 1
- MutS protein homolog 5
- Synaptonemal complex protein 2
- Pachytene checkpoint protein 2 homolog
- Structural maintenance of chromosomes protein 3
- Synaptonemal complex central element protein 1
Sequence:
MATAQLSHCITIHKASKETVFPSQITNEHESLKMVKKLFATSISCITYLRGLFPESSYGERHLDDLSLKILREDKKCPGSLHIIRWIQGCFDALEKRYLRMAVLTLYTDPMGSEKVTEMYQFKFKYTKEGATMDFDSHSSSTSFESGTNNEDIKKASVLLIRKLYILMQDLEPLPNNVVLTMKLHYYNAVTPHDYQPLGFKEGVNSHFLLFDKEPINVQVGFVSTGFHSMKVKVMTEATKVIDLENNLFRENSTTEIAHQGLDCDEEEECNDHIQRMNFVCSQQSSECSRKKRKVSEPVKVFIPNRK
Protein: Nitrogen regulatory protein P-II (PII signal transducing protein) (P0A3F4)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
Interaction partners:
- PipX
- Acetylglutamate kinase
- Ammonium transporter
- Ammonium transporter
- Global nitrogen regulator
- ADP-ribosylglycohydrolase-like
- Glutamine synthetase
Sequence:
MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQKGQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAARTGEIGDGKIFVSPVDQTIRIRTGEKNADAI
Protein: Fatty acid desaturase, putative (Q587G0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Fatty acid desaturase, putative
- very-long-chain
- Fatty acid elongase 1
- Short-chain dehydrogenase, putative
- Putative enoyl-CoA reductase
- Cytochrome b5, putative
- Cytochrome b5, putative
Sequence:
MLPKQQMGGSVCNASIETVNTEATDPSEAKKIVLNAGRSEKVNVYVPPSTLMVRDIQEQIPAEYFQRSMWRSFSYLSRDMFQLFLTFVIMYNFVLPMLDSSLLNAVPPVAWLSRAAAWMIYWFIQGLNGTALWVLAHECGHQAFCNSRRVNNAVGMILHSALLVPYHSWRLTHGTHHKHTNHLTKDLVFVPVQRSAVGEAVEEAPIVMLWNMALMFLFGWPMHLLVNVGGQKFDRFTSHFDPNAPFFRRADYNNVMVSNMGVLLTLSILGACSWSFGFAVVVRWYLIPYLWVNFWLVYITYMQHSDVRLPHYTHDHWTYVRGAVAAVDRDFGPLLNSWLHHINDSHVVHHLFSQMPHYNAIEVTRKHIRDILGDLYVTDAKPLLKSLVHTWRECRYVVPSEGICIYRS
Protein: Glutathione reductase (GR) (GRase) (GSR) (EC 1.8.1.7) (Q8T137)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Maintains high levels of reduced glutathione (GSH) in the cytosol by reducing glutathione disulfide (oxidized glutathione or GSSG). The amount of GSH may affect the determination of cell fate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glutathione synthetase
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Thioredoxin reductase
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Glutamate--cysteine ligase
- Glutathione S-transferase
- Glutathione S-transferase
- Glutathione transferase
Sequence:
MSSTNHFTYLVLGAGSGGIASARRAAKHLNAKGNGDRIGIVEVTRPGGTCVNVGCVPKKVMWNTSFIKEMINAAPSYGFDFGGQQVKFNWPTIKKARDEYIKRLNGIYDSNLAKDNIVRINGYGRFSGPKEIQVNGANGEKYTADHILIAAGGRPTVPDVPGKELGITSDGFFELEDLPKSTLVVGAGYIAVELAGVLHSLGSETTMVIRQKQFLRTFDEMLHTTLLKQMTDDGVKFVTEASIKSLERDVDGKRIIATTNAGVKLPPVECVIWAIGRVPNTDDLGIDKAGIQLTEQSGFIKVDEFQNTNVPGVHAVGDICGNFLLTPVAIAAGRRLSERLFNGKSDLKFEYENVATVVFSHPPIGTVGLTEQEAITKYGTENIKCYNTSFINMFYSVQVHKVRTSMKLVCLGKEEKVIGLHIIGDGCDEIIQGFAVAVKMGCTKWDLDNTCAIHPTSAEELVTMV
Protein: Extensin-3 (AtExt3) (AtExt5) (Extensin-3/5) (Protein ROOT-SHOOT-HYPOCOTYL-DEFECTIVE) (Q9FS16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Structural component which strengthens the primary cell wall. Forms dendritic structures indicating a propensity for self-assembly through tyrosine cross-linking. Forms intermolecular cross-links exclusively by pulcherosine (three Tyr). Scaffold formation requires an unobstructed C-terminus of EXT3. Required for the correct positioning of the cell plate during cytokinesis in cells of the developing embryo. Extensins contain a characteristic repeat of the pentapeptide Ser-Pro(4). For this particular extensin, a typical repeat of Ser-Pro(3) is found.
Subcellular location: Secreted, primary cell wall {ECO:0000269|PubMed:12034904}.
Interaction partners:
- Leucine-rich repeat extensin-like protein 1
- Proline-rich extensin-like family protein
- Arabinosyltransferase XEG113
- Hydroxyproline O-arabinosyltransferase 3
- Pentatricopeptide repeat-containing protein At4g19191
- Extensin-like protein
- Hydroxyproline O-arabinosyltransferase 1
- Extensin-2
- Leucine-rich repeat extensin-like protein 6
- Leucine-rich repeat extensin-like protein 2
Sequence:
MGSPMASLVATLLVLTISLTFVSQSTANYFYSSPPPPVKHYTPPVKHYSPPPVYHSPPPPKKHYEYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKKHYVYKSPPPPVKHYSPPPVYHSPPPPKEKYVYKSPPPPPVHHYSPPHHPYLYKSPPPPYHY
Protein: Transcriptional enhancer factor TEF-5 (DTEF-1) (TEA domain family member 3) (TEAD-3) (Q99594)
Organism: Homo sapiens (Human)
Function: Transcription factor which plays a key role in the Hippo signaling pathway, a pathway involved in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein MST1/MST2, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Acts by mediating gene expression of YAP1 and WWTR1/TAZ, thereby regulating cell proliferation, migration and epithelial mesenchymal transition (EMT) induction. Binds to multiple functional elements of the human chorionic somatomammotropin-B gene enhancer.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional coactivator YAP1
- WW domain-containing transcription regulator protein 1
- Transcription cofactor vestigial-like protein 4
- Transcription cofactor vestigial-like protein 1
- Transcription factor 7-like 2
- Transcription factor 7
- Transcription factor 7-like 1
- Lymphoid enhancer-binding factor 1
- Chorionic somatomammotropin hormone 2
- Calsenilin
Sequence:
MASNSWNASSSPGEAREDGPEGLDKGLDNDAEGVWSPDIEQSFQEALAIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARKKVREYQVGIKAMNLDQVSKDKALQSMASMSSAQIVSASVLQNKFSPPSPLPQAVFSTSSRFWSSPPLLGQQPGPSQDIKPFAQPAYPIQPPLPPTLSSYEPLAPLPSAAASVPVWQDRTIASSRLRLLEYSAFMEVQRDPDTYSKHLFVHIGQTNPAFSDPPLEAVDVRQIYDKFPEKKGGLKELYEKGPPNAFFLVKFWADLNSTIQEGPGAFYGVSSQYSSADSMTISVSTKVCSFGKQVVEKVETEYARLENGRFVYRIHRSPMCEYMINFIHKLKHLPEKYMMNSVLENFTILQVVTSRDSQETLLVIAFVFEVSTSEHGAQHHVYKLVKD
Protein: Serine/threonine-protein kinase pim-1 (EC 2.7.11.1) (P06803)
Organism: Mus musculus (Mouse)
Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B, induces 14-3-3 binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (By similarity). Promotes brown adipocyte differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1825810}. Nucleus {ECO:0000269|PubMed:1825810}. Cell membrane {ECO:0000269|PubMed:1825810}. Note=Mainly located in the cytoplasm.
Interaction partners:
- Serine/threonine-protein kinase pim-2
- Suppressor of cytokine signaling 1
Sequence:
MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK
Protein: 60S ribosomal protein L21 (Q9V9M7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS13
- GEO07453p1
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS7A
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS4
Sequence:
MTNSKGYRRGTRDMFSRPFRKHGVIPLSTYMRVFKIGDIVDIKGHGAVQKGLPYKAYHGKTGRIFNVTQHAVGVIVNKRVRGKILAKRVNVRIEHIHHSKCREDFLRRVKENERLLKEAKEKGQWVSLKRQPEQPKKAHFVKKLEEPIALAPIPYEFIA
Protein: Pro-cathepsin H (Cathepsin B3) (Cathepsin BA) [Cleaved into: Cathepsin H mini chain; Cathepsin H (EC 3.4.22.16); Cathepsin H heavy chain; Cathepsin H light chain] (P49935)
Organism: Mus musculus (Mouse)
Function: Important for the overall degradation of proteins in lysosomes.
Subcellular location: Lysosome.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Napsin-A
- Pulmonary surfactant-associated protein B
- Surfactant protein C
- Cystatin-A
- Toll-like receptor 4
Sequence:
MWAALPLLCAGAWLLSTGATAELTVNAIEKFHFKSWMKQHQKTYSSVEYNHRLQMFANNWRKIQAHNQRNHTFKMALNQFSDMSFAEIKHKFLWSEPQNCSATKSNYLRGTGPYPSSMDWRKKGNVVSPVKNQGACGSCWTFSTTGALESAVAIASGKMLSLAEQQLVDCAQAFNNHGCKGGLPSQAFEYILYNKGIMEEDSYPYIGKDSSCRFNPQKAVAFVKNVVNITLNDEAAMVEAVALYNPVSFAFEVTEDFLMYKSGVYSSKSCHKTPDKVNHAVLAVGYGEQNGLLYWIVKNSWGSQWGENGYFLIERGKNMCGLAACASYPIPQV
Protein: COP9 signalosome complex subunit 4 (SGN4) (Signalosome subunit 4) (JAB1-containing signalosome subunit 4) (Q68FS2)
Organism: Rattus norvegicus (Rat)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By similarity). Also involved in the deneddylation of non-cullin subunits such as STON2 (By similarity). The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BT78}. Nucleus {ECO:0000250|UniProtKB:Q9BT78}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:21102408}.
Interaction partners:
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 1
- COP9 signalosome subunit 7B
- COP9 signalosome subunit 7A
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
Sequence:
MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGTEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEVYHFTLEKVQPRVISFEEQVASIRQRLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
Protein: ABC transporter, white homologue (Q9EPG9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MACLMAAFSVGTAMNASNYSAAMTEPKSVCVSVDEVVSSNVDELETDLLNGHLKKVDNNFTEAQRFSSLPRRAAVNIEFKDLSYSVPEGPWWRKKGYKTLLKGISGKFNSGELVAIMGPSGAGKSTLMNILAGYRETGMKGAVLINGMPRDLRCFRKVSCYIMQDDMLLPHLTVQEAMMVSAHLKLQERDEGRREMVKEILTALGLLPCANTRTGSLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKGLAQGGRSIVCTIHQPSAKLFELFDQLYVLSQGQCVYRGKVSNLVPYLRDLGLNCPTYHNPADFVMEVASGEYGDQNSRLVRAVREGMCDSDYKRELGGDGDVNPFLWHRPAEEDSASMEGCHSFSASCLTQFCILFKRTFLSIMRDSVLTHLRITSHIGIGLLIGLLYLGIGNEAKKVLSNSGFLFFSMLFLMFAALMPTVLTFPLEMSVFLREHLNYWYSLKAYYLAKTMADVPFQIMFPVAYCSIVYWMTSQPSDAVRFVLFAALGTMTSLVAQSLGLLIGAASTSLQVATFVGPVTAIPVLLFSGFFVSFDTIPTYLQWMSYISYVRYGFEGVILSIYGLDREDLHCDIAETCHFQKSEAILRELDVENAKLYLDFIVLGIFFISLRLIAYFVLRYKIRAER
Protein: Protein wntless homolog (Wnt ligand secretion mediator) (F2Z4U3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}.
Interaction partners:
- Protein Wnt
- Protein Wnt
- Protein Wnt-5b
- Protein Wnt-8a
- Protein Wnt-4a
- Sorting nexin-3
- Protein Wnt
- Protein Wnt
- Protein Wnt-1
- Protein Wnt
Sequence:
MAGAIIENMSTKKLVILGVILMLFQAFSFMVGGLIAPSPTAAVSYLATKCVDNEKTHHKNPKWFTPWGPDQCSKIKDFDEAMVKKIEANNIVFAIHIPPPNTEMSTWFQFLLLILHFDIAFKIQNQIADGASITIDVRLAYRDDKLSEWTQMAHSVEQRKLSCNFTAAKTIENEGRLYDCDLLPFMELGSVAHKYYLLNVRLPVNERKKVNIGIGEINDMRLVGIHQNGGFTKVWFAMKTFLTPSVLIIMIWYWKRITQMTRPPVLLEKVIFALGISMTFINIPVEWFSVGFDWTWMLLFGDIRQGIFYAMLLSFWIIFCGEHLMDQTERNRFSVYWKQVIPIVFGSFCLFIFDMCERGVQLKNPFYSIWASDVGTELAMAFIIVAGICACLYFLFLCFMVFQVFRNISGKRSCLPAMTKARRLHYEGLIFRFKFLMLVTLACAAMTVIFFIISQVSEGHWLWGGHTVQVNSAFFTGIYGMWNLYVFALMFLYAPSHKRYGDEQSSADQAGNSGEDTQLTTTITHVDGPTEIYKMTGKEAQE