wanglab/gogpt-training-data huggingface dataset:
Protein: LIM domain and actin-binding protein 1 (Epithelial protein lost in neoplasm) (mEPLIN) (Q9ERG0)
Organism: Mus musculus (Mouse)
Function: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By similarity). Plays a role in cholesterol homeostasis. Influences plasma cholesterol levels through regulation of intestinal cholesterol absorption. May act as a scaffold protein by regulating NPC1L1 transportation, an essential protein for cholesterol absorption, to the plasma membrane by recruiting MYO5B to NPC1L1, and thus facilitates cholesterol uptake.
Subcellular location: Cytoplasm. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:17875928}. Cell membrane {ECO:0000269|PubMed:29880681}. Cell projection, ruffle {ECO:0000269|PubMed:17875928}. Note=Expressed mainly in the brush border membrane of the small intestine and colocalizes with NPC1L1 and MYO5B (PubMed:29880681). Colocalizes with PXN at focal adhesions in mesangial cells (By similarity). Colocalizes with actin stress fibers in quiescent cells. PDGF stimulation induced disassembly of stress fibers and formation of peripheral and dorsal ruffles, where LIMA1 is relocalized (PubMed:17875928). {ECO:0000250|UniProtKB:Q9UHB6, ECO:0000269|PubMed:17875928, ECO:0000269|PubMed:29880681}.
Interaction partners:
- Catenin beta-1
- Catenin delta-1
- Cadherin-1
- Vinculin
- Catenin alpha-1
- Baculoviral IAP repeat-containing protein 3
- Baculoviral IAP repeat-containing protein 2
Sequence:
MESTPFNRRQWTSLSLRVTAKELSLVNKNKSSAIVEIFSKYQKAAEEANMERKKNNPESLPQHFRRGTLSVLKKKWENPVAGAEFHTDSLPNSSSEGGHTADYPPAEVTDKPAPGVRADREEHTQPKPRFGSRPEAVIQSRYPRSENSHDFKAQATESQKMENCLGDSRHEAEKPETSENTETSGKIEKYNVPLNRLKMMFEKGEHNQTKSLWTQSRNAGGRRLSENNCSLDDWEIGAGHLSSSAFNSEKNESKRNLELPRLSETSIKDRMAKYQAAVSKQSSPASYTNELKTSESKTHKWEQKENVPPGPEACSVHQEGSKVSTTENSLVALSVPAEDDTCNSQVKSEAQQPMHPKPLSPDARTSSLPESSPSKTAKKFQAPAKESCVECQKTVYPMERLLANQQVFHISCFRCSYCNNKLSLGTYASLHGRIYCKPHFNQLFKSKGNYDEGFGHKQHKDLWASKSDNEETLGRPAQPPNAGESPHSPGVEDAPIAKVGVLAASMEAKASSQREREDKPAETKKLRIAWPPPAELGGSGSALEEGIKVSKPKWPPEDDVCKTEAPEDVDLDLKKLRRSSSLKERSRPFTVAASFRTSSIKSPKASSPSLRKGWSESEQSEEFGGGIATMERKQTENARPSGEKENVGKSRWQGEEVPRSKDRSSFELESENFMENGANIAEDDNHVHAQQSPLEPEAPGWSGFVDTTAAKEFTTQNQKSQDVGFWEGEVVRELSVEEQIKRNRYYDEDEDEE
Protein: Protein NLP2 (AtNLP2) (NIN-like protein 2) (Nodule inception protein-like protein 2) (Q7X9B9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00852}.
Interaction partners:
- MOB kinase activator-like 1B
- Putative MOB kinase activator-like 2B
- MOB kinase activator-like 2A
- Rop guanine nucleotide exchange factor 14
- Protein RKD5
- Protein RKD1
- MOB kinase activator-like 1A
- Protein RKD2
- Ypt/Rab-GAP domain of gyp1p superfamily protein
- Exportin-4
Sequence:
MEGGRGGGDGNFLPNSNFGVFSDSAMDMDFMDELLFDGCWLETTDGKSLKQTMGQQVSDSTTMNDNNNNSYLYGYQYAENLSQDHISNEETGRKFPPIPPGFLKIEDLSNQVPFDQSAVMSSAQAEKFLLEESEGGRRYWIAPRTSQGPSSSVKERLVQAIEGLNEEVQDKDFLIQIWLPIQQEGKNFLTTSEQPHFFNPKYSSLKRYRDVSVAYNFLADEDSKESVGLPGRVFLKKLPEWTPDVRFFRSEEYPRIKEAEQCDVRGSLALPVFERGSGTCLGVVEIVTTTQKMNYRPELDNICKALESVNLRSSRSLNPPSREFLQVYNEFYYAALPEVSEFLTLVCRVYDLPLALTWAPCARQGKVGSRHSDENFSECVSTVDDACIVPDHQSRHFLEACSEHHLLQGEGIVGKAFNATKLFFVPEVTTFSKTNYPLAHHAKISGLHAALAVPLKNKFNSSVEFVLEFFFPKACLDTEAQQDMLKSLSATLQQDFRSLNLFIDKELELEVVFPVREEVVFAENPLINAGTGEDMKPLPLEEISQEDSSWISHMIKANEKGKGVSLSWEYQKEEPKEEFMLTSGWDNNQIGSGHNNFLSEAEQFQKVTNSGLRIDMDPSFESASFGVGQTLLGSRRPGEKRRTKTEKTIGLEVLRQYFAGSLKDAAKSIGVCPTTLKRICRQHGITRWPSRKIKKVGHSLKKLQLVIDSVQGVQGSIQLDSFYTSFPELSSPHMSGTGTSFKNPNAQTENGVSAQGTAAAPKSPPSSSCSHSSGSSTCCSTGANQSTNTGTTSNTVTTLMAENASAILKRARSEVRLHTMNQDETKSLSRTLSHKTFSEHPLFENPPRLPENSSRKLKAGGASKVKATFGEAKVRFTLLPTWGFRELQHEIARRFNIDNIAPFDLKYLDDDKEWVLLTCEADLEECIDIYRSSQSRTIKISVHEASQVKLGGSFGSIGLGPSL
Protein: Haloalkane dehalogenase 2 (EC 3.8.1.5) (P9WMS1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Interaction partners:
- Haloalkane dehalogenase 3
- Haloalkane dehalogenase 1
- Probable zinc-type alcohol dehydrogenase
- Alcohol dehydrogenase B
- Probable alcohol dehydrogenase adh
- Probable alcohol dehydrogenase AdhA
- Magnesium transport protein CorA
Sequence:
MSIDFTPDPQLYPFESRWFDSSRGRIHYVDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFGYQIDEHARVIGEFVDHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPADTLAMKAFSRVMSSPPVQYAILRRNFFVERLIPAGTEHRPSSAVMAHYRAVQPNAAARRGVAEMPKQILAARPLLARLAREVPATLGTKPTLLIWGMKDVAFRPKTIIPRLSATFPDHVLVELPNAKHFIQEDAPDRIAAAIIERFG
Protein: Carbonic anhydrase-related protein (CARP) (Carbonic anhydrase VIII) (CA-VIII) (P35219)
Organism: Homo sapiens (Human)
Function: Does not have a carbonic anhydrase catalytic activity.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- 1,25-dihydroxyvitamin D
- Very low-density lipoprotein receptor
- Albumin
Sequence:
MADLSFIEDTVAFPEKEEDEEEEEEGVEWGYEEGVEWGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGPLPQGHEFELYEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPDPLLRDYWVYEGSLTIPPCSEGVTWILFRYPLTISQLQIEEFRRLRTHVKGAELVEGCDGILGDNFRPTQPLSDRVIRAAFQ
Protein: Triacylglycerol lipase 2 (EC 3.1.1.3) (Q67ZU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Triacylglycerol (TAG) lipase. May be involved for TAG storage breakdown during seed germination (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Small GTPase LIP1
- Receptor-like kinase LIP1
- Acyl carrier protein 3, mitochondrial
- Probable ubiquitin-conjugating enzyme E2 26
Sequence:
MAGSVMVPSVSIGLALSVLIFFALSLKTLEARGTFGRLAGQPPQRTAAGGICASSVHIFGYKCEEHDVVTQDGYILNMQRIPEGRAGAVAGDGGKRQPVLIQHGILVDGMSWLLNPADQNLPLILADQGFDVWMGNTRGTRFSRRHKYLNPSQRAFWNWTWDELVSYDLPAMFDHIHGLTGQKIHYLGHSLGTLIGFASFSEKGLVDQVRSAAMLSPVAYLSHMTTVIGDIAAKTFLAEATSILGWPEFNPKSGLVGDFIKAICLKAGIDCYDLVSVITGKNCCLNASTIDLFLANEPQSTSTKNMIHLAQTVRDKELRKYNYGSSDRNIKHYGQAIPPAYNISAIPHELPLFFSYGGLDSLADVKDVEFLLDQFKYHDIDKMNVQFVKDYAHADFIMGVTAKDVVYNQVATFFKRQA
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q59DQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MATIDGRPAQYGISLKQLRELMEHRGREGVMKIAENGGIHELCKKLYTSPNEGLSGSKADEEHRRETFGSNVIPPKPPKTFLTLVWEALQDVTLIILEVAALVSLGLSFYKPADEDAPVLQEEEEHHGWIEGLAILISVIVVVIVTAFNDYSKERQFRGLQNRIEGEHKFSVIRGGEVCQISVGDILVGDIAQVKYGDLLPADGCLIQSNDLKVDESSLTGESDHVKKGPDVDPMVLSGTHVMEGSGKMVVTAVGVNSQAGIIFTLLGAAVDEQEAEIKKMKKEAKRANKQKNLTGENDGRSQIKGSQAPSQRETVTSEITKSESEGNHLPQSSSSGAAETGHKKEKSVLQAKLTKLAIQIGYAGSTIAVLTVIILIIQFCIKTFVIDEKPWKNTYANNLVKHLIIGVTVLVVAVPEGLPLAVTLSLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQSYICEKLCKVLPTLSDIPQHVGNLITMGISVNSAYTSNIMAGHNPGDLPIQVGNKTECALLGFVQGLGVKYQSIRDEITEDKFTRVYTFNSVRKSMGTVIPRPNGGYRLYTKGASEIIMKKCAFIYGHEGTLEKFTRDMQERLIREVIEPMACDGLRTISVAYRDFVPGKAAINEVHIDGEPNWDDEENIMTNLTCLCVVGIEDPVRPEVPDAIRKCQRAGITVRMVTGDNINTARSIASKCGILRPNDDFLILEGKEFNRRIRDSNGDIQQHLIDKVWPKLRVLARSSPTDKYTLVKGIIDSTVSENREVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFSSIVKAVMWGRNVYDSIAKFLQFQLTVNVVAVIVAFIGACAVQDSPLKAVQMLWVNLIMDTLASLALATEFPTPDLLLRKPYGRTKPLISRTMMKNILGQALYQLIIIFGLLFVGDVILDIESGRGQELNAGPTQHFTIIFNTFVMMTLFNEINARKIHGQRNVIEGLLTNPIFYTIWIFTMISQVLIIQYGKMAFSTKALTLDQWLWCIFFGIGTLVWGQLITSVPTRKLPKILSWGRGHPEEYTDGMNLGEERFDSIDSDKKPRAGQILWIRGLTRLQTQIRVVNAFRQGLDARYGDHTNTSLAEVLRKQTSLSKRLSETSSIEYADNIPDELTIPEIDVERLSSHSHTETAV
Protein: Cathepsin Z-1 (EC 3.4.18.1) (G5EGP8)
Organism: Caenorhabditis elegans
Function: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Plays an essential role in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed. Probably, required for the degradation of the old cuticle.
Subcellular location: Secreted {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=In molting larvae, localizes in both the new and old cuticles, specifically at the interface where the old cuticle is being degraded before ecdysis (PubMed:14630920). Localizes to yolk granules in the developing oocyte (PubMed:16857685). {ECO:0000269|PubMed:14630920, ECO:0000269|PubMed:16857685}.
Interaction partners:
- ERGIC-53-like protein
- legumain
- Cystatin cpi-2
Sequence:
MRTFVLLLALCAICILASSAYGKVRKYSNRNRYNLKGCYKQTGRVFEHKRYDRIYETEDFDSEDLPKTWDWRDANGINYASADRNQHIPQYCGSCWAFGATSALADRINIKRKNAWPQAYLSVQEVIDCSGAGTCVMGGEPGGVYKYAHEHGIPHETCNNYQARDGKCDPYNRCGSCWPGECFSIKNYTLYKVSEYGTVHGYEKMKAEIYHKGPIACGIAATKAFETYAGGIYKEVTDEDIDHIISVHGWGVDHESGVEYWIGRNSWGEPWGEHGWFKIVTSQYKNAGSKYNLKIEEDCVWADPIV
Protein: OBG-type G domain-containing protein (Q380Z6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYSYFCFSSMQVQDKKIHLNIMVKVLCLHGFGQTGEIFEHQLNRLCVKLSSVAEFDFVDAPYPLPHDHTGSNSIATYSWCRQPCGEEPSEADDDYSIGDAVVKRHMAAEGMRYDVILGFSQGGLVAARYVMLRELHGGDGYGPPLKGLILAATPDPRRTFPGLASAFKDSARYDAENDGFLGPLPSLHIVGRKDGVVDPAESASFADACRPHADVLWHEHAHSFPTLQNIVMSLKSFFERIAQRNPGNDGGDSTLTAACEEELEMISCVYGEECVHRGKMTTVSLPLLLNCADGDLEGSPLAALRLCVALSKGYPAEIPKFDIVGGPSNHHVFYERWRAKLVSDTTAFMREGPEGKSGMLLPAIMFTGEQAVGALDFLKSVFAEGGEMHDSAGVATGEQWKERKVNDWLWEEDDSEGARSACIAESHRRAQEVLAGGSPSFRPYGRGDCEGGGCYDAGGRGRSLEFTIGLIGKPSAGKSTFYNAVTNPDNESKAARVAAFPFTTIDPNVGCGFGPIFCPCSLSQPSPSSTGQCGAKYGHVTTFGAPHRRHPIVVKDVAGLVQGAYRGKGKGNRFLNDLCDADVLVHIVDGAGATYADGSACAPGEGSTFDDIMWVRGELHSWIYDNLRAQWAAVVRKPLKIRTVFTGYHSPPSSIDALLRCLGISTEVELVRRLPAWGAAELHLLVATFVHLRFPIVVALNKADMRCAADKLICTLKERYPNETLVQMSAKMECNLLFLRQVGAVRYVPGDHSFEEVDGAPANVTDAVRKRAMKALVELREFFSPMHPDTTTGVQAVLAAALSLCPGHLVYPVDAIERPLNSFPHCFPFKGGTCAGEVFDALLRSNLLDGKLVRFEAVDTKYLVEGGEVSVLKRDTVLPGRHVVVRVLSTKRHLVAQKREGKECMLGVGPKV
Protein: Enolase (PfEN) (EC 4.2.1.11) (W7JLR6)
Organism: Plasmodium falciparum (isolate NF54)
Function: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as parasite development and invasion. Plays an essential role during ookinete invasion of the mosquito vector midgut by mediating the interaction of the ookinete with the midgut epithelium and, further, by binding to mammalian host plasminogen in the blood meal, whose conversion to active plasmin promotes the invasion process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19642995}. Nucleus {ECO:0000250|UniProtKB:Q8IJN7}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19642995}. Cell surface {ECO:0000269|PubMed:21949403}. Cell membrane {ECO:0000250|UniProtKB:Q7RA60}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7RA60}. Vacuole {ECO:0000250|UniProtKB:Q8IJN7}. Note=Partially localizes to the nucleus in rings and trophozoites. Localization to the nucleus and food vacuole is higher in early and mid-stage trophozoites compared to the late-stage trophozoites and schizonts (By similarity). In the nucleus, localizes to heterochromatin region (By similarity). In rings, nuclear localization is dependent on the actin cytoskeleton (By similarity). Localizes to the cell surface of merozoites (By similarity). In gametocytes, predominantly localizes to the actin cytoskeleton (PubMed:19642995). In the trophozoite food vacuole, colocalizes with hemozoin, a product of heme detoxification (By similarity). In sporozoites, localizes to punctate structures beneath the cell membrane (By similarity). Localizes to the cell surface of ookinetes, especially on the apical pellicle complex that is involved in invasion (PubMed:21949403). When phosphorylated at Thr-339, localizes to the cytoskeleton (By similarity). When phosphorylated at Ser-42, localizes to the cytoplasm (By similarity). When ubiquitinated at Lys-138, acetylated at Lys-133 and Lys-375 and phosphorylated at Tyr-139, localizes to the food vacuole (By similarity). When triubiquitinated at Lys-138, appears to colocalize with hemozoin in the food vacuole (By similarity). {ECO:0000250|UniProtKB:Q7RA60, ECO:0000250|UniProtKB:Q8IJN7, ECO:0000269|PubMed:19642995, ECO:0000269|PubMed:21949403}.
Interaction partners:
Sequence:
MAHVITRINAREILDSRGNPTVEVDLETNLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQKAIKNINEIIAPKLIGMNCTEQKKIDNLMVEELDGSKNEWGWSKSKLGANAILAISMAVCRAGAAANKVSLYKYLAQLAGKKSDQMVLPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEALRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNANEALDLLVTAIKSAGYEGKVKIAMDVAASEFYNSENKTYDLDFKTPNNDKSLVKTGAQLVDLYIDLVKKYPIVSIEDPFDQDDWENYAKLTAAIGKDVQIVGDDLLVTNPTRITKALEKNACNALLLKVNQIGSITEAIEACLLSQKNNWGVMVSHRSGETEDVFIADLVVALRTGQIKTGAPCRSERNAKYNQLLRIEESLGNNAVFAGEKFRLQLN
Protein: At1g11440 (Putative serine/threonine protein kinase) (T23J18.11) (Q9LPZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MANFYENYQSPYDYNQVNNLYDQNHYHYNQQQQQLGFEPMSYNYYNWNESESESEYVAYSGYDDPMSYNCYNWNGSESETTSAYVAYSVSTMSEPKHLFYDPNLYTTYESPPQFSIYCSVASALDFNEPEFDEYDPTPYGGGYDVVATYGKPLPPSVETCYPCSTAPHAKAPSPPEIIAPVPLGIYDGGQKNVVKKRVSFAEPVEEVKPIETIKEQEQEQDEDYDEESEDEDDGDDDDEEEEEGDEEAKEEEKDHSSSYGNEEYEVVDKGEVKALYVPSGYGLEATDLCEVIFGGYFPCVLRNKRRQEDEQDRGAAVSCWESNDSDPWKTTSDHLFGDSYPYGYENRSERNQFEVSSYGYRMY
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q57WF7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calcineurin B subunit, putative
- Probable eukaryotic initiation factor 4A
- Serine/threonine specific protein phosphatases domain-containing protein
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
Sequence:
MSRNDCVMMDKIIEGDGKTIPRQGSIVTLDYVGYLPDGRKFDSTIERGKPFVFRVGCGEVIKGWDEGIVQMSKGERSRLTMPPSLAFGSTGFPGIIPPNTVIVFEVTLLDVV
Protein: 45 kDa calcium-binding protein (Stromal cell-derived factor 4) (A0A5F9UP49)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus lumen {ECO:0000256|ARBA:ARBA00023769}.
Interaction partners:
Sequence:
MASRWGPLIGLAPCCLWLLGAVLLMDASARPANHSSTRERVANREENEILPPDHLNGVKLEMDGHLNRGFHQEVFLGKDLGGFDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEESKTHFRAVDPDGDGHVSWDEYKVKFLASKGHSEKEVADAIRLNEELKVDEETQEVLENLKDRWYQADSPPADLLLTEEEFLSFLHPEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTAEELESYMDPMNEYNALNEAKQMIAVADENQNHHLEPEEVLKYSEFFTGSKLVDYARSVHEEF
Protein: E3 ubiquitin-protein ligase LubX (EC 2.3.2.27) (Legionella U-box protein) (RING-type E3 ubiquitin transferase LubX) (Q5ZRQ0)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Acts in conjunction with host E2 ubiquitin-conjugating enzymes UBE2D1 (UBCH5A) or UBE2D3 (UBCH5C), and mediates polyubiquitination of host kinase CLK1.
Subcellular location: Secreted {ECO:0000269|PubMed:18284575}. Host cell {ECO:0000269|PubMed:18284575}. Note=Secreted via type IV secretion system (T4SS), and delivered into the host cell.
Interaction partners:
- SidH
Sequence:
MGYRIEMATRNPFDIDHKSKYLREAALEANLSHPETTPTMLTCPIDSGFLKDPVITPEGFVYNKSSILKWLETKKEDPQSRKPLTAKDLQPFPELLIIVNRFVETQTNYEKLKNRLVQNARVAARQKEYTEIPDIFLCPISKTLIKTPVITAQGKVYDQEALSNFLIATGNKDETGKKLSIDDVVVFDELYQQIKVYNFYRKREMQKNQIQPSVSSGFGFFSLNFLTSWLWGTEEKKEKTSSDMTY
Protein: E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (Q9QZS2)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3 (By similarity). Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation (By similarity). Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1 (By similarity). Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation (By similarity). Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10822263}. Nucleus {ECO:0000269|PubMed:10822263, ECO:0000269|PubMed:10849425}. Nucleus, PML body {ECO:0000250|UniProtKB:P78317}.
Interaction partners:
- Small ubiquitin-related modifier 3
- Ubiquitin-conjugating enzyme E2 D1
- Ubiquitin-conjugating enzyme E2 N
- Small ubiquitin-related modifier 2
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 1
- Mediator of DNA damage checkpoint protein 1
- Protein PML
- KxDL motif-containing protein 1
- E3 ubiquitin-protein ligase RNF114
Sequence:
MSTRNPQRKRRGGTVNSRQTQKRTRETTSTPEVSLETEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSRDKDVYVTTHTPRSTKDDGATGPRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI
Protein: Agamous-like MADS-box protein AGL31 (Protein MADS AFFECTING FLOWERING 2) (Q9FPN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that prevents vernalization by short periods of cold. Acts as a floral repressor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- AGAMOUS-like 77
- Protein INCREASED RESISTANCE TO MYZUS PERSICAE 1
- F-box/kelch-repeat protein At2g44700
Sequence:
MGRKKVEIKRIENKSSRQVTFSKRRNGLIEKARQLSILCESSIAVLVVSGSGKLYKSASGDNMSKIIDRYEIHHADELEALDLAEKTRNYLPLKELLEIVQSKLEESNVDNASVDTLISLEEQLETALSVTRARKTELMMGEVKSLQKTENLLREENQTLASQVGKKTFLVIEGDRGMSWENGSGNKVRETLPLLK
Protein: Protein LONGIFOLIA 1 (Protein TON1 RECRUITING MOTIF 2) (Q9LF24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In association with LNG2, regulates leaf morphology by promoting longitudinal polar cell elongation independently of ROT3.
Subcellular location: Nucleus {ECO:0000269|PubMed:17038516}.
Interaction partners:
- At5g26910
- GPI-anchored adhesin-like protein
- tRNA
- Small polypeptide DEVIL 16
- tRNA
- At3g62990
- Transmembrane protein
- Serine-rich adhesin for platelets-like protein
- GPI-anchored adhesin-like protein, putative
- tRNA
Sequence:
MSAKLLYNLSDENPNLNKQIGCMNGIFQVFYRQHYPPRRVTGDELKSLPSGKASDNVGDTNISADKKETEKSKKKKTAKEKQRGVSSESSSRLSFSSSPCSSSFSSADISTTASQFEQPGLSNGENPVREPTNGSPRWGGLMMPSDIRELVRSSIHKETRTRDEEALSQQPKSARANVSLLKESSPSRNSNEWSEGRRVVKLKDSPRFSYDERETRKTGAKLKETPRLSLDSRSNSFRSARSSCSPEPQELVTGHRRTTSSVVAKLMGLEVIPDEPVTIQNRENRFCDSPRPTSRVEVDLQRSRGFDSIKKMMPAKFPMKASPWAQVDGAKNQVKIPDATTLTVYGEIQKRLSQLEFKKSEKDLRALKQILEAMEKTQQLISKDDDDNKTLCSSNFMQRNNQPIPSAINTSSMNFKSSSIVVMKAATAPVFKDTGIAGSASFSPRNVALPNVKVGNLRQAQKVIPRKQSAMDVTPRPGYYKGQTESTMKNTSTRPLQSKSDMAKSGKIQKPSVSLRTPPKKLGFEKQSRPTSPKPELNKNQRQQLSRQQTESASPRRKPGIKSRGLQQSEDRLSDESSDLRSLRSDSNVSLASNLDTEVTSRYNYERNSDITEQHTPKQRSPDLGMRSLSKPLKVTVEQPSPVSVLDVAFDEDDSPSPVRKISIVFKEDDNLSSEESHWMNKNNNLCRSIVWPESNTSLKQPDAELTEGFMEDDAEFKNGDHKYISEIMLASGLLRDIDYSMISIQLHQAHLPINPSLFFVLEQNKTSNVSLQDNKHKGRGFGQQQTVNLVERSKRKLIFDTINEILAHRFAAEGCTKQPSITLSISTQRTHEKSSRGEELLQTLCSEIDRLQDNSKCILDEDDEDLIWEDLQSHGMNWKEIEGETPGLVLDIERLIFKDLIGEVVTSEFAAFPRMLSGQPRQLFHC
Protein: Uncharacterized protein C328.01c (O14116)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- GTP-binding nuclear protein spi1
- Exportin-T
- Protein argonaute
- Exportin-1
- Protein Dicer
- Uncharacterized protein C11G11.07
- Ran GTPase-activating protein 1
- Nucleoporin nup146
- mRNA export factor mex67
- Ran-specific GTPase-activating protein 1
Sequence:
MDEKGLSNILQALNVVHSPESSRETRFSAQQLLDELKDSYSSPSVAIQLLELNEQAFSSLGCKLDIHIVQHFSLSLFETSVGMNWKSFSNKEKESVTSFLCKISLEDNNLLSVHFVRSKLASVFIEIAKRDWYNTWREEFDSFLQSLWSLSLQHRQLSSLILRGIMEDLYQYDDPVASLRSHILFNALISILSSSSTLHKLYPSGLPYSVTIPSNNEGWLIRWGNALESQDDALECLKCFKSCLSWVATDSIREANIVSHICQILVQGPIFLKTHAIDCIYICVTRTMEIDDPLWEIVEEMLSPSSLYTLHQVYTATSESINIKTLSSTTPEYILLKKLSETIVALGQYNYLDSNRRKCIKLTSLDTYSLLVLEIMKHPSLLISAISQHFWVLALRDPIISKHEKFQIVYPELLSIASERLLRFEDAVVELIPESATAKYLQEDVEGVSAVHSFCGNFRRFMFDIVRLTVSITPIESLNWIQNRFQSTVLGNMEDIQSQTEFFSKTSPLYLTMDVGFSTIEAFLHGVTRWNENTSDDPATYEIILQNLFLWCKQLVEINFKDPMLITRLISVLVLFTSILARENTTLLGVVLEKIISAVTYDNTSASYGFSDVQKINEMRSRCCFELVRLGELMPNPLMNIFDQLQSIIDQLDNATTLTGSEIVMLKTFLFVITQFSDVNIEVKNEYFEKLVGPVVKTWLDVQPPVNSPMEFLNHIGFPQMAEYLSAKYPYNADYTQFELDADAASYQSNLETGRKWLWPIKCLGRFCEATCSNKHIHPSEFEGQKNLWQVILPNVVPNLLKLVEQLHCCYEPSFISGLGMHNSSILQKSIVERFWLHGVSQISKNQFLEESYKMDVSANKLIHSFGHFLRRLREYCYYAIASFMRLGQAFFCVPGLSKQFLTAFFSHAAGLSLHQWTSMVNVVIKPYCVNCPAELRDECLLPLLPALLSELDHKLVSEWRRINDRGLLVEEDAEETGEDDDLSEEMIEESLLRHLTYATAKLITETFLQITPTQSRSNVSSSLIGKETVEGPVKLSEYVLDNAIICEPLLCTLCHLLVIHDSRTVGLVVNAFLAITPLLVSEQAHSLVREFICQQVFQSVILAIHDPYFESMQSDFIRLACIILSYSQGITDSAFQLLASIPALANQENLVPAFFNKFREASTLKIQKALLTRLLNSGRIVPRTDRRAVNAAILDVSAKEMLKRFEKSVSLQDEQKNDVLSRDEDTGLANLFE
Protein: Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (Histone H3-K79 methyltransferase) (F1Q4W7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU271113}.
Interaction partners:
- MLLT10 histone lysine methyltransferase DOT1L cofactor
- Histone H3
- Histone H3.2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Uncharacterized protein LOC794380
- [histone H3]-lysine
- Histone H3.3
- Histone H3
- Si:dkey-108k21.24.
Sequence:
MLLFLPRITCKIVCLCVVQWKGTTQPMKLNKRPSNGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQIIDEMEMMEEDTFVDLGSGVGQVVLQVAAATNCKHYYGVEKADIPATYAESMDKEFKRWMKWYGKKHGEYTLERGDFLSEEWKERIASTSVIFVNNFAFGPEVDHQLKERFANMKEGGKIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLRGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEVARRRPQKDSKENKSNTTTPTKPKEHKQAQHDSGGEEEPVVPVKPSPKPRRAKILTRGRKLGNRKRGRPKKAPAATAAERKNKKSQSALDLLHAKTLSAAPAQEPYRSPQSPFYQLPPKVQHYTSSQLLMAPTPPGLQTLLDNIKVQYLHFMAYMKTPQYRTNLQQSLEQEKLRHTELSSQAQQLVNACHAHKERIHDLFQSKLEELGVKAVTVEDLVQAQKEITAHNMQLREQTKQLEHDMAELRDQSQLLLKARCEELKLDTLCWDTLKKEIEALRRQISEKQRHCLELQISIVELEKSQRQQELLQLKSSYSPCEVSPYRKALPGPDPRPTLDPDTPKLTPQSSMGLNGLSPELSINGTASPGYERCTGSAMGKNELLTHYLPISPDHEIVPPTPDSRTRQLGQPLPDYTRFSPAKIALRRHLNQDSAANQFRALGNIHRGDTGAISSPTLGFKQASPCSSEVQAVTTAKSTDRADKEKSPTAPGDTITSLPISIPLSTVHPSKLPVSIPLASVVLPNRVERLRSTLSPVLNPAGQSNGKPPLTPTSGYSSSSGLVNGSHSTMLTEDQDCDVASPPPHSTPVMGLQPRGSGLSPPLGTGGVLQYADGPPRLPPEDGHERQGPESDTEPLDSEARRRIFFSSSSSSSSSSSSTGGSRLHHGSVKQGHHHHSKHHHHHHHHHHHHSPSSHSQEGRKRGRRKRSSSGAVPMSGSPKRRVFPGLGCSSHSSGSPLNINSMVNNINQPLEISAISSPEQSGRSPCEQDLDQPPVLKRERPLELNNTGRYSSAPSSDEEGNGYAPDTSSSSRIERKIATISLDRDGPVRDLERGLQGRKSGASSVSSEVSSSSGTSKWKSTFSPISDPKPTPPDIRQGGSPFSVGASRGGTDSDSDHKPQRRGEREREPYGNSNLFLSQDGSGRSAVNTSERSLQKQKVREWDLKSVSGLASQNLFISAAASGGILSGKVGGAATVSSASAVGQYFPLGGASVLQPLFGTQAAGPATSGAPRLVNGHSALGSFSSAGLAGGAAGGIFHHMVSSSSSQQSGPNLPSSHNSQQRHLDTNPKAGASFLASGPNRTQTVLHAPSPPTLALPPPPPLLNTVPSQPSSPRSSRPQSSIPVATSSQSLAAASSSCTSSASSRPFTVHYPPHLQPPGSAGSGGTGASWRTLASYTASQIPGNRPR