wanglab/gogpt-training-data huggingface dataset:
Protein: Pectinesterase/pectinesterase inhibitor 18 (AtPMEpcrA) [Cleaved into: Pectinesterase inhibitor 18 (Pectin methylesterase inhibitor 18); Bifunctional pectinesterase 18/rRNA N-glycosylase (PE 18) (EC 3.1.1.11) (EC 3.2.2.22) (Pectin methylesterase 18) (Pectin methylesterase 4) (AtPME4) (Ribosome-inactivating protein)] (Q1JPL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin. Inhibits the elongation phase of protein synthesis.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Classical arabinogalactan protein 10
- Methyltransferase
- Peptide upstream protein
- Inactive GDSL esterase/lipase-like protein 23
- Probable pectate lyase 3
- Embryo-specific protein ATS3B
- Pectate lyase
- Pectate lyase
- Probable pectate lyase 13
- Probable pectate lyase 12
Sequence:
MSNSNQPLLSKPKSLKHKNLCLVLSFVAILGSVAFFTAQLISVNTNNNDDSLLTTSQICHGAHDQDSCQALLSEFTTLSLSKLNRLDLLHVFLKNSVWRLESTMTMVSEARIRSNGVRDKAGFADCEEMMDVSKDRMMSSMEELRGGNYNLESYSNVHTWLSSVLTNYMTCLESISDVSVNSKQIVKPQLEDLVSRARVALAIFVSVLPARDDLKMIISNRFPSWLTALDRKLLESSPKTLKVTANVVVAKDGTGKFKTVNEAVAAAPENSNTRYVIYVKKGVYKETIDIGKKKKNLMLVGDGKDATIITGSLNVIDGSTTFRSATVAANGDGFMAQDIWFQNTAGPAKHQAVALRVSADQTVINRCRIDAYQDTLYTHTLRQFYRDSYITGTVDFIFGNSAVVFQNCDIVARNPGAGQKNMLTAQGREDQNQNTAISIQKCKITASSDLAPVKGSVKTFLGRPWKLYSRTVIMQSFIDNHIDPAGWFPWDGEFALSTLYYGEYANTGPGADTSKRVNWKGFKVIKDSKEAEQFTVAKLIQGGLWLKPTGVTFQEWL
Protein: glutathione transferase (EC 2.5.1.18) (C8BLR2)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MSGKPVLHYANIRGRMEPIRWLLAAAGVEFEERILKTKDDLQKLRTDGCLLFQQVPMVEIDGMKMVQTRAILNYIAGKYNLYGKDLKERALIDMYVEGLADLFELIMYHEFKPANEKEKDLANIMDKATNRYLPVFEKVLKDHGHDFLVGNKLSKADVSLLENILGLEELKPDALAKFPLLQSFKARMSNIPSIKKFLQPGSAKKPLIQEKDIPSVIAIFH
Protein: F-box/FBD/LRR-repeat protein At4g26340 (Q8H1R7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- WRKY family transcription factor
- F-box protein At1g31080
- Putative F-box protein At1g47730
- F-box protein At1g30790
- Mitochondrial transcription termination factor family protein
- F-box protein At2g20380
- F-box/kelch-repeat protein At2g22030
- F-box protein At3g08750
- Putative F-box/kelch-repeat protein At4g02310
- F-box associated ubiquitination effector family protein
Sequence:
MDRISQLSDDLLLQILSFIPGKDVVATSLLSKRWQSLWMLVSELEYDDSYHTGDYKSFSQFVYRSLLSNNAPVIKHLHLNLGPDCPAIDIGLWIGFALTRRLRQLKINIRTSSNDASFSLPSSLYTSDTLETLRLINFVLLDVPSSVCLPSLKVLHLKTVDYEDDASLPSLLFGCPNLEELFVERHDQDLEMDVTFVVPSLRRLSMIDKNYGQCDRYVIDVPSLKYLNITDDAVYDVRQIENMPELVEAHVDITQGVTHKFLRALTSVRQLSLCLSLSEVMCPSGIIFSQLVHLNLSTVVKGWWDLLTSMLQDSPKLQSLKLIDKQHESGLCGIETPIGWKLPSSVPECLLFSLEAFEWIGYKGRRGDREVATYVLKNAACLRTAKFSPESTDVGEKYHMLKELASVPTASTSSKLLFD
Protein: Oleate hydratase (EC 4.2.1.53) (Fatty acid double bond hydratase) (Fatty acid hydratase) (C7DLJ6)
Organism: Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
Function: Catalyzes the hydration of oleate at its cis-9-double bond to yield 10-hydroxyoctadecanoate. The hydration of unsaturated fatty acids is suggested to be a detoxification mechanism and a survival strategy for living in fatty acid-rich environments.
Interaction partners:
Sequence:
MNPITSKFDKVLNASSEYGHVNHEPDSSKEQQRNTPQKSMPFSDQIGNYQRNKGIPVQSYDNSKIYIIGSGIAGMSAAYYFIRDGHVPAKNITFLEQLHIDGGSLDGAGNPTDGYIIRGGREMDMTYENLWDMFQDIPALEMPAPYSVLDEYRLINDNDSNYSKARLINNKGEIKDFSKFGLNKMDQLAIIRLLLKNKEELDDLTIEDYFSESFLKSNFWTFWRTMFAFENWHSLLELKLYMHRFLHAIDGLNDLSSLVFPKYNQYDTFVTPLRKFLQEKGVNIHLNTLVKDLDIHINTEGKVVEGIITEQDGKEVKIPVGKNDYVIVTTGSMTEDTFYGNNKTAPIIGIDNSTSGQSAGWKLWKNLAAKSEIFGKPEKFCSNIEKSAWESATLTCKPSALIDKLKEYSVNDPYSGKTVTGGIITITDSNWLMSFTCNRQPHFPEQPDDVLVLWVYALFMDKEGNYIKKTMLECTGDEILAELCYHLGIEDQLENVQKNTIVRTAFMPYITSMFMPRAKGDRPRVVPEGCKNLGLVGQFVETNNDVVFTMESSVRTARIAVYKLLNLNKQVPDINPLQYDIRHLLKAAKTLNDDKPFVGEGLLRKVLKGTYFEHVLPAGAAEEEEHESFIAEHVNKFREWVKGIRG
Protein: Transcription factor MYB30 (Myb-related protein 30) (AtMYB30) (Q9SCU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to the DNA sequence 5'-AACAAAC-3'. Acts as a positive regulator of hypersensitive cell death. Acts as a positive regulator of salicylic acid synthesis. Regulates very-long-chain fatty acid biosynthesis. Acts cooperatively with BZR2 to promote expression of a subset of brassinosteroids target genes. Transcriptional activity and hypersensitive response control negatively regulated by PLA2-ALPHA. Involved in the regulation of abscisic acid (ABA) signaling. Increased levels of MYB30 can accelerate flowering both in long and short days through the regulation of FT.
Subcellular location: Nucleus {ECO:0000269|PubMed:20696912}.
Interaction partners:
- E3 ubiquitin-protein ligase MIEL1
- Protein BRASSINAZOLE-RESISTANT 2
- E3 ubiquitin-protein ligase RHA2B
- Phospholipase A2-alpha
- Transcription factor BIM1
- Protein ECERIFERUM 2
- Ethylene-responsive transcription factor WIN1
- E3 SUMO-protein ligase SIZ1
- 3-ketoacyl-CoA synthase 6
- Non-specific lipid transfer protein GPI-anchored 1
Sequence:
MVRPPCCDKGGVKKGPWTPEEDIILVTYIQEHGPGNWRAVPTNTGLLRCSKSCRLRWTNYLRPGIKRGNFTEHEEKMIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLNKVNQDSHQELDRSSLSSSPSSSSANSNSNISRGQWERRLQTDIHLAKKALSEALSPAVAPIITSTVTTTSSSAESRRSTSSASGFLRTQETSTTYASSTENIAKLLKGWVKNSPKTQNSADQIASTEVKEVIKSDDGKECAGAFQSFSEFDHSYQQAGVSPDHETKPDITGCCSNQSQWSLFEKWLFEDSGGQIGDILLDENTNFF
Protein: PHC2 protein (B7ZLY0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MENELPVPHTSSSACATSSTSGASSSSGCNNSSSGGSGRPTGPQISVYSGIPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVSNRQGSTSGSNVSAQAPAQSSSINLAASPAAAQLLNRAQSVNSAAASGIAQQAVLLGNTSSPALTASQAQMYLRAQMVQNLTLRTQQTPAAAASGPTPTQPVLPSLALKPTPGGSQPLPTPAQSRNTAQASPAGAKPGIADSVMEPHKKGDGNSSVPGSMEGRAGLSRTVPAVAAHPLIAPAYAQLQPHQLLPQPSSKHLQPQFVIQQQPQPQQQQPPPQQSRPVLQAEPHPQLASVSPSVALQPSSEAHAMPLGPVTPALPLQCPTANLHKPGGSQQCHPPTPDTGPQNGHPEGVPHTPQRRFQHTSAVILQLQPASPVPQQCVPDDWKEMAPGEKSVPETRSGPSPHQQAIVTAMPGGLPVPTSPNIQPSPAHETGQGIVHALTDLSSPGMTSGNGNSASSIAGTAPQNGENKPPQAIVKPQILTHVIEGFVIQEGAEPFPVGRSSLLVGNLKKKYAQGFLPEKLPQQDHTTTTDSEMEEPYLQESKEEGAPLKLKCELCGRVDFAYKFKRSKRFCSMACAKRYNVGCTKRVGLFHSDRSKLQKAGAATHNRRRASKASLPPLTKDTKKQPTGTVPLSVTAALQLTHSQEDSSRCSDNSSYEEPLSPISASSSTSRRRQGQRDLELPDMHMRDLVGMGHHFLPSEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKDS
Protein: IGHV7-81 protein (Q6PIL0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDWTWSILFLVAAATGTYSQVQLVQSGHEVKQPGASVKVSCKASGYSFTTYGMNWVPQAPGQGLEWMGWFNTYTGNPTYAQGFTGRFVFSMDTSASTAYLQISSLKAEDMAMYYCARYTMWKPTS
Protein: Pyruvate decarboxylase 1 (AtPDC1) (EC 4.1.1.1) (O82647)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in ethanolic fermentation during anoxia.
Interaction partners:
- Alcohol dehydrogenase class-P
- Alcohol dehydrogenase-like 4
- Alcohol dehydrogenase-like 3
- Alcohol dehydrogenase-like 6
- L-lactate dehydrogenase
- Glucose-6-phosphate isomerase, cytosolic
- Pyruvate, phosphate dikinase 1, chloroplastic
- Alcohol dehydrogenase class-3
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
Sequence:
MDTKIGSIDDCKPTNGDVCSPTNGTVATIHNSVPSSAITINYCDATLGRHLARRLVQAGVTDVFSVPGDFNLTLLDHLMAEPDLNLIGCCNELNAGYAADGYARSRGVGACVVTFTVGGLSVLNAIAGAYSENLPLICIVGGPNSNDYGTNRILHHTIGLPDFSQELRCFQTVTCYQAVVNNLDDAHEQIDKAISTALKESKPVYISVSCNLAAIPHHTFSRDPVPFSLAPRLSNKMGLEAAVEATLEFLNKAVKPVMVGGPKLRVAKACDAFVELADASGYALAMMPSAKGFVPEHHPHFIGTYWGAVSTPFCSEIVESADAYIFAGPIFNDYSSVGYSLLLKKEKAIVVQPDRITVANGPTFGCILMSDFFRELSKRVKRNETAYENYHRIFVPEGKPLKCESREPLRVNTMFQHIQKMLSSETAVIAETGDSWFNCQKLKLPKGCGYEFQMQYGSIGWSVGATLGYAQASPEKRVLAFIGDGSFQVTVQDISTMLRNGQKTIIFLINNGGYTIEVEIHDGPYNVIKNWNYTGLVDAIHNGEGNCWTAKVRYEEELVEAITTATTEKKDCLCFIEVILHKDDTSKELLEWGSRVSAANSRPPNPQ
Protein: Choline/ethanolamine kinase (Choline kinase beta) (CK) (CKB) (EC 2.7.1.32) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (choline/ethanolamine kinase beta) (CKEKB) (O54783)
Organism: Rattus norvegicus (Rat)
Function: Has a key role in phospholipid metabolism, and catalyzes the first step of phosphatidylethanolamine and phosphatidylcholine biosynthesis.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline-phosphate cytidylyltransferase A
- Choline-phosphate cytidylyltransferase B
- Glycerophosphocholine phosphodiesterase GPCPD1
- Phosphoethanolamine/phosphocholine phosphatase
- Choline O-acetyltransferase
- Acetylcholinesterase
- Choline kinase alpha
- Ethanolamine-phosphate phospho-lyase
- Selenoprotein I
Sequence:
MAADGTGVVGGGAVGGPLSKDGLLDAKCPEPIPNRRRSSSLSRDAQRRAYQWCREYLGGAWRRARPEELSVCPVSGGLSNLLFRCSLPNHVPSMGGEPREVLLRLYGAILQGVDSLVLESVMFAILAERSLGPQLYGVFPEGRLEQYLPSRPLKTQELRDPVLSGAIATKMARFHGMEMPFTKEPRWLFGTMERYLKQIQDLPSTSLPQMNLVEMYSLKDEMNHLRTLLDATPSPVVFCHNDIQEGNILLLSEPDSDDNLMLVDFEYSSYNYRGFDIGNHFCEWVYDYTYEEWPFYKARPADYPTREQQLLFIRHYLAEVQKGEVLSEEEQKKQEEDLLIEISRYALASHFFWGLWSTLQASMSTIEFGYLEYAQSRFQFYFQQKGQLTSFLSP
Protein: Cytohesin-2 (PH, SEC7 and coiled-coil domain-containing protein 2) (Q2KI41)
Organism: Bos taurus (Bovine)
Function: Acts as a guanine-nucleotide exchange factor (GEF). Promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane (By similarity). Involved in neurite growth (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q99418}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99418}. Cytoplasm {ECO:0000250|UniProtKB:P63034}. Cell projection {ECO:0000250|UniProtKB:P63034}. Cell projection, growth cone {ECO:0000250|UniProtKB:P63034}. Note=Recruited to the cell membrane through its association with ARL4A, ARL4C and ARL4D. Also requires interaction with phosphoinositides for targeting to plasma membrane. In differentiating neuroblastoma cells, colocalizes with CCDC120 in both neurite shaft and growth cone areas. {ECO:0000250|UniProtKB:P63034, ECO:0000250|UniProtKB:Q99418}.
Interaction partners:
- ADP ribosylation factor 6
- ADP-ribosylation factor 1
- ADP-ribosylation factor 2
- Coiled-coil domain containing 120
- Trafficking regulator and scaffold protein tamalin
- ADP-ribosylation factor-like protein 4A
- ADP-ribosylation factor-like protein 4D
Sequence:
MEDGVYEPPDLTPEERMELENIRRRKQELLVEIQRLREELSEAMSEVEGLEANEGSKTLQRNRKMAMGRKKFNMDPKKGIQFLVENELLQNTPEEIARFLYKGEGLNKTAIGDYLGEREELNLAVLHAFVDLHEFTDLNLVQALRQFLWSFRLPGEAQKIDRMMEAFAQRYCLCNPGVFQSTDTCYVLSFAVIMLNTSLHNPNVRDKPGLERFVAMNRGINEGGDLPEELLRNLYDSIRNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGAQAPSPPSLPGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVDDPRKPNCFELYIPNNKGQLIKACKTEADGRVVEGNHMVYRISAPTQEEKDEWIKSIQAAVSVDPFYEMLAARKKRISVKKKQEQP
Protein: phosphorylase kinase (EC 2.7.11.19) (J3KNN3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTLDVGPEDELPDWAAAKEFYQKYDPKDVIGRGVSSVVRRCVHRATGHEFAVKIMEVTAERLSPEQLEEVREATRRETHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRKGELFDYLTEKVALSEKETRSIMRSLLEAVSFLHANNIVHRDLKPENILLDDNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLLFPSWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSSTVKDLISRLLQVDPEARLTAEQALQHPFFERCEGSQPWNLTPRQRFRVAVWTVLAAGRVALSTHRVRPLTKNALLRDPYALRSVRHLIDNCAFRLYGHWVKKGEQQNRAALFQHRPPGPFPIMGPEEEGDSAAITEDEAVLVLG
Protein: Ankyrin repeat-containing protein P16F5.05c (Q9HFE7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Protein LTV1
- Probable assembly chaperone of rpl4
- Pre-rRNA-processing protein tsr2
- Ribosome assembly protein rrb1
- Uncharacterized WD repeat-containing protein C25H1.08c
- Uncharacterized protein C13G1.09
- 20S-pre-rRNA D-site endonuclease nob1
- Ribosomal RNA-processing protein 1 homolog
- 25S rRNA
Sequence:
MDVDDLIYACRAADEELLDEIIEKCPQELSRRDENGNSGLHMASANGHIAVVQKIIPYLNKEVINAQNESGNTAMHWAALNGHAEICKLLLEAGGDPHIKNIYEKSPIYEADIRNQQKVMDLFLDFEIAKGSEENTGDEEKLEDGI
Protein: Trafficking protein particle complex subunit 23 (TRAPP subunit 23) (Transport protein particle 23 kDa subunit) (Q03784)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation.
Subcellular location: Golgi apparatus, cis-Golgi network. Endoplasmic reticulum. Preautophagosomal structure.
Interaction partners:
- Trafficking protein particle complex subunit BET5
- Trafficking protein particle complex II-specific subunit 120
- Trafficking protein particle complex II-specific subunit 130
- Trafficking protein particle complex subunit 31
- Trafficking protein particle complex subunit BET3
- Trafficking protein particle complex subunit 33
- Trafficking protein particle complex III-specific subunit 85
- TRAPP-associated protein TCA17
- Trafficking protein particle complex subunit 20
- GTP-binding protein YPT1
Sequence:
MAIETILVINKSGGLIYQRNFTNDEQKLNSNEYLILASTLHGVFAIASQLTPKALQLTQQTNIENTIPYIPYVGMSSNRSDTRNGGGNNNKHTNNEKLGSFKGDDFFKEPFTNWNKSGLRQLCTDQFTMFIYQTLTGLKFVAISSSVMPQRQPTIATTDKPDRPKSTSNLAIQIADNFLRKVYCLYSDYVMKDPSYSMEMPIRSNLFDEKVKKMVENLQ
Protein: Virulence factor mce family protein (O53543)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAGSGVPSHRSMVIKVSVFAVVMLLVAAGLVVVFGDFRFGPTTVYHATFTDASRLKAGQKVRIAGVPVGSVKAVKLNPDHSIDVAFAIDRSYTLYSSTRAVIRYENLVGDRFLEITSGPGELRKLPPGGTINVAHTQPALDLDALLGGLRPVLKGFDADKINTITSAVIELLQGQGGPLANVLADTGAFSAALGARDQLIGEVITNLNAVLATVDAKSAQFSASVDQLQQLVSGLAKNRDPIAGAISPLASTTTDLTELLRNSRRPLQGILENARPLATELDNRKAEVNNDIEQLGEDYLRLSALGSYGAFFNIYFCSVTIKINGPAGSDILLPIGGQPDPSKGRCAFAK
Protein: E3 ubiquitin-protein ligase MARCHF2 (EC 2.3.2.27) (Membrane-associated RING finger protein 2) (Membrane-associated RING-CH protein II) (MARCH-II) (RING finger protein 172) (RING-type E3 ubiquitin transferase MARCHF2) (Q1LVZ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: E3 ubiquitin-protein ligase which may be involved in endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P0N8}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9P0N8}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q5I0I2}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9P0N8}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9P0N8}. Cell membrane {ECO:0000250|UniProtKB:Q9P0N8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Stx6 protein
- Peroxisomal N
- Ubiquitin-conjugating enzyme E2 J2
- PDZK1-interacting protein 1.
Sequence:
MTTGECCHLPGSLCDCTGNAALSKTVEEADNRRAQYVTQVTAKDGRLLSTVIKALGTQSDRPICRICHEGQDVCNSEGLLSPCDCTGTLGTVHKSCLEKWLSSSNTSYCELCHTEFTIERRPRPLTEWLRDPGPRNEKRTLFCDMVCFLFITPLAAISGWLCLRGAQDHLHFNSRLEAVGLIALTIALFTIYVLWTLVSFRYHCQLYSEWRRTNQKVRLLIPDTKGAHSTQHSLLSTKLLKKTADETIV
Protein: E3 ubiquitin-protein ligase RMA2 (EC 2.3.2.27) (Protein RING membrane-anchor 2) (RING-type E3 ubiquitin transferase RMA2) (P93030)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of the auxin-binding protein ERABP1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19224217}; Single-pass type IV membrane protein {ECO:0000269|PubMed:19224217}.
Interaction partners:
- E3 ubiquitin-protein ligase RHA1B
- E3 ubiquitin-protein ligase ATL76
- At1g31940/F5M6.6
- At2g35585
- Mitochondrial transcription termination factor family protein
- Probable acyl-activating enzyme 17, peroxisomal
- Ethylene-responsive transcription factor ERF060
Sequence:
MEIEKDEDDTTLVDSGGDFDCNICLDQVRDPVVTLCGHLFCWPCIHKWTYASNNSRQRVDQYDHKREPPKCPVCKSDVSEATLVPIYGRGQKAPQSGSNVPSRPTGPVYDLRGVGQRLGEGESQRYMYRMPDPVMGVVCEMVYRRLFGESSSNMAPYRDMNVRSRRRAMQAEESLSRVYLFLLCFMFMCLFLF
Protein: Delta-1 crystallin (Delta crystallin I) (Q7SIE0)
Organism: Meleagris gallopavo (Wild turkey)
Function: Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles.
Interaction partners:
Sequence:
MATEGDKLLGGRFVGSVDPIMEILSSSISTEQRLTEVDIQASMAYAKALEKASILTKTELEKILSGLEKISEESSKGVLVMTQSDEDIQTAIERRLKELIGDIAGKLQTGRSRNEQVVTDLKLLLKSSISVISTHLLQLIKTLVERAAIEIDIIMPGYTHLQKALPIRWSQFLLSHAVALTRDSERLGEVKKRITVLPLGSGVLAGNPLEIDRELLRSELDMTSITLNSIDAISERDFVVELISVATLLMIHLSKLAEDLIIFSTTEFGFVTLSDAYSTGSSLLPQKKNPDSLELIRSKAGRVFGRLAAILMVLKGIPSTFSKDLQEDKEAVLDVVDTLTAVLQVATGVISTLQINKENMEKALTPELLSTDLALYLVRKGMPIRQAQTASGKAVHLAETKGITINNLTLEDLKSISPLFASDVSQVFSVVNSVEQYTAVGGTAKSSVTAQIEQLRELLKKQKEQA
Protein: Villin-1 (P09327)
Organism: Homo sapiens (Human)
Function: Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.
Subcellular location: Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, microvillus. Cell projection, filopodium tip {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Note=Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia (By similarity). Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment. {ECO:0000250}.
Interaction partners:
- Spermatid nuclear transition protein 1
- COMM domain-containing protein 6
Sequence:
MTKLSAQVKGSLNITTPGLQIWRIEAMQMVPVPSSTFGSFFDGDCYIILAIHKTASSLSYDIHYWIGQDSSLDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESEAFRGYFKQGLVIRKGGVASGMKHVETNSYDVQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESTRMERLRGMTLAKEIRDQERGGRTYVGVVDGENELASPKLMEVMNHVLGKRRELKAAVPDTVVEPALKAALKLYHVSDSEGNLVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKKANEQEKKGAMSHALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTASNRTSGLGKTHTVGSVAKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHFYGGDCYLLLYTYLIGEKQHYLLYVWQGSQASQDEITASAYQAVILDQKYNGEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRTNNLETGPSTRLFQVQGTGANNTKAFEVPARANFLNSNDVFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENLVITPRLFECSNKTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKHANEEEKKAAATTAQEYLKTHPSGRDPETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYEDLKAELGNSRDWSQITAEVTSPKVDVFNANSNLSSGPLPIFPLEQLVNKPVEELPEGVDPSRKEEHLSIEDFTQAFGMTPAAFSALPRWKQQNLKKEKGLF
Protein: Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28) (A2T3Q0)
Organism: Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
Subcellular location: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
Interaction partners:
Sequence:
MEKLTDLNYTLSVITLMNNTLHTILEDPGMAYFPYIASVLTVLFALHKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIYDKLTVQTTGEIDMTKEINQKNVRTLEEWESGKNPYEPREVTAAM
Protein: At2g46540/F11C10.23 (Expressed protein) (F11C10.23/F11C10.23) (Fiber) (Q9ZPY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Wiskott-aldrich syndrome family protein, putative
- B12D protein
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
- At1g72040
- NADH-ubiquinone oxidoreductase chain 2
- NADH dehydrogenase iron-sulfur protein 8-B, mitochondrial
- MICOS complex subunit, putative
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase subunit 7
Sequence:
MPVMEKLRMFVAQEPVVAASCLIGGVGLFLPAVVRPILDSLEASKQVKAPPLTDVIAGVTGKKQS
Protein: DNA repair protein RAD50 (EC 3.6.-.-) (153 kDa protein) (P12753)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site.
Subcellular location: Nucleus {ECO:0000269|PubMed:9845372}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.
Interaction partners:
- Double-strand break repair protein MRE11
- DNA repair protein XRS2
- DNA endonuclease SAE2
- Serine/threonine-protein kinase TEL1
- ATP-dependent DNA helicase II subunit 1
- DNA repair and recombination protein RAD52
- Serine/threonine-protein kinase MEC1
- ATP-dependent helicase SGS1
- DNA repair protein RAD51
- Flap endonuclease 1
Sequence:
MSAIYKLSIQGIRSFDSNDRETIEFGKPLTLIVGMNGSGKTTIIECLKYATTGDLPPNSKGGVFIHDPKITGEKDIRAQVKLAFTSANGLNMIVTRNIQLLMKKTTTTFKTLEGQLVAINNSGDRSTLSTRSLELDAQVPLYLGVPKAILEYVIFCHQEDSLWPLSEPSNLKKKFDEIFQAMKFTKALDNLKSIKKDMSVDIKLLKQSVEHLKLDKDRSKAMKLNIHQLQTKIDQYNEEVSEIESQLNEITEKSDKLFKSNQDFQKILSKVENLKNTKLSISDQVKRLSNSIDILDLSKPDLQNLLANFSKVLMDKNNQLRDLETDISSLKDRQSSLQSLSNSLIRRQGELEAGKETYEKNRNHLSSLKEAFQHKFQGLSNIENSDMAQVNHEMSQFKAFISQDLTDTIDQFAKDIQLKETNLSDLIKSITVDSQNLEYNKKDRSKLIHDSEELAEKLKSFKSLSTQDSLNHELENLKTYKEKLQSWESENIIPKLNQKIEEKNNEMIILENQIEKFQDRIMKTNQQADLYAKLGLIKKSINTKLDELQKITEKLQNDSRIRQVFPLTQEFQRADLEMDFQKLFINMQKNIAINNKKMHELDRRYTNALYNLNTIEKDLQDNQKSKEKVIQLLSENLPEDCTIDEYNDVLEETELSYKTALENLKMHQTTLEFNRKALEIAERDSCCYLCSRKFENESFKSKLLQELKTKTDANFEKTLKDTVQNEKEYLHSLRLLEKHIITLNSINEKIDNSQKCLEKAKEETKTSKSKLDELEVDSTKLKDEKELAESEIRPLIEKFTYLEKELKDLENSSKTISEELSIYNTSEDGIQTVDELRDQQRKMNDSLRELRKTISDLQMEKDEKVRENSRMINLIKEKELTVSEIESSLTQKQNIDDSIRSKRENINDIDSRVKELEARIISLKNKKDEAQSVLDKVKNERDIQVRNKQKTVADINRLIDRFQTIYNEVVDFEAKGFDELQTTIKELELNKAQMLELKEQLDLKSNEVNEEKRKLADSNNEEKNLKQNLELIELKSQLQHIESEISRLDVQNAEAERDKYQEESLRLRTRFEKLSSENAGKLGEMKQLQNQIDSLTHQLRTDYKDIEKNYHKEWVELQTRSFVTDDIDVYSKALDSAIMKYHGLKMQDINRIIDELWKRTYSGTDIDTIKIRSDEVSSTVKGKSYNYRVVMYKQDVELDMRGRCSAGQKVLASIIIRLALSETFGANCGVIALDEPTTNLDEENIESLAKSLHNIINMRRHQKNFQLIVITHDEKFLGHMNAAAFTDHFFKVKRDDRQKSQIEWVDINRVTY