wanglab/gogpt-training-data huggingface dataset:
Protein: MG81 protein (Q14830)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
NSGKKLSHFLPPEFRSFAVDPQITSLDVLQHILIRAFDLSGKKNFGISYLGRDRLGQEVYLSLLSDWDLSTAFATASKPYLQLRVDIRPSEDSPLLEDWDIISPKDVIGSDVLLAEKRSSLTTAALPFTQSILTQVGRTLSKVQQVLSWSYGEDVKPFKPPLSDAEFHTYLNHEGQLSRPEELRLRIYHGGVEPSLRKVVWRYLLNVYPDGLTGRERMDYMKRKSREYEQLKSEWAQRASPEDLEFIRSTVLKDVLRTDRAHPYYAGPEDGPHLRALHDLLTTYAVTHPQVSYCQGMSDLASPILAVMDHEGHAFVCFCGIMKRLAANFHPDGRAMATKFAHLKLLLRHADPDFYQYLQEAGADDLFFCYRWLLLELKREFAFDDALRMLEVTWSSLPPDPPEHEVELVGPPSQVADTGFGGHRGWPVRQRHMLRPAGGGGSTFEDAVDHLATASQGPGGGGRLLRQASLDGLQQLRDNIGSRRDPLVQLPHPAALISSKSLSEPLLNSPDPLLSSFSHPDSPSSSSPPSTQEASPTGDMAVGSPLMQEVGSPKDPGKSLPPVPPMGLPPPQEFGRGNPFMLFLCLAILLEHRDHIMRNGLDYNELAMHFDRLVRKHHLGRVLRRARALFADYLQSEVWDSEEGAEATAAS
Protein: Synaptojanin-2-binding protein (Mitochondrial outer membrane protein 25) (P57105)
Organism: Homo sapiens (Human)
Function: Regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:32973005}.
Interaction partners:
- Ribosome binding protein 1.
- Synaptojanin-2
- Protein Abitram
- Activin receptor type-2A
- Cytochrome c oxidase assembly protein COX16 homolog, mitochondrial
- Ras-related protein Ral-A
- Peroxisome assembly protein 26
Sequence:
MNGRVDYLVTEEEINLTRGPSGLGFNIVGGTDQQYVSNDSGIYVSRIKENGAAALDGRLQEGDKILSVNGQDLKNLLHQDAVDLFRNAGYAVSLRVQHRLQVQNGPIGHRGEGDPSGIPIFMVLVPVFALTMVAAWAFMRYRQQL
Protein: 4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (P14010)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Deaminates gamma-aminobutyric acid (GABA) to succinate-semialdehyde, which in turn is converted to succinate by the succinate semialdehyde dehydrogenase (By similarity). Required for the degradation of GABA, which is important for utilization of GABA as nitrogen source.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Succinate-semialdehyde dehydrogenase
- succinate-semialdehyde dehydrogenase [NAD
- succinate-semialdehyde dehydrogenase [NAD
- methylmalonate-semialdehyde dehydrogenase
- Glutamate decarboxylase
- Glutamate decarboxylase
- Aldehyde dehydrogenase
- aldehyde dehydrogenase
- Aldehyde dehydrogenase ALDH
- Aldehyde dehydrogenase family
Sequence:
MASAFRSSLKLRASARLPAVRTITTTPRLRAAEKPYFPNEPTAPKLATAIPGPKNKAASEQLNEVFDVRSLNMLADYTKSVGNYIADLDGNMLLDVYAQIASIPVGYNNPHLLKVAASPEMATSLINRPALGNFPSADWAHILKTGILKVAPKGLDQVFTAMAGSDANETAYKAAFMYYRQQQRGGPEKEFTEEEIQSSMLNQTPGSPQLSIMSFKAGFHGRLFGSLSTTRSKPIHKLDIPAFDWPQAPFPSLKYPLEEHAKENAEEEQRCLQEAERLIKEWHNPVAAIIVEPIQSEGGDNHASPAFFRGLREITKRNNVLFIVDEVQTGVGATGKFWAHDHWNLETPPDMVTFSKKAQTAGYYFGNPALRPNKPYRQFNTWMGDPSRALIFRGIIEEIERLFLVENTAATGDYLYSGLERLAKQYPEHLQNLRGKGQGTFIAWDTPKRDEFLVKGKGVGINIGGSGQNAVRLRPMLIFQKHHADILLESIEKIIKQL
Protein: Uncharacterized protein (Q57Y87)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFRKRYRPLDPAEERSVGVEQALHVGFLRDEQSYCFRWPDAPLTAMLRRSDDSLVLGMQSGSGSGTQNAVVLPPVPRLSAVLAEHDKAELFSSLSTNNTAISFSADSSSASGIVLNRGKRQFSAPASTCVDDSVFSFSSFQMKELESSGALKAFYEAHAFSTVSATGDGCDKVLKVLARRRMEEEIVRLEWRAYYETEKVSPAIQRILLLTVAVPFLDNFESSVLASTEGEAKWQRIIYELWVKWRIGSVKAGEVATASDGTPWGAPLLPGSFVSSLSREYFTTVGPDRSGALRGVRANDAKGADGEGCQVLSSAAVGRRGAYGYLRWRIDLYEPRLRAVPKEGDDEYGLSSSTKLVGAAEVNNIVEEKVPSVLCDVRLGGRVDPLDALALTDIRSDVGTWRQWLAHV
Protein: Glutathione-specific gamma-glutamylcyclotransferase (Gamma-GCG) (EC 4.3.2.7) (P87305)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Gamma-glutamylcyclotransferase acting specifically on glutathione, but not on other gamma-glutamyl peptides. Allows utilization of gluthathione through subsequent cleavage of the Cys-Gly dipeptide by Cys-Gly metallodipeptidase dug1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C11D3.15
- Uncharacterized protein C11D3.14c
- Glutathione synthetase large chain
- Putative aminopeptidase C13A11.05
- Glutathione hydrolase proenzyme 2
- Glutathione hydrolase proenzyme 1
- Glutathione S-transferase 3
- Glutathione S-transferase 1
- Cys-Gly metallodipeptidase dug1
- Glutathione S-transferase 2
Sequence:
MKTLSPEGSLWVFGYGSLIWHPPPHYDYSIPCFIKGYVRRFWMRSEDHRGTVNSPGLVLTLIPYEEWKQFSDWSFTPFDEGCWGMAFRIPAKYATQVREYLDDREVNGYTAHSVPVYAHTGDEIPVLENCLVYVGTSKSPQFQPSDDLTQMAKIISTRRGKSGDNFVYLFELAKCLRHLSPESKDIHVFELEAEVRKQMQKTR
Protein: Miles to go, isoform H (M9PD19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVRLNVAEQHSSSNNNGNISNSSISNTNGTIITSNNNAGGSCSSTTSSTTSLNSNPASPACTMVMLPAPQQHLLVQQQQQQQQQQQQQQQPQQPPPQLQQQHGPQQQQQQQQQQHSPSDGGSSNCSLPASPPLLQQTATPPQGAQIVPPVCALHHPQQQLALMAAMQHHHHLPPPHALHHAPLPPPPPNLPPPHENGHGGGGSGVAVGGGGISPNGGGGSSASSVSSLSSGSGGSGGQVNGLSNGTNGIAPLPPGQLYIQYPGEFYPPEYYIAPHPHEGICPQHPHHPHPHHHQPMCAMSTEYGKPQSKMITYTHCFDLKCPAVQMVSQNRPPPPMPVPVQVPQYVNENGTLTHVMLSPQQYQQLHPGQGHLHPAPFISANGTSHFYTPVAGYPGPGPAGNGPPHYHLPPPPPPQQQQQQPPQQPQQQAPQGPPPPQQQQQQQQQVAPPAVQGAPSTGSVGAAQGAPATATATHTHAHSHSHSHAHSHTHPQPHAHSPHSPSPPNYRDERSQRQHNKLLRKLEKQRESNPPHSPSPRRANELNGHNNNNIPPGVPLPGHLNNHHHAVNHQGRRLPQQHQGQAHQVAQQQQSQARNGNPQHPQRAGSSVGGASSVGTSEDGEDNSSLAGDDEEEYHRENSIIEQISAIEKPEVIDVTSRAAKIIWESPAIANTVTVDMRQLRYQVLLCDSGKQCKYKSLYQGEAYECIVQDLQPGQDYLVRLQVHYQKLTGTVSDPTEFRTPPCEPDQPPPPKLVSRTKNSINLRWAAPAANGASIQHYLLEYDEGRMPGQPQKFVELAKIKAKHYVIGKLQPTTVYSFRLAAVNEAGQSPYSPVASYSTSGNPPPVPKPPQLLASSSSSLKLGWERRAQDGDFLLQLQDAETGHGFLNTYKGTELQTECLQLRRASSYQFRLRSENEAGFSPWSPEVSYRTLAERPGRPGKPHAKGKIHGTQFKARWDAPSDSGGAEILCYHLELSAAGPAFERIYSGAETEAMCERLQPGTTYALRACCEGPAGQSPYSDIGHVTTEAVPPSAPPPPHCSDPPSPYAALLKLRPPEYNGGAPILEFEAQMRRLEQVQPPQLVYRGKQTYFVAQDLTPGGMYETQVRAINRIGAGSWSQWMRFTAAAAAPGVPEELRVLVKSATHLGVSWQPPLQENGAPVTSYTLKSASQERKEDDSEEEVKEPPSSEFHNCYQGPQTCAELRNLSPYTRYHFRIQASNSAGTGNSSDVISVCTPAAVPGAPQMQGYEFTAQEVTLNWTQPAAHGSPICSYNIEYGERTIATPDACTRYTVSGLMPETGYKFRVQAVNAIGAGAFSAYAKLTTQPAPPAPPRLECSGAGHNYIKLKWGENGNGKVVNSNPSGNGGDFTKYFVEMYVARAKQFQAVYSGTNCMCKVHKLQERSSYTFRIYAHTDRAGDGDYSEEFVFETSATLPANIKPPRVVQEGSVCLMELPGQLGMQLTLEWQHSKNSFNDRVEYELQYAVLGAAELEGESLSPKGRSSSSSGSSNGAPINLPNHDYRQLYRGPETKFTIDNLAAGTCYQFRVCPVRIAAGGELLYGQPSSPLRYQVPSELDPSSATCHHHLHGSTATPAMASSQRSSRKLSAGNGSTNGLHMRSVSASAISGASGVGADPVAIGRLQQELSGFNACADPQHHHHHHHHHHHQPCGGGVGGAGGISGATDSHHQHQHHMHHSHHMHHAHHPHTGMGGSSSNSSSSTAAAISSSLAQAGGLRRIVCKVTSLYSNRRRLSDQQKAVCIVVSFLVGTFLVAMLVNMLRG
Protein: Dermonecrotic toxin LiSicTox-alphaII1 (EC 4.6.1.-) (Dermonecrotic toxin 4) (DT4) (LiRecDT4) (Phospholipase D) (Sphingomyelin phosphodiesterase D 4) (SMD 4) (SMase D 4) (Sphingomyelinase D 4) (Q1W695)
Organism: Loxosceles intermedia (Brown spider)
Function: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) wih high activity. It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Shows high hemolytic activity. Causes dermonecrosis, induces inflammatory response, platelet aggregation and increases vessel permeability. Shows no lethality when injected at higher dose into mice. May cause complement-dependent hemolysis as well as in a complement-independent manner (By similarity). The hemolysis provoked in a complement-independent manner may be composed of several steps (By similarity). The toxin may bind to erythrocyte membranes, may hydrolyze membrane phospholipids (SM and LPC) thus generating metabolism products that may cause hemolysis, probably by provoking an increase of calcium inside cells (By similarity). The calcium influx may be due to the opening of L-type calcium channels, since L-type calcium channel blockers inhibit calcium influx (By similarity).
Subcellular location: Secreted {ECO:0000305|PubMed:17296256}.
Interaction partners:
Sequence:
MLLHIALILGCWSVFSEGAETDVAERADGRRPIWNMGHMVNGIWQIDQFVDLGVNSIEFDINFDKNGKPVYTYHGVPCDCFRSCLNWEYFGEFLTALRHRTTPGDKLYKEKLILFVFDMKTNSLYDNQAYQAGVNMATDIFKYYWNNGQNGGRAYFILSIPNLNHYDLIKGFRETITKKGHPELMEKVGYDFSANDNIPDVEKAYGKVGVTDHVWQSDGITNCIARGLSRVKEAVKERDSGGVINKVYIWTIDKFSSTRDALDAGVDGIMTNYPYVLNDVLKEGAYKNKFRMATYEDNPWVTFKA
Protein: Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (Bendless-like ubiquitin-conjugating enzyme) (E2 ubiquitin-conjugating enzyme N) (Ubc13) (UbcH13) (Ubiquitin carrier protein N) (Ubiquitin-protein ligase N) (P61088)
Organism: Homo sapiens (Human)
Function: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UB2V1, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production. UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:19340006}. Cytoplasm {ECO:0000269|PubMed:19340006}.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin thioesterase OTUB1
- E3 ubiquitin-protein ligase RNF8
- Ubiquitin conjugating enzyme E2 V1
- E3 ubiquitin-protein ligase RNF168
- E3 ubiquitin-protein ligase CHIP
- Ubiquitin-conjugating enzyme E2 variant 2
- TNF receptor-associated factor 6
- Baculoviral IAP repeat-containing protein 2
Sequence:
MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
Protein: At5g58020 (RTF2 RING-finger protein) (Q6NQ98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g25682
- Suppressor of mec-8 and unc-52 protein homolog 1
- Pre-mRNA-processing-splicing factor 8A
- Probable small nuclear ribonucleoprotein F
- Pre-mRNA-splicing factor 18
- DGCR14-like protein
- cyclin-dependent kinase
- Coilin
- RNA-binding motif protein 25
- SAC3 family protein A
Sequence:
MHIRRQIFVKSPDCQKVVALQLDPAQSLLTLSGITSLLESSQRISFSACSITLDGKLLNGSTRIQVSKLPSVSMLTLFPRLRGGGGDGGATGAESRDCYLNMYAEKKPDKVDPNEQRLSKWLNCALSNEPLAEPCVIDLLGNLFNKEVLVHALLSKRLPKQFSYIKGLKDMVNIKLTPVAGSDGSSQDTTSAQFQCPVSGLEFNGKYKFFALRGCGHVMSAKALKEVKSSSCLVCHADVKDSDKIVINGTEEEVDLLRERMEEEKAKLREKKGVSKKSKNGAAVVADTGAKVAKRQIEDGNVNGNGITVKKFKAADKVPVNATKEVYASLFTSSKKKSDFRETYSCRSLPLGRN
Protein: Cytochrome f, chloroplastic (Q8GZR2)
Organism: Euglena gracilis
Function: Translocates protons across the thylakoid membrane and transfers electrons from photosystem II to photosystem I. It receives electrons from the Rieske iron-sulfur protein and passes them to plastocyanin.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:12837550}; Single-pass membrane protein {ECO:0000269|PubMed:12837550}.
Interaction partners:
Sequence:
MASLQTPVMVGTVVGCVAGVVGFLAMSSNAATSLSVAPASTSTQIIANPSVIAPQYQGSVTSEDVAMEASQTDFAEVAEISSPVQVQSWSMIFSAMLAVPLAAAAMFFMKKSTTEERRPLVSIDDLLSVGKKAVVASAVVGAAAGSANAYPIFAQQAYGNPREATGRIVCANCHLASKPTEIEVPQAVLPDQVFEAVTKVPFSGPSGFFNVVDPSTVVGSVTFAGTQPVGFIQESGVPVSQALVDIATPGTPDTVFKATIKVPYDESLKQVAGNGRAAPLNVGAVLILPEGFRLAPPERIPEKMKEEINGLQFIQYSKDTPNILVVGPVPGKKYAEMTVALLSPDPRVDKKAEFGTLPIYVGGNRGRGQLYPTGEKSNNNIYNVEHSGKIADIQLNEKKRIYTVAVQQKDGEIINEDLPAGAELIVKVGDVVEAGQAISTNPNVGGFGQAESEIVLQNPGRVQAFLFFSFTVLATQTLLVVKKKQYEQVQLSEMNF
Protein: Lymphoid-specific helicase (PASG) (Q3BDS6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSGIVKEETRSISPHCPKPNESEEPEGTTIEETTMEKSKHEEMVITKEMEEEEKNLEEEGEKKEREMMEEARQSRGNDSQEMRFKRLQHLLEKSNIYSKFLLTKMEQQQQEEKLKKERLEKKAAVLKQKGSDKKTVKVERKKRGREDYKIADVMTKEEIMSKAKKPKMEEEAQASVKLEAEDIEKLSDTNSDIKGRLSETLRENSKQMLDPERTVNGQPVPAQQPQLFTGGVMRWYQVEGIEWLRMLWENGINGILADEMGLGKTIQCIAHIAMMVEKKVLGPFLVVAPLSTLPNWISEFKRFTPEVSVLLYHGPQKERLDLVKKIRQHQGSLRMCPVVVTSFEIAMRDRKFLQRFHWNYLIVDEGHRIKNLNCRLVQELKMLPTDNKLLLTGTPLQNNLSELWSLLNFLLPDVFDDLKSFESWFDISTITSDAENIVANEREQNILHMLHLILTPFLLRRLKSDVTLEVPPKKEIVVYAPLTNKQEAFYMAIVNKTIAKLLGQEKDESAPAPLTPSGRPKRRSRKVVNYTEPNTDSMKDLEKYLEKVQQELDSQASSTPVVNVFMPVDAQVNLKLQNILMLLKRCCNHAYLIEYPLDPTTGDFKIDEQLVEASGKFLILDRMLPELKKRGHKVLIFSQMTSILDILMDYCYLRGYEYSRLDGSMSYADRDENMKKFSSDPEVFLFLLSTRAGGLGINLTSADTVIIFDSDWNPQADLQAQDRCHRIGQTKPVVVHRLITANTIDEKILERASAKRKLEKMVIHKNKFKGSKAELKQSKSCLDVDELVELLKSRDYDGAVKGTKGKVISDKDLQILLDRSDLMDQAKKRVKQEKDGVFKVIEAKDDNGEISLS
Protein: phosphatidate phosphatase (EC 3.1.3.4) (A0A0B4JCQ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNIDEGDAPISSATNNNNTSSSNDEQLSAPLVTARTGDDSPLSEIPHTPTSNPRLDLDIHFFSDTEITTPVGGGGAGSGRAAGGRPSTPIQSDSELETTMRDNRHVVTEESTASWKWGELPTPEQAKNEAMSAAQVQQSEHQSMLSNMFSFMKRANRLRKEKGVGEVGDIYLSDLDAGSMDPEMAALYFPSPLSKAASPPEEDGESGNGTSLPHSPSSLEEGQKSIDSDFDETKQQRDNKYLDFVAMSMCGMSEQGAPPSDEEFDRHLVNYPDVCKSPSIFSSPNLVVRLNGKYYTWMAACPIVMTMITFQKPLTHDAIEQLMSQTVDGKCLPGDEKQEAVAQADNGGQTKRYWWSWRRSQDAAPNHLNNTHGMPLGKDEKDGDQAAVATQTSRPTSPDITDPTLSKSDSLVNAENTSALVDNLEELTMASNKSDEPKERYKKSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSGYINQSLEVDEYFPLLTNQDEFDYRTDIFDDEESEEELQFSDDYDVDVEHGSSEESSGDEDDDEALYNDDFANDDNGIQAVVASGDERTADVGLIMRVRRVSTKNEVIMASPPKWINS
Protein: UPF0589 protein C32H8.01c (Q9C0V9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Vacuolar protein sorting-associated protein vts1
- Putative MutL protein homolog 1
- Suppressor protein of bem1/bed5 double mutants
- DNA mismatch repair protein msh6
- DNA mismatch repair protein msh3
- MutS protein homolog 1
- DNA mismatch repair protein msh2
Sequence:
MLKKMPMSNKFENFYTLRQVSEVDKKPCFICYKPTKWVLITKTKLDFFYVCYNHLQDRGFATPISVIKSVTNKIDTNKLEAKDESKNVEKDATGNPQESKQEPNLEVQQTEKEKDVDSASAENESINSSSSSSKECSTQTQSKHYNLHRDIFQMRIRYHANRAAAEKTARLLQSGQGLPSPPSKPLP
Protein: ATP synthase mitochondrial F1 complex assembly factor 2 (C9J2Q2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MWRSCLRLRDGGRRLLNRPAGGPSASMSPGPTIPSPARAYAPPTERKRFYQNVSITQGEGGFEINLDHRKLKTPQAKLFTVPSEALAIAVATEWDSQQDTIKYYTMHLTTLCNTSLDNPTQRNKDQLIRAAVKFLDTDTICYRVEEPETLVELQRNEWDPIIEWAEKRYGVEISSSTSIMGPSIPAKTREVLVSHLASYNTWALQ
Protein: WD repeat-containing protein 1 (Q5RKI0)
Organism: Rattus norvegicus (Rat)
Function: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Enhances cofilin-mediated actin severing. Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusions. Involved in myocardium sarcomere organization. Required for cardiomyocyte growth and maintenance. Involved in megakaryocyte maturation and platelet shedding. Required for the establishment of planar cell polarity (PCP) during follicular epithelium development and for cell shape changes during PCP; the function seems to implicate cooperation with CFL1 and/or DSTN/ADF. Involved in the generation/maintenance of cortical tension. Involved in assembly and maintenance of epithelial apical cell junctions and plays a role in the organization of the perijunctional actomyosin belt (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15337274}. Cell projection, podosome {ECO:0000250|UniProtKB:O75083}.
Interaction partners:
- F-actin-capping protein subunit beta
- Cofilin 2
- Cofilin-1
- Actin-related protein 3
- Actin, cytoplasmic 2
- Actin related protein 3B
- Filamin, alpha
- Adenylyl cyclase-associated protein 1
Sequence:
MPYEIKKVFASLPQVERGVSKILGGDPKGDNFLYTNGKCVILRNIDNPAVADIYTEHAHQVVVAKYAPSGFYIASGDISGKLRIWDTTQKEHILKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDTGSSVGEITGHNKVINSVDIKQNRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIFIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVNVNSVVSTFPMGSNVLDQQLGCLWQKDHLLSISLSGYINYLDKNNPSKPLRVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGENDSFSGKGHTNQVSRMTVDESGQLVSCSMDDTVRYTNLTLRDYSGQGVVKLDVQPKCVAVGPGGYTVVVCIGQIVLLKDQKKCFSIDNPGYEPEVVAVHPGGDTVAVGGSDGNVRVYSILGATLKDEGKLLEAKGPVTDLAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETKVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY
Protein: Synaptonemal complex protein 2 (SCP-2) (Synaptonemal complex lateral element protein) (rnSCP2) (O70608)
Organism: Rattus norvegicus (Rat)
Function: Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase. Plays a role in the assembly of synaptonemal complexes. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility. Required for insertion of SYCP3 into synaptonemal complexes. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements.
Subcellular location: Nucleus {ECO:0000269|PubMed:9933407}. Chromosome {ECO:0000269|PubMed:9592139, ECO:0000269|PubMed:9933407}. Note=In axial/lateral elements of the tripartite segments of synaptonemal complexes. {ECO:0000269|PubMed:9933407}.
Interaction partners:
- Synaptonemal complex protein 1
Sequence:
MPVRPDPQQLEKCIDDALRKNDFKPLVTLLQIDICEDVKIKCSKQFLRKLDDLICRELHKKDIQTISNILISIGRCSKNIFILGQTGLQTMIKQGLVQKMVSWFENSKEIILSQRQSKDEAVMNMIEDLFDLLMVVYDVNDEGKNQVLESFIPHICALVIDSRVNFCIQQEALKKMNLMLDRIPQDANKILCNQEILTLMSNMGERILDVGDYELQVGIVEALCRMTTEKRRQELAYEWFSMDFIANAFKKIKDCEFETDCRIFLNLVNGMLGDRRRVFTFPCLSAFLGKYELQIPSDEKLEEFWIDFNLGSHTLSFYIAGDDDDHQWEAVTVPEEKVDMYNIEVRESKKLLTLTLKNIVKISKKEGKELLLYFDAALEITNVTKKLFGGNKYKEFTRKQDISVAKTSIHVLFDASGSQILVPESQPSPVKENLIHLKEKSNLQKKLTNPLEPDNSSSQRDRKNSQDEITTPSRKKMSEASMIVPDTDRYTVRSPILLINTSTPRRSRAPLQAIHSAEKAVSKTSESGVDYAVSLKSRQSDGRNRGNNRANHNKTATVQNKGHEHHESPDQTFNEIEETLSDAYAVEKVDKPVLPGVLDISKNKAHSRWACWTPVTTIKLCNNQRSCALPGDTFTQDTGVNKKCTKQKSVSDDDSEETQRVKYSKDVIKCNKSEEAEVCERNIQEQNHPKYSQKKNTANAKKNDWHIESETTYKSVLLNKTTEESLIYKKTCVLSKDVNTTICDKSPSRKSMRSHTKSRKELMSEVTSCELDEIPVRENSKGKRFTGTAESLINLINKRYNSSDDMISTRKLKEPRDGSGFSKKPELQFNKVQRKSYRKLKTVVNVTSECPLNDVYNFSLNGADEPVIKLGIQEFQATTREASMDNSIKLVDVRNRDERDLSLKTKDERILSHERKTLFSDTETECGWDDSKTDISWLRKPKSKRLMDYSRNKNTKKCKSIKSRSSTEKGQPRSTVVLSKNIAKNDYEVIVDGRTRLPRRATKTKKNYKDLSTSGSESESEKEISYLFKDKLPTKEETVHSSAQTKKLPKKQQKVFNTEALKGQPSEEQKNSSTLRNGREDSLYLSSASVSGSSSSVEVMRCTEKITERDFTQDYDYITKSLSPYPKAASPEFLNRSNRVVGHGKSPRISETSAVCVRKSCSPASGLPFSPRHTTKNNSVMNIKNTNSVINNQRTQHCNSYSDVSSNSSEKLYMEPESPDSCENHVQSKREENHAASPFSLSSEKIEKIWFDMPNDNTHVSGPSQRGSKRRMYLEEDELSNPSEAEVQEAEEREHLVSKKLCQREHFDQHTSETSLSTPEFSVPKDWQQELQGAGMFYDNINSDYKRKTDTQHKIMDDFTTKTLKLTQQHLLAMACQARGHRDENIDKFQVTLLDELEKVEKDSQTLRDLEKEFVDIEEKIVHKMRAFHQSERERFRALKTSLDKSLLVYNSVYEENVLTSEMCLMKANMKMLQDKLLKEMHEEELLNIRRGLESLFKDHEGNNA
Protein: Small polypeptide DEVIL 10 (Small polypeptide ROTUNDIFOLIA LIKE 12) (Small polypeptide ROT-FOUR-LIKE 12) (Q6IM91)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q7XXN8}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 6
- AT1G25275 protein
- At3g13845
- Transmembrane protein
- Protein RALF-like 24
- Succinate dehydrogenase assembly factor 4
- Small polypeptide DEVIL 6
- AT4g05070 protein
- Transmembrane protein
- Secreted transmembrane peptide 5
Sequence:
MCLFMSNSSLPTKPNRKTRFGDRCLLMAKQQRTRLYILRRCVSMLLCWHDHSISD
Protein: Myosin-11 (G5EBY3)
Organism: Caenorhabditis elegans
Interaction partners:
- Myosin regulatory light chain
- Myosin-2 essential light chain
- Actin
- Anillin-like protein 1
- Protein ECT2
- EF-hand domain-containing protein
- Rho-associated protein kinase let-502
- EF-hand domain-containing protein
- Myosin, essential light chain
- WAPL domain-containing protein
Sequence:
MTSSRQKDDEIDQLRAKTDFLNPSISADWAKKKLMWVPSEKDGFALGAVIGEPHADGTIDIELMETGERQRVSSDDCQKPNPPKYDKCEDMSMLTCLNEASVLHNLKQRYFSNLYYTYSGLFCVVINPYKRIPIYTDTIAEQFKCKKRKEMPPHIFAVADEAYRSMLQERDDQSILCTGESGAGKTENTKKVIQYLAYVANRSMVKNRKTSVDLDTSTNRIMGQLEEQLLQANPILEAFGNSKTVKNDNSSRFGKFIRVHFDSTGCISGANIEFYLLEKSRVLKQAPNERSFHIFYQLLKGLSKVQREHYLLEDSLSKYKFVSNGDSKLAGVDDGAEMKETLNAMSIMGLNDEEIGGILRVVSAVMLFGNLEFSHENKNNDQAVLLNDAVAQKIASLLGVNVTELMRAFLKPKIKVQRDLVHRAQSVDQVNFSVGAIAKASYERLFRWLVHRLNKSLDRTRQQSVSFIGILDIAGFEIFETNSFEQLCINYTNEKLQQLFNNTMFVREQQEYLDEGLEWKFLDFGLNLQPTIDLIDKPMGIMSTLDDVCLFPQGNDQSFVQRLNNTHSQHPKYVVPEIRSRSDFAVVHYAGRVDYQSEGWRVKNMDPLNENVIDVLKTSKESLIVDMWKDIADVCSLSAADSTSDTGVFGSRVPKKGMFRTVSQLYKEQLARLMSTLNNTNPHFVRCIIPNHEKKHGVLNAHLVLDQLRCNGVLEGIRICRQGFPTRLPFQEFRQRYEKLLAPDVNPAGFMDGKNAVYRIVQYLEVDANLFRIGQSKIFFRSGVIAEFEEMRDQKLSALIESFQAQCRGWLGRRVMVRRREQEVAIKILQRNGLAWMRLREWQWWRLLTKVKPLLEVTNKDELIAEREQELKVTAEKLRRSEVFISDYKQQMEKMDEERLVLKTRLDAESSERAEIFEERSRMAARRDELEGILEEVSKRLEIEEQKAKKADSESRKLTEMVRHLEENLEDEERSRQKLLLEKNSIESRLKELEAQGLELEDSGNKLSKEKKALEERCEDLSSRLIDEVERSKQLVKAKARLEATVAEINDELEKEKQQRHNAETARRAAETQLREEQESCLEKTRKAEELTNQLMRKESELSQISIRNDEELAARQQLEREIREIRAQLDDAIEETNKEKAARQKAEKARRDMAEELESYKQELEESNDKTVLHSQLKAKRDEEYAHLQKQLEETVKSSEEVVEEMKAQNQKKIEELNETIDQLKRQKISADKAKSSAESDNENFRAELSNIASARLEAEKKRKAAETSLMEKDHKMREMQSNLDDLMAKLSKMNNELESIQKAKSADETLNSNLLKKNASLDMQLSELTEASEEDRRTRATLNNKIRQLEEDLAVAVEARDDALDAQEKIEKEVKEVKSLLAEARKKLDEENREVMEELRKKKEKELSAEKERADMAEQARDKAERAKKKAIQEAEDVQKELTDVVAATREMERKMRKFDQQLAEERNNTLLAQQERDMAHQMLRDAETKALVLSNELSEKKDIVDQLEKDKRTLKLEIDNLASTKDDAGKNVYELEKTKRRLDEELSRAEQQIIELEDALQLADDARSRVEVNMQAMRSEFERQLASREEDEDDRKKGLTSKIRNLTEELESEQRARQAAIANKKKIESQISELTEKNEASLRQIEDLSRQLRKAQLGWKDLQLDVTEARAAMEDALAGQRDAEKRARASEDEIKRLTADIQAVSSSKRKAEAERDELIEEVSSLRASSFSNEEKRRLEAKVIDLEDQLDEEASANELAQEKVRKSQQQLEQMTADLAMERSVCERTESDKIALERANRDLKQQLQDAENTAVARLRTQINVAEAKVSSLEQQLSLEEQDKMRQGRTLRRMETKMAEMQQMLEEEKRQGESNRQAVDRQNARIRQLRTQLEDTEAERDRLTNKLKDERRRAEEMTDLNETLSRDVSLLKQRETTARRTPGLIGHRESRRFGSNTSLARDEFRGSALTNEMSPSDRPASRLTSGTGSQLGNTDEDRDSVRN