wanglab/gogpt-training-data huggingface dataset:
Protein: Myosin heavy chain-like, isoform A (Q9VEZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFNFMKKSAGDEDKERRKREKKLRKEAKGTSGGPGMGGVTGVTGSMSTDELLRLDEVRRSLKIRGRRKEKEKLPSGITADYSADFFAALNADANGGSNGGAVGAADPEQDRGNEEIVASVMTHIESRASNGAGVSVNYSEVTHSLLSGGLKNRFLPPIPPKPPKRGILKGSRSNMTNVHEEISFAGSAGGAGGTPEMLLRNTFQNESLYEGAARGAGSIGSNSSQHGTSFTSVESLRSDGEQTGGQQRAMTLPANARYGALPQGNSQGSHLHVLTSPSPSADSLTDTTNSSFATPPFSLSPVGESQGIDRWARVHAFEDVELPLPPVQLVKLPPPRQLVIRRQKSPRQDFGFSLRKAICLDRTESLTSPIFRPVIFAEPGAGGGATGLLPGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQPVAELVELSKRCMAPSTATVEEIDHSITNGNCNTLRRSASKRFKRQSRHENGNGGGEEGGAKGVGHDLEADVADASQPERVWLVHRGGFTAAIRLPTASSGRDEENKLSLRLLHNGEQLTVDEDDVEKQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSMFRGCKTEDMPPHVYSLAQTAYRSLVETRRDQSLIFMGRSGSGKSTSFKHALNYLALAAGAYNNFINAEKVNALCTILEAFGNTKTCLNSNATRMTQLLSLDFDQTGQIASASLQVLLPERQRAGRRLGHEHSFHIMTRLLAGAAGLLQKELHLENITSEDSHPFISLSQKLEDRHRAANDFMRTVQAFETLNIDAKAVRGIWSILAAIYHLGIAGVTKLGTGSTARTQFANPTAARKASGLLGVNLEDLSSAAFGLTQPNAPNGGLSPSKSPTSDTGHEWAWECLEALVIGLYSEALAAVVALINRQICTSSHTIASIMLIDTPGFQNPASCGQQVGATLADLRHNYLQERLQMLFHHTTLVAPRDRYAQELVEIEMDLASECHPGPLISLIDKAPQNHVVRSSQRDLREHDRRGMLWLLDEEAIYPNSNDDTFLERLFSHYGDREHHSLLRKCAGPRQFVLHHLQGTNPVLYAVDGWVRHSREHPGIRNAVSLLQDSSREEINRLYIGSLTRGSGAMVFCGSFAGLEGTQSLRRVSSIRRSFTTAGVKRNSIMLQVKFTVDGIIDTLRRTGTHFVHCYLLQHNAGKHTKYTANGSPSSAAGQVSSEEEMVNVPLLRSQLRGSQVLEAARLHRLGFPESVPLLEFVRRFGLLAGDLASNKDVSVEQILAVNELDVASYRIGPSQILFRSGVLSELEAKRDVLLSDRIIQLQAFCRGYLARKKMSQRRVQELAVRCIQRNVKAFLAVRDWPWWRLLVRVTPLLNVHRTEEQLKTANEELLMLRAKLEKIECDRSEVKAENQKLEAKLSELTVDLAEERSTAHIATERLEAETAERLKLEKELGDQTNKVKNLQETTEKLEMELICAKSDLNGISEDEDAENEDGVGGGVYKLKYERVARELEFTKRRLHTQHEHDLEQLVALKKHLEMKLSDAYEEVVEQRQVVGQWKRKAQKMTNEMNDLRMLLEEQNARNNLLEKKQRKFDAECQSLQDAVRQERQAKERYGREKDVLQAEKFTLEQTLADTRLDLEFKEEKLASLQRELEEMTFGGGTEEEFAQLRRSKNETERRAKEQEEELDEMAGQIQLLEQAKLRLEMTLETMRKEARRESQQRDEELEEVRGNGYKKIKALECQLETEHEERTLLLREKHELERRLSSMEDRDRVDRDAEEALNQKLRRDLRKYKALLKDAQTQLERLKADTPGKTLIRQLRNQLEDAESARSLAMKARQTAEAELTEVQAMFDESHRARNDAEERANAAHRDRAELQAQIEENEEELGELMKKYSATVKQLNTEQINVSEAEFKLNEMEAERNNLKEQVAELQHRLDNVENLGDPSMAMMSKRLELRTKELESRLELEQATRARLEVQVNRHKEALEKLQNEVTQSKMREMQAQDVIKKSQKSLRDMREEFHAVSSREQESLTRRKDLEKKVEQMESEGAALKNDLRLALQRIADLQQAMEEEGEEELSESDESLSSVGSISDLEDRLRPVHVKRSSQQSLNGSIGGGGGSVVSSTRTVVFEKDDNSPRNNAK
Protein: Apical junction molecule ajm-1 (jam-1) (A0A1C3NSL9)
Organism: Caenorhabditis elegans
Function: Controls adherens junction integrity. Required for the correct rate and completion of elongation of the embryos.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Cell projection, cilium {ECO:0000269|PubMed:27623382}. Cell junction, adherens junction {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}. Note=grdn-1-dependent localization at sensory neuron dendritic tips (PubMed:27623382). The coiled-coil domain is sufficient to localize to apical junctions (PubMed:11715019). {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:27623382}.
Interaction partners:
- Disks large homolog 1
- Protein Scribble homolog let-413
- Alpha-catenin-like protein hmp-1
- Moesin/ezrin/radixin homolog 1
- Secretory carrier-associated membrane protein
- Cell junction protein VAB-9
- Cadherin-related hmr-1
- Protein unc-119
- Microtubule-actin cross-linking factor 1
- Protein kinase C-like 3
Sequence:
MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHKLADADRDQEEELVFNEERRKTVTMDDNASLRSASITFDANRDEQDLLNESFASNPTDETVLMQKTKDEMDATSERPRSPLDLPPPPASVVLHPSAPPPPPPPLSSTEVVGNTTTTTTTHYAPKTWNDPSITTAPKIPVSLLSGAQPLPSVLTQRTTTSSYSAPNYSASSMSGVPSDVAPPPPLPIPNQSSSSAASYQHHHASSISKSISSSREDLLSEHATSRSTVREIPVHRAPSTAPSHSSVFEYHMMPTTTSTYHHVETPSDEYYRREVMTRTIITRSTEALSQTPLGRPASPLDRYLPYPTTTTTTSGDGRTREEKTVDYKVTYHRDIEEQERRIREDQARRQQEEQDRRDREDNARRILAQREHQEMERLREQQNLSERALAERERADKERLQQERLLRQQREKKRREEWDRLESIRLAEEEAELARRRALEKERIDREKAEEERKTMERLERERARLERERLEEERRQKEKAETERIERERREHERIEIERIERIKRERIERERREREEKKAEEDRLLRERLELERIERERRELEARERQELELQRREAEDRERQRLEDEAREMRRREEERREAELVADVHRQAEERERLRKRQEREEAERLERIRLEQQKIDMERIDAERRERERKEEERREFELIEAARRKKEARDRDRLDEMERERVREEEERREKERREQERRIAAEKERKRRQEEEEEIARLNELQRAAAARQAQRNAELDRQRQRDELDRKAQELSEREMREKERRDRERANEEAQLADLLERERHNQLIRENERREAVERANNRRLEDRRSRDKLDHIVRERSEKEQFELEKRRLLAEKEAMNRKKNHLLSSETLAKLTQPMYYTTREPEVTTKVERQVIERIDRNVWVEDVPYAPSQSAMGYLDNDENNRDRLYNPNDLNRNGSSRSRYQRAKNEKARRDFYHSSQDSADPVTERFRKSTDDLTTRSRPEYRGPLLQKFHDSEFRTTALNETDGLPYRRMGPSPYEQPFAKLLEETERRYAHYNSRASNPSIYQSSRYYYPERHGQPQHTDNTRAESVVAYERESRRESPADQAHIRSRSADYLMDRRIREETEVPENQLQKTRVEPHDQSPRESRISEYEMRFRKSTEKLTVPDWYRENRPQGQTAQTSTYRYGNGVEPMSTTTTTTTVINGTSSHQQAPPPVPPQPIGNIGLPRGMFDRYKDDIEELRRSRSSLHQTGQQETSNRQGSTLSVGGIVDQGHALPGYTVSEVPNAWNLHTSRTSRVVEVADTFVGTSSHEYGNFTNRYGGRVTIEEVLDSIFQKVTPTNQRLNFDRSYPQADELFQGNVDGPGIYTNNYSVMRQVLKSPERAEHILQNEELFVRCTECHRTRELSAARLFFVSCKHCYTYYCSRECRHNNWPNHSGRCSFARINTLCKDVIMKVREDEQAQAFMSKVARDGFSVSGRGSVNIRLSSPQLAQAYVSNGWRALSAYPNDQLLYYYTVKALIAERKEPSLIALCNRYEPREKFILSVSIIADIEHCPETPPPETRELSAVQFSSPRSRYEAIQNQNAPYFSEFAHNV
Protein: RNA polymerase II subunit A C-terminal domain phosphatase (EC 3.1.3.16) (K7EJD2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU366066}.
Interaction partners:
Sequence:
ASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVRDPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELAGAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMDKERPQEEAE
Protein: Acetylserotonin O-methyltransferase (EC 2.1.1.4) (Hydroxyindole O-methyltransferase) (HIOMT) (P46597)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
Interaction partners:
- Serotonin N-acetyltransferase
- Cytochrome P450 1A2
- Cytochrome P450 1B1
- Indoleamine 2,3-dioxygenase 1
- Cytochrome P450 1A1
- Indoleamine 2,3-dioxygenase 2
- Aldehyde oxidase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
Sequence:
MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHGTELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPTSQCSMLKYMGRTSYRCWGHLADAVREGRNQYLETFGVPAEELFTAIYRSEGERLQFMQALQEVWSVNGRSVLTAFDLSVFPLMCDLGGGAGALAKECMSLYPGCKITVFDIPEVVWTAKQHFSFQEEEQIDFQEGDFFKDPLPEADLYILARVLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYSLNMLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARK
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (Q7KTP1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MFCFLLVFGVNVVLVHLTTGEFSANVQPDVEAMAAAALSGMEMGSGPGSEGYEDADNEKSKTVENARSLTCYCDGSCPDNVSNGTCETRPGGSCFSAVQQLYDETTGMYEEERTYGCMPPEDNGGFLMCKVAAVPHLHGKNIVCCDKEDFCNRDLYPTYTPKLTTPAPDLPVSSESLHTLAVFGSIIISLSVFMLIVASLCFTYKRREKLRKQPRLINSMCNSQLSPLSQLVEQSSGSGSGLPLLVQRTIAKQIQMVRLVGKGRYGEVWLAKWRDERVAVKTFFTTEEASWFRETEIYQTVLMRHDNILGFIAADIKGNGSWTQMLLITDYHEMGSLHDYLSMSVINPQKLQLLAFSLASGLAHLHDEIFGTPGKPAIAHRDIKSKNILVKRNGQCAIADFGLAVKYNSELDVIHIAQNPRVGTRRYMAPEVLSQQLDPKQFEEFKRADMYSVGLVLWEMTRRCYTPVSGTKTTTCEDYALPYHDVVPSDPTFEDMHAVVCVKGFRPPIPSRWQEDDVLATVSKIMQECWHPNPTVRLTALRVKKTLGRLETDCLIDVPIKIV
Protein: Carboxypeptidase A6 (E7F2H8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Proprotein convertase subtilisin/kexin type 1 inhibitor, like precursor
- Carboxypeptidase E
- Neurotensin.
Sequence:
MALRSTDVSSNVKSAVLLGCVLILCTAPNNVDSYLYNNRYVGDQVFRIIPSSKPEVQAVKQLFQNLTVDLWQPNSASLIRENSSIDVHVRRDKTHWLRNHLHQEHIYYEVLISNLQTEIEKQTGYRSSRKRRSELQYDYEVYHPLEEIQSWMFEMNRTHSHLVDLFSIGQSYEGRPLYVLQLGKRTRFFKKAVWIDCGVHAREWIGPAFCQWFVKEALNSYQHDSSMRRLMNQLNFYIMPVFNVDGYHYSWKMDRFWRKTRSKIPKYHCRGVDANRNWKVKWCDEGASLHPCDDTYCGPFPESEPEVKAVAKFLRKHKKRVKAYISMHAYAQMLLYPYSYKYATIPNFNCVESAAQNAVSALYSAYGVRYRYGPASSTLYVSSGSSMDWAYKNGIPYAFAFELRDTGYYGFLLPEALINPTCTETMRAVKTIASGLLRKCTK
Protein: NEDD8-conjugating enzyme Ubc12 (EC 2.3.2.-) (RUB1 carrier protein 1) (RUB1-conjugating enzyme 1) (Q9SDY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin-like protein NEDD8/RUB1 from the ECR1-AXR1 E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- RING-box protein 1a
- NEDD8-like protein RUB3
- NEDD8-activating enzyme E1 regulatory subunit AXL
- NEDD8-activating enzyme E1 regulatory subunit AXR1
- F12F1.16 protein
- RING-box protein 1b
- Ubiquitin-like modifier-activating enzyme 5
- Ubiquitin-NEDD8-like protein RUB1
- Ubiquitin-activating enzyme E1 1
Sequence:
MIGLFKVKEKQREQAQNATRGGASVKKQSAGELRLHKDISELNLPSSCSISFPNGKDDLMNFEVSIKPDDGYYHNGTFVFTFQVSPVYPHEAPKVKCKTKVYHPNIDLEGNVCLNILREDWKPVLNINTVIYGLFHLFTEPNSEDPLNHDAAAVLRDNPKLFETNVRRAMTGGYVGQTFFPRCI
Protein: protein deglycase (EC 3.5.1.124) (Maillard deglycase) (Parkinsonism-associated deglycase) (Protein DJ-1) (Protein/nucleic acid deglycase DJ-1) (V9HWC2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
Interaction partners:
Sequence:
MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQVKAPLVLKD
Protein: Fondue, isoform A (Q8INW9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKLLILALCLGVVCGDFQQSHYSTHGQAVEQARKNAGYGGGYSGSFGAGVDGASAQVDDSALGKLESSYDSVGATESAEGASAGGLGGAVETLGGSAGTNTIGAGVGSSFGSNFASGFGGQNAASFGAQNAAGFGAQNAASFGAQNAASFGSSFSSNAAFQTSSASNFGSTAAHQVGSNVEFADNANAGNKVDFGGVNAVDSSAQLLSGVQTVQSVPTSEYYRHEKIVSTPQQVVYTIPGGSQRYVHHEERIVEQPTQVTQTVPVQTAHYYQRKVTTTASAPQLVQPVASSRLTYGSNAASTFGSNAASNFGSNAATNFGSNAATNFGSNAAFNSQFGSSYGQNFQQNSQLSQLLSQTQQAARQQAALQAASANQVQAGSGYAAGSQGGFNSGYNSAFNSGSQFGFNSASSLNSASSLNSASTGNSAALLSGSLLGGSQGSLLSGQVGGQQSLLSGSLLSGQQNLGLGLNAAQTGQVVGASSVGAGLSAGAGNLGSGYRTKQWEKQSKWSSQNSYDSNGHVNNYKDLVTGESESVDINGKRAGYHAVTASVDDNGKIGTHSVHS
Protein: Arsenate reductase (EC 1.20.4.1) (Arsenical pump modifier) (P0AB96)
Organism: Escherichia coli (strain K12)
Function: Involved in resistance to arsenate. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)].
Interaction partners:
- Arsenical pump membrane protein
- Arsenical resistance operon repressor
Sequence:
MSNITIYHNPACGTSRNTLEMIRNSGTEPTIIHYLETPPTRDELVKLIADMGISVRALLRKNVEPYEELGLAEDKFTDDRLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLEILPDAQKGAFSKEDGEKVVDEAGKRLK
Protein: N-acetylgalactosaminyltransferase 4 (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) (pp-GaNTase 4) (Q8IA42)
Organism: Drosophila melanogaster (Fruit fly)
Function: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the diglycosylated Muc5AC-3/13 as substrate.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Transport and Golgi organization protein 1
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
Sequence:
MAIKKRYVKRLLRKVVLLLVVIVTVSLVTTLVVERRMKNAAELTEQLDPNGDPITPVFRAANIHPTRKAPRPPFQDRNSVVDIPRSDKLQGFRLPEPKGERKDWHDYAAMEADRKRSGFGEHGVAVKIENPDEKQLEKEHYEMNGFNGLISDRISVNRSVPDLRLEACKTRKYLAKLPNISVIFIFFNEHFNTLLRSIYSVINRTPPELLKQIVLVDDGSEWDVLKQPLDDYVQQHFPHLVTIVRNPERQGLIGARIAGAKVAVGQVMVFFDSHIEVNYNWLPPLIEPIAINPKISTCPMVDTISHEDFSYFSGNKDGARGGFDWKMLYKQLPVLPEDALDKSMPYRSPVMMGGLFAINTDFFWDLGGYDDQLDIWGGEQYELSFKIWMCGGMLLDVPCSRVAHIFRGPMKPRGNPRGHNFVAKNHKRVAEVWMDEYKQYVYKRDPKTYDNLDAGDLTRQRGVRERLKCKSFHWFMTEVAPDFLVKFPPVEPPSYAAGIIQNVANPVYCLDNMGKSTEEAVGMFSCADNRTHPQPNQFWELSIFRDLRMKGFDSVCLDVHEGPPNATVWMWSCHSQGGNQFWYYDRQTQRLVHGENNKRCLEGFVENGIAKVVANSCENGNDRQRWEFGFVNHTMLDTFYDGLK
Protein: WD repeat-containing protein 5 (Q498M4)
Organism: Rattus norvegicus (Rat)
Function: Contributes to histone modification (By similarity). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (By similarity). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (By similarity). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (By similarity). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (By similarity). May regulate osteoblasts differentiation (By similarity). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein dpy-30 homolog
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Retinoblastoma-binding protein 5
- Histone-lysine N-methyltransferase
- 5'-AMP-activated protein kinase subunit gamma-1
- Histone acetyltransferase
- Host cell factor 1
- CXXC-type zinc finger protein 1
- KAT8 regulatory NSL complex subunit 1
- [histone H3]-lysine
Sequence:
MATEEKKPETEAARAQPTPSSSATQSKPTPVKPNYALKFTLAGHTKAVSSVKFSPNGEWLASSSADKLIKIWGAYDGKFEKTISGHKLGISDVAWSSDSNLLVSASDDKTLKIWDVSSGKCLKTLKGHSNYVFCCNFNPQSNLIVSGSFDESVRIWDVKTGKCLKTLPAHSDPVSAVHFNRDGSLIVSSSYDGLCRIWDTASGQCLKTLIDDDNPPVSFVKFSPNGKYILAATLDNTLKLWDYSKGKCLKTYTGHKNEKYCIFANFSVTGGKWIVSGSEDNLVYIWNLQTKEIVQKLQGHTDVVISTACHPTENIIASAALENDKTIKLWKSDC
Protein: Evasin-4 (EVA4) (P0C8E9)
Organism: Rhipicephalus sanguineus (Brown dog tick) (Ixodes sanguineus)
Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL3, CCL5, CCL7, CCL8, CCL11, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL21, CCL22, CCL23, CCL24, CCL25 and CCL26 with nanomolar affinity. Binds to CCL3 and CCL5 with 1:1 stoichiometry. Although binding to CCL25 is observed, does not inhibit CCL25-induced chemotaxis.Has been shown to reduce cardiac injury and inflammation in mice through its anti-CCL5 activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAFKYWFVFAAVLYARQWLSTKCEVPQMTSSSAPDLEEEDDYTAYAPLTCYFTNSTLGLLAPPNCSVLCNSTTTWFNETSPNNASCLLTVDFLTQDAILQENQPYNCSVGHCDNGTCAGPPRHAQCW
Protein: Ankyrin 2 (A0A5F9ZI15)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKDNNE
Protein: Organic cation/carnitine transporter 2 (CT1) (High-affinity sodium-dependent carnitine cotransporter) (Solute carrier family 22 member 5) (UST2r) (O70594)
Organism: Rattus norvegicus (Rat)
Function: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76082}. Apical cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 15 member 2
- Mitochondrial carnitine/acylcarnitine carrier protein
- Solute carrier organic anion transporter family member 4C1
- Solute carrier family 15 member 1
- Trimethyllysine dioxygenase, mitochondrial
- Multidrug and toxin extrusion protein 1
Sequence:
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFNGMSIVFLAGTPEHRCLVPHTVNLSSAWRNHSIPLETKDGRQVPQSCRRYRLATIANFSALGLEPGRDVDLEQLEQENCLDGWEYNKDVFLSTIVTEWDLVCKDDWKAPLTTSLFFVGVLMGSFISGQLSDRFGRKNVLFLTMGMQTGFSFLQLFSVNFEMFTVLFVLVGMGQISNYVAAFVLGTEILSKSIRIIFATLGVCIFYAFGFMVLPLFAYFIRDWRMLLLALTVPGVLCGALWWFIPESPRWLISQGRVKEAEVIIRKAAKFNGIVAPSTIFDPSELQDLNSKKPQSHHIYDLVRTRNIRIITIMSIILWLTISVGYFGLSLDTPNLHGDIYVNCFLLAAVEVPAYVLAWLLLQHLPRRYSISAALFLGGSVLLFIQLVPSELFYLSTALVMVGKFGITSAYSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFFPESFGAPLPDTIDQMLRVKGIKQWQIQSQTRTQKDGGESPTVLKSTAF
Protein: Tubulin alpha-1C chain (EC 3.6.5.-) (Alpha-tubulin 6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain] (Q6AYZ1)
Organism: Rattus norvegicus (Rat)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-4B chain
- Microtubule-associated protein tau
- Tubulin beta chain
- Tubulin beta chain
- Cell division control protein 42 homolog
- Tubulin beta-5 chain
- Tubulin beta-3 chain
- Tubulin beta-2B chain
- Tubulin beta-2A chain
- Granzyme B
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLARVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSAEGDDEGEEY
Protein: Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) (Q8VEE4)
Organism: Mus musculus (Mouse)
Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus, PML body {ECO:0000250|UniProtKB:P27694}.
Interaction partners:
- Replication protein A 14 kDa subunit
- DNA topoisomerase 3-alpha
- RecQ-like DNA helicase BLM
- RecQ-mediated genome instability protein 1
- Replication protein A 32 kDa subunit
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- DNA repair protein RAD52 homolog
- Fanconi anemia group M protein homolog
- Protein timeless homolog
- TIMELESS-interacting protein
Sequence:
MVGHLSEGAIEVMIQQENTSIKPILQVINIRPISTGNRSPRYRLLMSDGLNTLSSFMLATQLNTLVEGGQLASNCVCQVHKFIVNTLKDGRKVVVLMDLEVMKSAEDVGLKIGNPVPYNEGYGQQQQQQQQQQQQAVPSPASAATPPASKPQPQNGSLGMGSTAAKAYGASKPFGKPAGTGLLQPSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGALKIANKQFSAVKNDYEMTFNNETSVLPCEDGHHLPTVQFDFTGIGDLESKAKDALVDIIGICKSYEDSIKITVKSNNREVAKRNIYLMDMSGKVVTTTLWGEDADKFDGSRQPVMAIKGARVSDFGGRSLSVLSSSTVIVNPDIPEAYKLRGWFDSEGQALDGVSISDHRSGGAGGGNTNWKTLHEAKSENLGQGDKADYFSTVAAVVFLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDREFPNFKYRMILSANIADFQENQWVTCFQESAEAILGQNTMYLGELKEKNEQAFEEVFQNANFRSFTFRIRVKLETYNDESRIKATVMDVKPVDFRDYGRRLIANIRKNM
Protein: U-box domain-containing protein 75 (OsPUB75) (EC 2.3.2.27) (Protein ERECT LEAF 1) (Protein TAIHU DWARF1) (RING-type E3 ubiquitin transferase PUB75) (Q10PI9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: E3 ubiquitin ligase that may function as positive regulator of brassinosteroid (BR) signaling. Possesses E3 ubiquitin ligase in vitro. Acts together with the heterotrimeric G alpha subunit GPA1 at the plasma membrane to mediate a BR signaling pathway that affects plant growth and development. Does not seem to be involved in gibberellin or cytokinin responses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23526892}; Peripheral membrane protein {ECO:0000305|PubMed:23526892}.
Interaction partners:
Sequence:
MPQYQELPCGGQVLDIDTALKDGILGGGPELGDAAAGDGGKQPVELRKMMDELDAAGDGGGDEAVPAVFICPISLEPMVDPVTLCTGQTYESANISRWLALGHRTCPTTMQELWDVTPIPNTTLRQLIAAWFSRRYTRFKKRSADFHGRAAELVHALRGTAVPKRQPLKGQARVAALRELRSLAAAHQSVTKAIAEAGGVGLLTSLLGPFTSHAVGSEAVAILVSGVPLDADAKAALMQPAKVSLLVDMLNEGAVDTKINCVRLIRILMEEKGFRPDTVASLSLLVGVMRLVRDKRHPDGVAAGLELLNSICAVHKPARSLIVSIGAVPQLVELLPELPTECVEPALDILDALAAVPEGRIALKDCPRTITNAVRLLMRVSEACTRRALSMLWVVCRMAPEECAPAALDAGLGAKLLLVIQSGCGPELKQQASELLKLCTMNCTSTVFISKCKLTKTIQ