wanglab/gogpt-training-data huggingface dataset:
Protein: ADAM10 endopeptidase (EC 3.4.24.81) (A8DZ03)
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:
MSSKCAFNIVFVSIIFIIIVNGYAKDISGVKRGHERLNEYISHYETLNYDHEHIRASHNRARRSVTKDQYVHLKFASHGRDFHLRLKRDLNTFSNKLDFYDSKGPIDVSTDHIYEGEVIGDRNSYVFGSIHNGVFEGKIITERDAYYVEHAKHYFPTNRTATTTPPSTSTTSSATTATKSTQPTRPLAKSNTSTTAVNSKTENFIKKIAESTTTSQQLPEYTESSSSSTTTFPPTTEYFEDEKERNAEDELDFHSIIYKESHVEDAYENVREGHVAGCGITDEVSQWMENIQNSAVEELPEPMSKDYQKLHRKQLHKKSAPQQQQQPHPPKKYISGDEDFKYPHQKYTKEANFAEGAFYDPSTGRRLGSSANVADWHQLVHERVRRATDNGAGDRGSSGGSGRGREDNKNTCSLYIQTDPLIWRHIREGIADHDRGRKYEVDEKTREEITSLIAHHVTAVNYIYRNTKFDGRTEHRNIRFEVQRIKIDDDSACRNSYNGPHNAFCNEHMDVSNFLNLHSLEDHSDFCLAYVFTYRDFTGGTLGLAWVASASGASGGICEKYKTYTETVGGQYQSTKRSLNTGIITFVNYNSRVPPKVSQLTLAHEIGHNFGSPHDYPQECRPGGLNGNYIMFASATSGDRPNNSKFSPCSIRNISNVLDVLVGNTKRDCFKASEGAFCGNKIVESGEECDCGFNEEECKDKCCYPRLISEYDQSLNSSAKGCTRRAKTQCSPSQGPCCLSNSCTFVPTSYHQKCKEETECSWSSTCNGTTAECPEPRHRDDKTMCNNGTALCIRGECSGSPCLLWNMTKCFLTSTTLPHVSKRKLCDLACQDGNDTSTCRSTSEFADKYNIQKGGISLQPGSPCDNFQGYCDVFLKCRAVDADGPLLRLKNLLLNRKTLQTVAEWIVDNWYLVVLMGVAFIVVMGSFIKCCAVHTPSSNPKKRRARRISETLRAPMNTLRRMQRHPNQRGAGPRSIPPPAHEAQHYSRGGDGRGGGGGGGGRHGGSRSHHQQHPHDWDRHQGGHSIVPLPTGGSHSSRNSAANQARRSDGRGPRSTSSGRPQAIASGSGAASGAARSHGGYGAEQAIPGSIGGGVQAAISSGGVVARAQLPLPLPPPNGQQQMQQQQQLQLQQPAISPQQQPQQAFYTPKGVCPISLQVER
Protein: Oep protein (Teratocarcinoma-derived growth factor 1) (A7MCB2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTSQLFGFLMFAVIICQAVSLESGCEGSECVKVGVSGKPKQYAEFLNKFNEMNTQTPQRQHRNAEAALPFVGLTGVAKQSRTCCKNGGTCILGSFCACPKYFTGRSCEYDERLRDCGVIPHGEWVQKGCSYCRCGYGLLHCFPHVFSKDCDDSQEVRWHRSGSLRTLSSTIVMFAPFILHRLL
Protein: Protein phosphatase 1 regulatory subunit 14 (Q14BX6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU369059}; Peripheral membrane protein {ECO:0000256|RuleBase:RU369059}.
Interaction partners:
Sequence:
MADSGPSGGPALTDPGPEPGSANTGPRVYFESPPGTPGETPGPGNNPDKDDQVRRPHRPDKIIVKYDRKELRKRLNLDDWILEQLTGLYDCKEEEIPELEIDVDELLDMESDDTRAARVKELLVDCYKPTEAFINDLLDRIRGMQKLTIPLKN
Protein: ATP-dependent RNA helicase SUV3, mitochondrial (EC 3.6.4.13) (Q59TB2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for intron-independent turnover and processing of mitochondrial RNA. It is a key control element in nuclear-mitochondrial interactions (By similarity). Required for embedded hyphal growth, for wild-type respiratory growth, and biofilm development. Required for chlamydospore formation, distinctive morphological feature of the fungal pathogen C.albicans that can be induced to form in oxygen-limited environments and has been reported in clinical specimens. Plays am important role in virulence.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Msu1p
- Negative regulator of sporulation MDS3
- Nuclear pore complex protein Nup85
- Ribosomal RNA-processing protein 44
- Virulence protein SSD1
- ATP-dependent RNA helicase MSS116, mitochondrial
- ribonuclease Z
- ATP-dependent RNA helicase MRH4, mitochondrial
Sequence:
MLLCQKPTYRLLRYSVKRYVASLYSLRGVSTRVNLIHRTYATTVAKDNIDHNDSSPVFNNNEVRFENINASIHPILLDLKNKLIKGKFDSPYTILNDQPSDVKTEIFQSFEQQLSKALSSKSTPENKITLVDYLNPTLDNISSLLHLISNNTYPNNFLEFSNLSSNNDLIMQLFTQLLHKIFLQYRIENASFEKPKVDFSNPAEWFPEARKMKRKIIMHVGPTNSGKTYNSLIKLSKSKTGYYAGPLRLLAREIYEKFNSQGIGCNLITGEEVVPSIDKYGKVSGIASGTIEMIPLHKKMDLCVIDEIQMIADPLRGSVWTNAVLGVLAHEIHLCGEESAVPFIQKMVEITGDELEIKKFNRLGKLTVEKSNTSLQQLKKGDCLVVFSKKKILKFKCDIERNTRLKVGVIYGALPPEIRSQEASKFNNGEYDVLVASDAIGMGLNLKINRIVFSGVNKFNGSTVEKLSVSQVKQIAGRAGRFSAQHGSKEGFVTALHRSSLVYIDQCLKTPVSEISKACIWPTSNIWRQYMANDPHKSSLSSVYENFLTNVLKFQSDNFFISELDQKVQLLNLVAKNRLLSTMIIDDQLTISETPINFRTSVNPKLLKNTVIKFYETIVKRDCKSILDFDFLDLELLSQNSFVGTDVMVPLQKVDKLEDMHRLVLLFLWLSQRFPTLFIDKDSAMEVKALVEKRINQELVNVERANSFFSDRSNGYEPRR
Protein: FI18308p1 (PDGF- and VEGF-receptor related, isoform I (EC 2.7.10.1)) (E1JHB6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAMLPRLILLPLLLILRISWSDAVPLQQFSPDPDDSIENCGGENGAPLMTPCKSAIILDAQTSTTLKCEDDEPMSWWTSQSQYVHVKSFDNTEDPARPFGTSLHLIEVTADYVAAYYCVKTSKFSQIAKEEQSDEAMIELVNQGYASSIYVYVNDPDTKLVDSHNVVTARQYTDVVIPCKPAMPDTEVLLETSNGEMHSSKSVGRYDPQRGFTIEIRSIVDGGDYYCRPNPPFPHNEEEMTSIEVRFIATGLDIPRTQTTNMVYTYAPGVTDGDDEVLTVTNQSTGNLALIRGGDGTLSRERARRSPARLAPMNASPSPRPGQDGKPLPKPVIRSSVEHHVFTDTNFTLDCEQSAYVESVYGMEWFTPSRDENRIFASQSRTDPKTRNSTHQTGRSTLTVLNAQPSDTGLYKCVTTDNSNQNVQRATYRIKVLKQNESYLNVGEPSGHYNVQEYANRTIQMTANFEGFPTPSFSWFKPDGTEVRQSENNFKILSTELSTMLQVLNAQLQDSGTYVLRGSNSFGVVQREYNVSVMDAPALKMSDAYVQVGSVARLECTVRSYPPAIVTFFFRPCSLEPQWPTCSVLNQNFSLPSEQEKYQFQTRPRPGKLSVERIYEVSFLPTEPGILTCIAQNIIDGKERRTLTKAHVLLGNISENMTIYGFDKDHKIAKEDNVNFTCEALAYHFDGNLKWFINGEDLKESDSVHIETSHTKYSYKSTVHITTISDRDRGTYECRAYHNDKDAVYSSREIDLYVHDPSAPQWTNGGQEGHSKIKRKLSQTLELECASTAVPVAIVRWFKDDKEVTESKLRHIIEKESKLLITHLYPGDEGVYKCVVENRLDRIERSFTVVISDLPGISMAWVWFGVILFLILIGLCVFLAVRYQKEHKRHLALKAAGLANFEEGAVGHINPDLTLDEQAELLPYNREFEFPRENLKLGKQLGAGAFGVVLKGEAKGIRREEPTTTVAVKMVKATADNEVVRALVSELKIMVHLGQHLNVVNLLGAVTKNIAKRELMVIVEYCRFGNIQNFLLRNRKCFINQINPDTDHIDPSIMTQRMSDNYELHRDTNGGGLKYANVGFPIHSYINEPHNNNTQPPTHRRNSDNDPRSGTRAGRTGSGTATYSYDRQMDTCATVMTTVPEDDQIMSNNSVQPAWRSNYKTDSTEAMTVTTVDLISWAFQVARGMDYLSSKKVLHGDLAARNILLCEDNVVKICDFGLARSMYRGDNYKKSENGKLPIKWLALESLSDHVFSTYSDVWSYGIVLWEMFSLAKVPYPGIDPNQELFNKLNDGYRMEKPKFANQELYEIMLECWRKNPESRPLFAELEKRFANMLGEDVASHYLDLNNPYMQSNIEYMKKQSTDYLALMGSPDELAPAAPRYVNGHIVPDIRARQSPTLSNNLNSGSSKPLRKKNGMPTVDVADQAPEEIPMLHRSSTGSDGSPEQGRRFNQALKQQYVTPTPSPRHHVETKLNGEPSENYVNMKPPRKNIPGKTTTGGGGAAAGASTEAFSNPSYQPLSTVNEKEQRRY
Protein: FI19428p1 (Salty dog, isoform B) (Q9V9U2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- FI02923p
- AT22075p
- IP16073p
Sequence:
MASSVSNLASTVATATTATLEDLHFSLTDYIVFSLMLSASAGIGVYFGFFSKAKNTTEEYLQGGKRMPTLPVAISLVSSQLSGVAMMSVPAETYSFGFNMIFVVWAMVLSVPVLIYIIVPVFYDNNVSNCYEYLELRFSKRTRQLVTITFILNQFLMLPVYMFVPSLAFSQVTGYNIHLINTVVSSICVFYTMLGGIKAVVWTDVVQGSVMLISVVLVAILGTSNTGGITNVLENAAEGGRFDFSFGIDPRLRLTFISGMASGLLMWTGKLGLDQSCVQRIVSLPSYGHAKRCLLMAGVGFLLIMSFTCFTGIIMFAYYYGCDPIQAGLVSKPDKLMPFFIQDIMGHMMGMPGVFISCVFSASLSSLSASLNSFAGVVYFDYIKPRINHSEAKANATMKLVIVVMGAYCIVGGFIVQNFNSIIQTMWTITGINMGAVVGVFCLGMFVPRCNAKVAVSGIAFSCLVMLWIIINGQMNFKAGLIKYDPLPNGLDQCEAKGFEVILNAIRNKNVTNVGTTAIPSLEAPKELTTAFDSNRDFSIYDTSFYWYKVLGALLVFAWAIPMSYVWPLDKEEKQNPKLYSPFVRSMLNKPSPVLELEELPLKTPLSEEQIKEKENGSATEA
Protein: NADH-cytochrome b5 reductase 2 (EC 1.6.2.2) (Mitochondrial cytochrome b reductase) (Q6FUX5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: May mediate the reduction of outer membrane cytochrome b5.
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- NADH-cytochrome b5 reductase
- NADH-cytochrome b5 reductase 1
- Candida glabrata strain CBS138 chromosome L complete sequence
- Dihydroorotate dehydrogenase
- EKC/KEOPS complex subunit CGI121
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MAFARFARPTQRFLPFAIGAVAVTAGALYLNGWNTIKNENPKVFIGDRKWIDLELEKIIEESHDTKRFFFKLPTDDSVSGLTLASAVLTKFMTPKGNPVIRPYTPVSDLSEKGYIEFVIKHYEGGKMTDHLFQLKPKDTLAFQGPIPKWQWKPNSFDTITLLGGGTGITPLYQLVHHITQNKEDKTKINLFYGSKTPSDILLKKELDDLQKKYPEQLNIQYFVDKDDTGKFDGNKGFITKDFLAKNAPGPKEKTQVFVCGPPPFMDSLSGQKKSPMEQGDLTGALKDLGYSQDQVFKF
Protein: Elicitor peptide 3 (Q8LAX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Elicitor of plant defense.
Interaction partners:
- Elicitor peptide 2
- Leucine-rich repeat receptor-like protein kinase PEPR1
- Leucine-rich repeat receptor-like protein kinase PEPR2
- Precursor of elicitor peptide 1
- Elicitor peptide 5
- Transmembrane protein
- Elicitor peptide 4
- Cytochrome P450, family 705, subfamily A, polypeptide 33
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Elicitor peptide 6
Sequence:
MENLRNGEDNGSLIPFTFFDQSSVTIPLLKCSGLESSSSSSSSCDLSSSHSEEDESIDIKEEEEEEEEDGMTIEIKARGKNKTKPTPSSGKGGKHN
Protein: Flagellar M-ring protein (P25798)
Organism: Escherichia coli (strain K12)
Function: The M ring may be actively involved in energy transduction.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}. Bacterial flagellum basal body {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Flagellar biosynthesis protein FlhA
- Flagellar hook protein FlgE
- Flagellar basal-body rod protein FlgC
- Flagellar protein FliO
- Flagellar P-ring protein
- Flagellar hook-length control protein
- Flagellar biosynthetic protein FliQ
- Flagellum-specific ATP synthase
- Flagellar assembly protein FliH
- Flagellar hook-basal body complex protein FliE
Sequence:
MNATAAQTKSLEWLNRLRANPKIPLIVAGSAAVAVMVALILWAKAPDYRTLFSNLSDQDGGAIVSQLTQMNIPYRFSEASGAIEVPADKVHELRLRLAQQGLPKGGAVGFELLDQEKFGISQFSEQVNYQRALEGELSRTIETIGPVKGARVHLAMPKPSLFVREQKSPSASVTVNLLPGRALDEGQISAIVHLVSSAVAGLPPGNVTLVDQGGHLLTQSNTSGRDLNDAQLKYASDVEGRIQRRIEAILSPIVGNGNIHAQVTAQLDFASKEQTEEQYRPNGDESHAALRSRQLNESEQSGSGYPGGVPGALSNQPAPANNAPISTPPANQNNRQQQASTTSNSGPRSTQRNETSNYEVDRTIRHTKMNVGDVQRLSVAVVVNYKTLPDGKPLPLSNEQMKQIEDLTREAMGFSEKRGDSLNVVNSPFNSSDESGGELPFWQQQAFIDQLLAAGRWLLVLLVAWLLWRKAVRPQLTRRAEAMKAVQQQAQAREEVEDAVEVRLSKDEQLQQRRANQRLGAEVMSQRIREMSDNDPRVVALVIRQWINNDHE
Protein: Glycine betaine-binding protein YehZ (P33362)
Organism: Escherichia coli (strain K12)
Function: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Binds glycine betaine with low affinity.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Glycine betaine uptake system ATP-binding protein YehX
- Glycine betaine uptake system permease protein YehY
- Glycine betaine uptake system permease protein YehW
- Glycine betaine/proline betaine transport system permease protein ProW
- Glycine betaine/proline betaine transport system ATP-binding protein ProV
- Glycine betaine/proline betaine-binding periplasmic protein
Sequence:
MPLLKLWAGSLVMLAAVSLPLQAASPVKVGSKIDTEGALLGNIILQVLESHGVPTVNKVQLGTTPVVRGAITSGELDIYPEYTGNGAFFFKDENDAAWKNAQQGYEKVKKLDSEHNKLIWLTPAPANNTWTIAVRQDVAEKNKLTSLADLSRYLQEGGTFKLAASAEFIERADALPAFEKAYGFKLGQDQLLSLAGGDTAVTIKAAAQQTSGVNAAMAYGTDGPVAALGLQTLSDPQGVQPIYAPAPVVRESVLREYPQMAQWLQPVFASLDAKTLQQLNASIAVEGLDAKKVAADYLKQKGWTK
Protein: ATP sulfurylase 4, chloroplastic (EC 2.7.7.4) (Q9S7D8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfate adenylyltransferase. Catalyzes the first step of the sulfate assimilation pathway.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:10806350}.
Interaction partners:
- Adenylyl-sulfate kinase 1, chloroplastic
- Adenylyl-sulfate kinase 2, chloroplastic
- Adenylyl-sulfate kinase 3
- Adenylyl-sulfate kinase 4, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- Bifunctional adenosine 5'-phosphosulfate phosphorylase/adenylylsulfatase HINT4
- FAD synthase
- Sulfate transporter 2.1
Sequence:
MASSAAAIVSGSPFRSSPLIHNHHASRYAPGSISVVSLPRQVSRRGLSVKSGLIEPDGGKLMNLVVEESRRRVMKHEAETVPARIKLNRVDLEWVHVLSEGWASPLKGFMRQSEFLQTLHFNSFRLEDGSVVNMSVPIVLAIDDDQKFRIGDSNQVTLVDSVGNPIAILNDIEIYKHPKEERIARTWGTTARGLPYAEEAITKAGNWLIGGDLQVLEPIKYNDGLDRFRLSPSQLREEFIRRGADAVFAFQLRNPVHNGHALLMTDTRRRLLEMGYKNPVLLLNPLGGFTKADDVPLSWRMRQHEKVLEDGVLDPETTVVSIFPSPMLYAGPTEVQWHAKARINAGANFYIVGRDPAGMGHPTEKRDLYDADHGKKVLSMAPGLERLNILPFKVAAYDKTQGKMAFFDPSRSQDFLFISGTKMRGLAKKKENPPDGFMCPSGWKVLVDYYDSLSAETGNGRVSEAVASA
Protein: Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein) (Q9BTE3)
Organism: Homo sapiens (Human)
Function: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion.
Subcellular location: Nucleus {ECO:0000269|PubMed:17296731}. Note=Associates with chromatin. Highly associated with chromatin in G1/S and S phases, reduced binding to chromatin in G2, and further decreased binding in early M phase. It then reassociates with chromatin in late M phase. Dissociates from chromatin later than component of the MCM complex.
Interaction partners:
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM2
- DNA helicase MCM8
- Protein MCM10 homolog
- DNA helicase MCM9
- DNA replication factor Cdt1
Sequence:
MPCGEDWLSHPLGIVQGFFAQNGVNPDWEKKVIEYFKEKLKENNAPKWVPSLNEVPLHYLKPNSFVKFRCMIQDMFDPEFYMGVYETVNQNTKAHVLHFGKYRDVAECGPQQELDLNSPRNTTLERQTFYCVPVPGESTWVKEAYVNANQARVSPSTSYTPSRHKRSYEDDDDMDLQPNKQKDQHAGARQAGSVGGLQWCGEPKRLETEASTGQQLNSLNLSSPFDLNFPLPGEKGPACLVKVYEDWDCFKVNDILELYGILSVDPVLSILNNDERDASALLDPMECTDTAEEQRVHSPPASLVPRIHVILAQKLQHINPLLPACLNKEESKTCKFVSSFMSELSPVRAELLGFLTHALLGDSLAAEYLILHLISTVYTRRDVLPLGKFTVNLSGCPRNSTFTEHLYRIIQHLVPASFRLQMTIENMNHLKFIPHKDYTANRLVSGLLQLPSNTSLVIDETLLEQGQLDTPGVHNVTALSNLITWQKVDYDFSYHQMEFPCNINVFITSEGRSLLPADCQIHLQPQLIPPNMEEYMNSLLSAVLPSVLNKFRIYLTLLRFLEYSISDEITKAVEDDFVEMRKNDPQSITADDLHQLLVVARCLSLSAGQTTLSRERWLRAKQLESLRRTRLQQQKCVNGNEL
Protein: Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) (P04272)
Organism: Bos taurus (Bovine)
Function: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane.
Interaction partners:
- Protein S100-A10
- Tissue-type plasminogen activator
- Protein S100-A4
- AHNAK nucleoprotein
- Plasminogen
- AHNAK nucleoprotein 2.
- Protein S100
- Annexin A1
- Cathepsin B
- CD63 antigen
Sequence:
MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIVSDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKKKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
Protein: Seven in absentia homolog 3 (Siah-3) (Q8IW03)
Organism: Homo sapiens (Human)
Function: Negative regulator of PRKN translocation to damaged mitochondria. Acts probably by destabilizing PINK1 protein, hence inhibiting PRKN targeting to dysfunctional depolarized mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24270810}.
Interaction partners:
Sequence:
MLFFTQCFGAVLDLIHLRFQHYKAKRVFSAAGQLVCVVNPTHNLKYVSSRRAVTQSAPEQGSFHPHHLSHHHCHHRHHHHLRHHAHPHHLHHQEAGLHANPVTPCLCMCPLFSCQWEGRLEVVVPHLRQIHRVDILQGAEIVFLATDMHLPAPADWIIMHSCLGHHFLLVLRKQERHEGHPQFFATMMLIGTPTQADCFTYRLELNRNHRRLKWEATPRSVLECVDSVITDGDCLVLNTSLAQLFSDNGSLAIGIAITATEVLPSEAEM
Protein: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1 (EC 3.1.3.67) (O94526)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a phosphoinositide 3-phosphatase and regulates PtdIns(3,4,5)P3 levels.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:15249580}.
Interaction partners:
- Phosphatidylinositol 4-phosphate 5-kinase its3
- Phosphatidylinositol 3-kinase pik3
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Uncharacterized protein C3C7.01c
- Uncharacterized protein C19F5.03
- Inositol-1,4,5-trisphosphate 5-phosphatase 2
- Inositol-1,4,5-trisphosphate 5-phosphatase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase lsb6
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
Sequence:
MNILRSVVSRGRKGLKQEKVNRSFAYLDMVYITSKVIAMSTPAAGIHKLYRNDELDVFKYLTTQLKDNWILLNLCAEETVYHLELFKPNVINYGFQDHNPPPLLFLWAIVMNMDALFQTQPLLTLVVHCKAGKGRTGTVICSYLVAFGGLTAKQSLELYTEKRMVRGHGLTISSQIRYVYYIEILKQFPNYLKAVEFNTGTTFFKSFKCLNIKKNSSLILSLHAFSKGRNINPVALWKSSDISSHNVSIKEGKRIWGIQCNLETSEKDLLLRVERKGQFYFPSSVQCWFHTHFQPMLVEYTNGINFQQGINSFLQGQQSISFSWSEMDNSRRSDPFFEQLTIVYENVF
Protein: Son of sevenless homolog 1 (SOS-1) (mSOS-1) (Q62245)
Organism: Mus musculus (Mouse)
Function: Promotes the exchange of Ras-bound GDP by GTP. Probably by promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3 in response to EGF (By similarity). Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity.
Interaction partners:
- GTPase HRas
- Tyrosine-protein phosphatase non-receptor type 11
- Growth factor receptor-bound protein 2
- GTPase KRas
- Epidermal growth factor receptor
- SHC-transforming protein 1
- Abl interactor 1
- Epidermal growth factor receptor kinase substrate 8
- GRB2-associated-binding protein 1
- Focal adhesion kinase 1
Sequence:
MQAQQLPYEFFSEENAPKWRGLLVPALKKVQGQVHPTLESNDDALQYVEELILQLLNMLCQAQPRSASDVEERVQKSFPHPIDKWAIADAQSAIEKRKRRNPLSLPAERIHHLLREVLGYKIDHQVSVYIVAVLEYISADILKLVGNYVRNIRHYEITKQDIKVAMCADKVLMDMFHQDVEDINILSLTDEEPSTSGEQTYYDLVKAFMAEIRQYIRELNLIIKVFREPFVSNSKLFSSNDVENIFSRIVDIHELSVKLLGHIEDTVEMTDEGSPHPLVGSCFEDLAEELAFDPYESYARDILRPGFHGHFLSQLSKPGAALYLQSIGEGFKEAVQYVLPRLLLAPVYHCLHYFELLKQLEEKSEDQEDKECMKQAITALLNVQSGMEKICSKSLAKRRLSESACRFYSQQMKGKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASSAEYRLKEKFFMRKVQINDKDDTSEYKHAFEIILKDGNSVIFSAKSAEEKNNWMAALISLQYRSTLERMLDVTVLQEEKEEQMRLPSAEVYRFAEPDSEENILFEENVQPKAGIPIIKAGTVLKLIERLTYHMYADPNFVRTFLTTYRSFCRPQELLSLLIERFEIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLNVCRHWVEHHFYDFERDADLLQRMEEFIGTVRGKAMKKWVESITKIIQRKKIARDNGPGHNITFQSSPPTVEWHISRPGHIETFDLLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNILKTEEGNPEVLRRHGKELINFSKRRRVAEITGEIQQYQNQPYCLRVEPDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIEPRHPKPLPRFPKKYSYPLKSPGVRPSNPRPGTMRHPTPLQQEPRKISYSRIPESETESTASAPNSPRTPLTPPPASGTSSNTDVCSVFDSDHSASPFHSRSASVSSISLSKGTDEVPVPPPVPPRRRPESAPAESSPSKIMSKHLDSPPAIPPRQPTSKAYSPRYSISDRTSISDPPESPPLLPPREPVRTPDVFSSSPLHLQPPPLGKKSDHGNAFFPNSPSPFTPPPPQTPSPHGTRRHLPSPPLTQEMDLHSIAGPPVPPRQSTSQLIPKLPPKTYKREHTHPSMHRDGPPLLENAHSS
Protein: BARP protein (Q38CV6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFNNLWLLLTVLCTAGIRAHGDWRDCYAARKPPPAGHVRVVCNLAEQLRGLPDTVSSALVNAAAASSKAFEAKVQAEEAVELAESRGLNVTKAKEAAVRATLAAEAAATAASNVEINAANVTSSRLARRNPNTGFEKIAMCENLDEDVREAAVKCTKKAENVTTQSLNEALHRLENLYTNMSALESLRVEHVEIERFFEMLEEHVEEAVSAQRQAEDAAAEAIKIAAADEKVRGYKKEEINQTAGPNTGPVVNSVASPEGSVLLLMAGLFLGSVL
Protein: Phenylalanine ammonia-lyase (PAL) (EC 4.3.1.24) (P26600)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: This is a key enzyme of plant metabolism catalyzing the first reaction in the biosynthesis from L-phenylalanine of a wide variety of natural products based on the phenylpropane skeleton.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
- trans-cinnamate 4-monooxygenase
- RING-type domain-containing protein
- histidinol-phosphate transaminase
- Tyrosine decarboxylase
- Tyrosine decarboxylase
- Tryptophan decarboxylase
- Tryptophan decarboxylase
- Aminotransferase class I/classII large domain-containing protein
- Aminotransferase class I/classII large domain-containing protein
Sequence:
MASSIVQNGHVNGEAMDLCKKSINVNDPLNWEMAAESLRGSHLDEVKKMVDEFRKPIVKLGGETLTVAQVASIANVDNKSNGVKVELSESARAGVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKNGGALQKELIRFLNAGVFGNGTESSHTLPHSATRAAMLVRINTLLQGYSGIRFEILEAITKLINSNITPCLPLRGTITASGDLVPLSYIAGLLTGRPNSKAVGPNGEKLNAEERFRVAGVTSGFFELQPKEGLALVNGTAVGSGMASMVLFESNILAVMSEVLSAIFAEVMNGKPEFTDYLTHKLKHHPGQIEAAAIMEHILDGSSYVKAAQKLHEMDPLQKPKQDRYALRTSPQWLGPQIEVIRAATKMIEREINSVNDNPLIDVSRNKALHGGNFQGTPIGVSMDNTRLALASIGKLMFAQFSELVNDYYNNGLPLNLTAGRNPSLDYGLKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISARKTAEAVDILKLMSSTYLVALCQAIDLRHLEENLKNAVKNTVSQVAKKTLAMGANGELHPARFCEKELLQVVEREYLFTYADDPCSSTYPLMQKLRQVLVDHAMKNGESEKNLNSSIFQKIVAFEDELKAVLPKEVESARAVVESGNPAIPNRITECRSYPLYRLVRQEVGTELLTGEKVRSPGEEIDKVFTAFCNGQIIDPLLECLKSWNGAPIPIC
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258 (Oligosaccharyl transferase subunit TMEM258) (Transmembrane protein 258) (P61166)
Organism: Mus musculus (Mouse)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Involved in ER homeostasis in the colonic epithelium.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P61165}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P61165}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P61165}. Cytoplasm {ECO:0000250|UniProtKB:P61165}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Oligosaccharyltransferase complex subunit OSTC
Sequence:
MELEAMSRYTSPVNPAVFPHLTVVLLAIGMFFTAWFFVYEVTSTKYTRDIYKELLISLVASLFMGFGVLFLLLWVGIYV
Protein: RhoA (F1CG58)
Organism: Meleagris gallopavo (Wild turkey)
Interaction partners:
Sequence:
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGRKKSGCLLL
Protein: Lsm8p (Q6QA14)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLSQYLRRRVSVVTVDGRYLVGVLHAADQLMNLVLTSCAERVFDDEAEDSTDPNDIKNNRNGTNGATPPGGEMREHSLGVLMIRGSDVVCVASVNTVEEAKLSRKLWRGRNLPVVERVARSATASVKGG