wanglab/gogpt-training-data huggingface dataset:
Protein: Stimulator of interferon response cGAMP interactor 1 (A0A494C0T1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000256|ARBA:ARBA00004542}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004542}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00004457}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004457}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}.
Interaction partners:
Sequence:
MLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRNLQMTAASRCPRRFSGTCGRRKRKRLLWAA
Protein: Vacuolar protein sorting-associated protein 72 homolog (Protein YL-1) (Q9VKM6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, this complex acetylates phosphorylated H2AV in nucleosomes and exchanges it with unmodified H2AV.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- YEATS domain-containing protein 4
- DNA methyltransferase 1-associated protein 1
- RuvB-like helicase 2
- RuvB-like helicase 1
- Histone H2A.v
- Brahma associated protein 55kD
- NuA4 complex subunit EAF3 homolog
- MRG/MORF4L binding protein
- Transcription-associated protein 1
- Actin-related protein 6
Sequence:
MAASRSRRNNAGNKIAHLLNEEEEDDFYKTSYGGFQEDEEDKEYEQKDEEEDVVDSDFSIDENDEPVSDQEEAPEKKRKRGVVNTKAYKETKPAVKKETKATPALHKKRPGGGVTKRRPRPRFTVLDSGRKSIRTSTAIKTQATKIRLKELDDARKRKKKKVRVEDYMPTQEELLEEAKITEEENTKSLEKFQKMELEKKKSRPTKRTFSGPTIRYHSLTMPAMRKPTRGANPAVDSKDLAGKCERTFVTIENDFNDKVFQSLFRHKAPPKASNGICPITRLPARYFDPITQQPYYSIQAFKILREAYYMQLEQQGGGSEQPELAKWLEWRKLVKENRLKASAAASKNGDN
Protein: Testis-expressed protein 101 (Cell surface receptor NYD-SP8) (Scleroderma-associated autoantigen) (Spermatogenesis-related gene protein) (Q9BY14)
Organism: Homo sapiens (Human)
Function: Plays a role in fertilization by controlling binding of sperm to zona pellucida and migration of spermatozoa into the oviduct (By similarity). May play a role in signal transduction and promote protein tyrosine phosphorylation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9JMI7}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9JMI7}. Membrane raft {ECO:0000250|UniProtKB:Q9JMI7}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9JMI7}. Secreted {ECO:0000250|UniProtKB:Q9JMI7}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9JMI7}. Note=Located on plasma membrane of spermatocytes, round and elongated spermatids, and testicular spermatozoa. {ECO:0000250|UniProtKB:Q9JMI7}.
Interaction partners:
- Dipeptidase 3
- Lymphocyte antigen 6K
- Urokinase plasminogen activator surface receptor
- Sperm acrosome membrane-associated protein 4
Sequence:
MGTPRIQHLLILLVLGASLLTSGLELYCQKGLSMTVEADPANMFNWTTEEVETCDKGALCQETILIIKAGTETAILATKGCIPEGEEAITIVQHSSPPGLIVTSYSNYCEDSFCNDKDSLSQFWEFSETTASTVSTTLHCPTCVALGTCFSAPSLPCPNGTTRCYQGKLEITGGGIESSVEVKGCTAMIGCRLMSGILAVGPMFVREACPHQLLTQPRKTENGATCLPIPVWGLQLLLPLLLPSFIHFS
Protein: Synaptotagmin-17 (Protein B/K) (Synaptotagmin XVII) (SytXVII) (Q9BSW7)
Organism: Homo sapiens (Human)
Function: Plays a role in dendrite formation by melanocytes.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- C-type lectin domain family 19 member A
- Charged multivesicular body protein 4a
Sequence:
MAYIQLEPLNEGFLSRISGLLLCRWTCRHCCQKCYESSCCQSSEDEVEILGPFPAQTPPWLMASRSSDKDGDSVHTASEVPLTPRTNSPDGRRSSSDTSKSTYSLTRRISSLESRRPSSPLIDIKPIEFGVLSAKKEPIQPSVLRRTYNPDDYFRKFEPHLYSLDSNSDDVDSLTDEEILSKYQLGMLHFSTQYDLLHNHLTVRVIEARDLPPPISHDGSRQDMAHSNPYVKICLLPDQKNSKQTGVKRKTQKPVFEERYTFEIPFLEAQRRTLLLTVVDFDKFSRHCVIGKVSVPLCEVDLVKGGHWWKALIPSSQNEVELGELLLSLNYLPSAGRLNVDVIRAKQLLQTDVSQGSDPFVKIQLVHGLKLVKTKKTSFLRGTIDPFYNESFSFKVPQEELENASLVFTVFGHNMKSSNDFIGRIVIGQYSSGPSETNHWRRMLNTHRTAVEQWHSLRSRAECDRVSPASLEVT
Protein: Deubiquitinase DESI2 (EC 3.4.19.12) (Desumoylating isopeptidase 2) (DeSI-2) (PPPDE peptidase domain-containing protein 1) (Palmitoyl protein thioesterase DESI2) (EC 3.1.2.22) (Protein FAM152A) (S-depalmitoylase DESI2) (Q9BSY9)
Organism: Homo sapiens (Human)
Function: Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Deubiquitinates 'Lys-48'-linked polyubiquitination of RPS7 leading to its stabilization.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9D291}.
Interaction partners:
- SUMO-specific isopeptidase USPL1
Sequence:
MGANQLVVLNVYDMYWMNEYTSSIGIGVFHSGIEVYGREFAYGGHPYPFSGIFEISPGNASELGETFKFKEAVVLGSTDFLEDDIEKIVEELGKEYKGNAYHLMHKNCNHFSSALSEILCGKEIPRWINRLAYFSSCIPFLQSCLPKEWLTPAALQSSVSQELQDELEEAEDAAASASVASTAAGSRPGRHTKL
Protein: Protein COS6 (P53344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YEL073C
- Uncharacterized protein YGL258W-A
Sequence:
MKENELKNEKSVDVLSVKQLESQKTVLPQDLFRSSFTWFCYEIYKSLVFRIWMLLWLPLSVWWKLSNNWIYPLMVSLLVLFWGPVFVLVIFRLSRKRSLSKQLTQFCKEITKNTPSSDPHDWEVVAANLNSYFYENKAWNTKYFFFSAMSCQEAFRTTLLEPFSLKKDEAAKVKSFKDSVPYIEEALEVYFTEVEKQWKLFNSEKSWSPVGLEDAKLPKEAYRFKLTWVLKRIFNRRCLPLFLFYLHNVFISRNDGTIARPLFLVVLFFIMTRDFRNMRMIVLSVKMEHKMQFLSTIINEQESGANGWDEIAKKMNRYLFEKKVWKNEEFFFDGIDCEWFFSHFFYRVLSAKKSMRALSLNVELWPYIKEAQLSCSEESLA
Protein: 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) (Acetyl-CoA acetyltransferase) (EC 2.3.1.9) (Acetyl-CoA acyltransferase) (Acyl-CoA hydrolase, mitochondrial) (EC 3.1.2.-, EC 3.1.2.1, EC 3.1.2.2) (Beta-ketothiolase) (Mitochondrial 3-oxoacyl-CoA thiolase) (T1) (P42765)
Organism: Homo sapiens (Human)
Function: In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms (Probable). Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies (Probable). Also displays hydrolase activity on various fatty acyl-CoAs. Thereby, could be responsible for the production of acetate in a side reaction to beta-oxidation (Probable). Abolishes BNIP3-mediated apoptosis and mitochondrial damage.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18371312}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Enoyl-CoA delta isomerase 2
- Peroxisomal acyl-coenzyme A oxidase 3
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-hydroxyacyl-CoA dehydrogenase type-2
Sequence:
MALLRGVFVVAAKRTPFGAYGGLLKDFTATDLSEFAAKAALSAGKVSPETVDSVIMGNVLQSSSDAIYLARHVGLRVGIPKETPALTINRLCGSGFQSIVNGCQEICVKEAEVVLCGGTESMSQAPYCVRNVRFGTKLGSDIKLEDSLWVSLTDQHVQLPMAMTAENLAVKHKISREECDKYALQSQQRWKAANDAGYFNDEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPPVFKKDGTVTAGNASGVADGAGAVIIASEDAVKKHNFTPLARIVGYFVSGCDPSIMGIGPVPAISGALKKAGLSLKDMDLVEVNEAFAPQYLAVERSLDLDISKTNVNGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIAVIIQSTA
Protein: Branched-chain amino acid transport system 2 carrier protein (LIV-II) (P19072)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Component of the LIV-II transport system for branched-chain amino acids. BraB is specific for isoleucine, leucine and valine. The LIV-II transport system is coupled to sodium and lithium ions.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Leucine-, isoleucine-, valine-, threonine-, and alanine-binding protein
Sequence:
MTHLKGFDLLALGFMTFALFLGAGNIIFPPSAGMAAGEHVWSAAFGFLLTGVGLPLLTVVALARVGGGIGRLTQPIGRRAGVAFAIAVYLAIGPLFATPRTAVVSFEMGVAPFTGDGGVPLLIYTVAYFSVVLFLVLNPGRLVDRVGKVITPVLLSALLVLGGAAIFAPAGEIGSSSGEYQSAPLVQGFLQGYLTMDTLGALVFGIVIATAIRDRGISDSRLVTRYSMIAGVIAATGLSLVYLALFYLGATSQGIAGDAQNGVQILTAYVQQTFGVSGSLLLAVVITLACLTTAVGLITACGEFFSDLLPVSYKTVVIVFSLFSLLVANQGLTQLISLSVPVLVGLYPLAIVLIALSLFDRLWVSAPRVFVPVMIVALLFGIVDGLGAAKLNGWVPDVFAKLPLADQSLGWLLPVSIALVLAVVCDRLLGKPREAVA
Protein: Diacylglycerol kinase (DAG kinase) (EC 2.7.1.107) (E9PNL8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIPRYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTTSKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRVSMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKLSPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLPTSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAVSTGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Protein: Amelogenin (Amelogenin 173A/173B) (Leucine-rich amelogenin peptide) (LRAP) (P45561)
Organism: Sus scrofa (Pig)
Function: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Ameloblastin
- Enamelin
- Kallikrein-4
- Matrix metalloproteinase-20
- Amelotin.
- Tuftelin
- Peripherin 2.
- Neuropeptide Y receptor type 2
- Somatotropin
- Peptidase S1 domain-containing protein
Sequence:
MGTWILFACLLGAAFSMPLPPHPGHPGYINFSYEVLTPLKWYQNMIRHPYTSYGYEPMGGWLHHQIIPVVSQQTPQSHALQPHHHIPMVPAQQPGIPQQPMMPLPGQHSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPLQPQSPMHPIQPLLPQPPLPPMFSMQSLLPDLPLEAWPATDKTKREEVD
Protein: Sphingomyelin phosphodiesterase 4 (EC 3.1.4.12) (Neutral sphingomyelinase 3) (nSMase-3) (nSMase3) (Neutral sphingomyelinase III) (Q9NXE4)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide. It has a relevant role in the homeostasis of membrane sphingolipids, thereby influencing membrane integrity, and endoplasmic reticulum organization and function. May sensitize cells to DNA damage-induced apoptosis. In skeletal muscle, mediates TNF-stimulated oxidant production (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16517606, ECO:0000269|PubMed:18505924, ECO:0000269|PubMed:31495489}; Single-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16517606}; Single-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:31495489}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q6ZPR5}.
Interaction partners:
- Sphingomyelin phosphodiesterase 3
- Sphingomyelin phosphodiesterase 2
- Sphingomyelin phosphodiesterase
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Phosphatidylcholine:ceramide cholinephosphotransferase 2
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
- Sphingolipid delta
- Ceramide synthase 6
- Ceramide synthase 2
- Sphingolipid delta
Sequence:
MTTFGAVAEWRLPSLRRATLWIPQWFAKKAIFNSPLEAAMAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPAKELHTIFPWLVESIFGSLDGVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKASIQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTSDCAYFILVDRYLSWFLPTEGSVPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRHISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLSVSSALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSPLEEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSDSQPRCVSEKWAPFVQENLLMYTKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAEMIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAVTDASFKVKSHVYSLEGQDCKYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYTANDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCIVGEDGLILTPLGRYQIINGLRRFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFAGQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVAGHTRGPRLSLRFLGSYRTLVSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
Protein: Probable receptor-like protein kinase At5g61350 (EC 2.7.11.-) (Q9FLJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Probable serine/threonine protein kinase IRE3
- Cyclase-associated protein 1
- GPI-anchored protein LLG3
- GPI-anchored protein LLG2
- At3g52790
- Jacalin-related lectin 19
Sequence:
MGGDFRHFSSHVSLLLLFLLIVKSSSSFTPADNYLIDCGSSDETKLSDGRNFKSDQQSVAFLQTDEDIKTSVDSIPITDSNASTLPLYLTARIFAGKSTYSFYISRPGRHWIRLHFYPLNHPLYNLTNSVFSVTTDTTVLLHDFSAGDTSSIVFKEYLIYAAEKLSLYFKPHKGSTAFINAVEIVSVPDELVPDSASSVPQAPDFKGLSSFSLEILHRINIGGDLISPKIDPLSRTWLSDKPYNTFPEGSRNVTVDPSTITYPDGGATALIAPNPVYATAEEMADAQTSQPNFNLSWRMSVDFGHDYFIRLHFCDIVSKSLNDLIFNVFINKLSAISALDLSSLTSALGTAYYADFVLNASTITNGSILVQVGPTPNLQSGKPNAILNGLEIMKLNNAAGSLDGLFGVDGKYKGPIGGMSSKKLAIAGIGFVMALTAFLGVVVLLVRWQRRPKDWQKQNSFSSWLLPLHASHSSYISSKGGSTSRRMSIFGSKKSKSNGFSSFFSNQGLGRYFPFTELQTATQNFDENAVCGVGGFGKVYIGEIDGGTQVAIKRGSQSSEQGINEFQTEIQMLSKLRHRHLVSLIGFCDENKEMILVYEYMSNGPLRDHLYGSKENDPNPIPTLSWKQRLEICIGSARGLHYLHTGAAQGIIHRDVKTTNILLDENLVAKVSDFGLSKDAPMDEGHVSTAVKGSFGYLDPEYFRRQQLTDKSDVYSFGVVLFEVLCARPVINPQLPREQVNLAEYAMNLHRKGMLEKIIDPKIVGTISKGSLRKFVEAAEKCLAEYGVDRPGMGDVLWNLEYALQLQEASAQVDLSEDKTTMNIEMDLIPGEEMQSPSHSIP
Protein: Slx-like 1 (Q9D515)
Organism: Mus musculus (Mouse)
Interaction partners:
- Predicted gene, 20852
- Predicted gene, 20806
- 
- Spermiogenesis specific transcript on the Y 2
- Y-linked testis-specific protein 1
- Predicted gene 16405
- Serine-rich secreted Y-linked protein
Sequence:
MALKKLWAIPKDGYLLLLDYDDEDDDINFLEDAHSEENVSFSEEWQRFASSVETPIENRNLLSGEQQDGNASKLDLMEEQNPVTHDDENEIPEEIVGDTREMINNKSCEQYKTTFQKFDMDVQNFNEQQEKSVGLMNLETNNSDMLFDVDGELRK
Protein: Tripartite motif-containing protein 72 (EC 2.3.2.27) (Mitsugumin-53) (Mg53) (Q1XH17)
Organism: Mus musculus (Mouse)
Function: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:19029292, ECO:0000269|PubMed:19043407}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19029292, ECO:0000269|PubMed:19043407}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
Interaction partners:
- Caveolin-3
- Dysferlin
- Annexin A1
- Caveolae-associated protein 1
- Ubiquitin-conjugating enzyme E2 H
- T-cell receptor-associated transmembrane adapter 1
Sequence:
MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA
Protein: Protein E6 (P21735)
Organism: Human papillomavirus 45
Function: This protein has transforming activity in vitro.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MARFDDPKQRPYKLPDLCTELNTSLQDVSIACVYCKATLERTEVYQFAFKDLCIVYRDCIAYAACHKCIDFYSRIRELRYYSNSVYGETLEKITNTELYNLLIRCLRCQKPLNPAEKRRHLKDKRRFHSIAGQYRGQCNTCCDQARQERLRRRRETQV
Protein: ETO1-like protein 1 (Ethylene overproducer 1-like protein 1) (Q9ZQX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possible regulator of the ethylene pathway, which acts by regulating the stability of 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes. May act as a substrate-specific adapter that connects ACS enzymes, such as ACS5, to ubiquitin ligase complexes, leading to proteasomal degradation of ACS enzymes (By similarity).
Interaction partners:
- 1-aminocyclopropane-1-carboxylate synthase 5
- E3 ubiquitin-protein ligase XBAT32
- Catalytics
- 1-aminocyclopropane-1-carboxylate synthase 9
- 1-aminocyclopropane-1-carboxylate synthase 7
- 1-aminocyclopropane-1-carboxylate synthase 6
- Chromo domain-containing protein LHP1
- Cullin-3A
- At1g56440
- Cullin-3B
Sequence:
MRTFYPSDSCKESQLDSLNPQSWLQVERGKLSSSASSSAPLCRESFIKVPEPQILPHYKPLDYVEVLAQIHEELDTCPLQERSILYLLQYQVFRGLGETKLRRRSLQSAWQEATTVHEKVVFGSWLRYEKQGEEVITDLLSSCGKYSEEFVPLDIASYFPATTASSPEAASVKTNRSVSKNVVFKIGEEKIACQRRKIASLSAPFHAMLYGNFTESLLDEIDMSENHVSSSAMRVVRDFSVVGVLIGVSKNLLLEVLVFANKFCCERLKDACDRELASLISSMECAIELMDFALEENSPILASSCLQVFLYEMPDSLNDERVVEVLTRVNRSQVSTMAGKAPFSLYSCLSEVSMCIDPRSDRTLGFLEKLVDFAENDRQQVLGFHRLGCMRLLRKEYREAEEAFETAFNLGHVYSATGLARLGYIQGHRLWAYEKLSSVISSVSPPLGWMYQERSFYCEGDKKLEDLEKATELDPTLTYPYMYRAVTRMSKQNAKAALEEINRILGFKLALECLEIRFCLYLGMDDYEAALRDIQAALTLCPDYRMFDGKVAGRQLQTLVYEHVENWTTADCWMQLYEKWSNVDDIGSLSVIYQMLESDACKGVLYFRQSLLLLRLNCPEAAMRSLQLAREHASSDHERLVYEGWILYDTGHCEEGLQKAKESIGIKRSFEAYFLQAYALAESSLDPSSSSTVVSLLEDALKCPSDRLRKGQALNNLGSVYVDCEKLDLAADCYINALKVRHTRAHQGLARVHFLRNDKAAAYEEMTRLIEKAQNNASAYEKRSEYCDRELAKSDLEMVTRLDPLRVYPYRYRAAVLMDSRKEREAITELSRAIAFKADLHLLHLRAAFHEHIGDVTSALRDCRAALSVDPNHQEMLELHSRVNSHEP
Protein: Flotillin (Q9BTI6)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004543}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004543}. Membrane {ECO:0000256|RuleBase:RU366054}. Endosome {ECO:0000256|RuleBase:RU366054}.
Interaction partners:
Sequence:
MGNCHTVGPNEALVVSGGCCGSDYKQYVFGGWAWAWWCISDTQRISLEIMTLQPRCEDVETAEGVALTVTGVAQVKIMTEKELLAVACEQFLGKNVQDIKNVVLQTLEGHLRSILGTLTVEQIYQDRDQFAKLVREVAAPDVGRMGIEILSFTIKDVYDKVDYLSSLGKTQTAVVQRDADIGVAEAERDAGIREAECKKEMLDVKFMADTKIADSKRAFELQKSAFSEEVNIKTAEAQLAYELQGAREQQKIRQEEIEIEVVQRKKQIAVEAQEILRTDKELIATVRRPAEAEAHRIQQIAEGEKVKQVLLAQAEAEKIRKIGEAEATVIEAMGKAEAERMKLKAEAYQKYGDAAKMALVLEALPQIAAKIAAPLPVPSGKIKNS
Protein: Uroplakin-1b (UP1b) (Uroplakin Ib) (UPIb) (P38573)
Organism: Bos taurus (Bovine)
Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uroplakin-2
- Uroplakin-3b
- Uroplakin-1a
- Uroplakin-3a
- Cilia- and flagella-associated protein 91
Sequence:
MAKDDSTVRCFQGLLIFGNVIIGMCSIALMAECIFFVSDQNSLYPLLEATNNDDIYAAAWIGMFVGICLFCLSVLGIVGIMKSNRKILLVYFILMFIVYAFEVASCITAATQRDFFTPNLFLKQMLERYQNNSPPNNDDQWKNNGVTKTWDRLMLQDNCCGVNGPSDWQKYTSAFRTENSDADYPWPRQCCVMNSLKEPLNLDACKLGVPGYYHSQGCYELISGPMNRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIDY
Protein: t-SNARE coiled-coil homology domain-containing protein (Q54LH0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}.
Interaction partners:
- SNARE-complex protein Syntaxin-18 N-terminal domain-containing protein
- Vesicle-trafficking protein SEC22b
- Uncharacterized protein
- Uncharacterized protein
- Centrosomal protein 103 kDa
- t-SNARE family protein
- V-SNARE family protein
- Alpha-soluble NSF attachment protein
- Golgi SNAP receptor complex member 1
- Sec20 family protein
Sequence:
MTTNISDIKKIEINLKRLISSCEKIIADDDKVDVINGEGEIRPVLIDNTFTVERYIPTMLSLLKQLNEKMYEQNKQQHQHQQQQQQQQSLSSPLFQLYTNTANQLSSPQIAQLSSPSSSSTTPSSSTSTPSSSSSNYIISKEALSEYSRKIDVIVGLVNKEKLNSPISNKPSIVRLQASSISHSKKMDEIQTVMKTRNKEEKKKIDQLIPQNVDNSNNNNSNNNNNNNNNIIKTPNRSNFSSSNNNNLSPALRFRNQFQNRNSELKSLLGNKAAENDNLFNNELLDDDSFEKKTEEQRLQQELLTSELLDYSESLKNHSNTMSTKLSEEDKKLNELGQLVDTSSSKIQRQNLNLKDYTSKSTKDTLNYCLIIVFVLIVFIFTYMLMKLSKKVDPNY
Protein: Holin (Gene product 11) (gp11) (O64204)
Organism: Mycobacterium phage D29 (Mycobacteriophage D29)
Function: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space (Probable). Determines the precise timing of host cell lysis. Participates with the endolysin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell.
Subcellular location: Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04168}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04168, ECO:0000305}.
Interaction partners:
Sequence:
MSPKIRETLYYVGTLVPGILGIALIWGGIDAGAAANIGDIVAGALNLVGAAAPATAAVKVNQQRKDGTLTTSPVDQVTRGVEQVLAAKQNAEAEVERVKQALESAVNGAVPQLGPLASQILNGIQPAYSQPFDPHTQPWNR
Protein: Aminoglycoside (3'') (9) adenylyltransferase (EC 2.7.7.47) (AadA) (Aminoglycoside nucleotidyltransferase (3'') (9) adenyltransferase) (ANT(3'') (9) adenyltransferase) (Q8ZPX9)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Mediates bacterial resistance to the antibiotics streptomycin and spectinomycin, does not confer resistance to kanamycin. Binds ATP first, then antibiotic.
Interaction partners:
- Dihydropteroate synthase
- Peptidyl-lysine N-acetyltransferase YjaB
- Small ribosomal subunit protein uS12
- Dihydrofolate reductase
Sequence:
MTLSIPPSIQCQTEAACRLITRVTGDTLRAIHLYGSAVAGGLKPNSDIDLLVTICQPLTEAQRATLMQELLALSSPPGASAEKRALEVTVVLYSQLVPWCFPPSREMQFGEWLREDICQGIYEPAQQDWDMVLLITQILETSIPLKGERAERLFTPAPAAQLLKALRYPLDLWQSTADVQGDEYHIVLTLARIWYTLSTGRFTSKDAAADWLLPQLPEDYAATLRAAQREYLGLEQQDWHILLPAVVRFVDFAKAHIPTQFT
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q9VNR2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
Interaction partners:
Sequence:
MLLSTSESSTHSASEVAGRLQVDVRTGLKWTEAKYRAKIIGHNELLLVAEDPTWKKYIEQFRNPLILLLLGSALVSVIMKQFDDAVSITIAILIVVTVAFIQEYRSEKSLEELKKLVPPECHCLREGRLDTFLARELVPGDIVHLNVGDRVPADVRLFEAVDLSIDESSFTGETEPARKITDVLLNNTNVKDHSNMKNIAFMGTLVRCGNGKGIVVSTGERSEFGEVFKMMQAEEAPKTPLQKSMDILGAQLSFYSFLIIGVIMLLGWLQGKPLSEMFNISVSLAVAAIPEGLPIVVTVTLALGVMRMAKRNSIVKKLPTVETLGCVNVICSDKTGTLTKNEMTATIIITSDGYMADVTGAGYNDQGEIHIRHCNNVEMAKTNITNLLEIGAVCNNAYIQNGTLLGQPTEGALVAVAMKNGMYATAENYVRIQEYPFSSEQKMMAVKCIHKYNNNKEEIFFAKGALETLLPQCTKYQFGTQTVPLTKQNEAEFLAEAYEIGRKGLRVLALAKGRSMQDLIYCGLVGITDPPRPLVRESIEMLMQSGVRVKMVTGDAQETALAIANLIGIDTIHHQTLSGQEMDQMNEHQLDKVANNVSVFYRVSPRHKLEIVKSLQRSGNIVGMTGDGVNDGVALKKADIGIAMGKNGTDVCKEAADMILVNDDFHTIIAAIEEGKGIFYNIRNFVRFQLSTSIAALALIALATLMDIANPLNAMQILWINIIMDGPPAQSLGVEPVDHDVLKQKPRNVKQPMITKSVVVNVLLSASIIVLGTLWVFQREMADGTLGKTKRDTTMTFTCFVFFDMFNALSCRSQTKSVFTIGLTTNRMFLLAVAFSIIGQMLVVYFPPLQMVFQTEALTPYDIFFLVSLTSSVLVVSEIKKWFERTMERKMYSTRSELDFV