wanglab/gogpt-training-data huggingface dataset:
Protein: Patched (Q6UY90)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Hedgehog protein
- Sonic hedgehog protein
- Hedgehog protein
- Protein smoothened
- Cell adhesion molecule-related/down-regulated by oncogenes
- Growth arrest-specific 1.
- Brother of CDO
- GLI family zinc finger 1
- GLI family zinc finger 2
- E3 ubiquitin-protein ligase
Sequence:
MASAGNAAGALGRQAGGGRRRRTGGPHRAAPDRDYLHRPSYCDAAFALEQISKGKATGRKAPLWLRAKFQRLLFKLGCYIQKNCGKFLVVGLLIFGAFAVGLKAANLETNVEELWVEVGGRVSRELNYTRQKIGEEAMFNPQLMIQTPKEEGANVLTTEALLQHLDSALQASRVHVYMYNRQWKLEHLCYKSGELITETGYMDQIIEYLYPCLIITPLDCFWEGAKLQSGTAYLLGKPPLRWTNFDPLEFLEELKKINYQVDSWEEMLNKAEVGHGYMDRPCLNPADPDCPATAPNKNSTKPLDVALVLNGGCQGLSRKYMHWQEELIVGGTVKNATGKLVSAHALQTMFQLMTPKQMYEHFRGYDYVSHINWNEDRAAAILEAWQRTYVEVVHQSVAPNSTQKVLSFTTTTLDDILKSFSDVSVIRVASGYLLMLAYACLTMLRWDCSKSQGAVGLAGVLLVALSVAAGLGLCSLIGISFNAATTQVLPFLALGVGVDDVFLLAHAFSETGQNKRIPFEDRTGECLKRTGASVALTSISNVTAFFMAALIPIPALRAFSLQAAVVVVFNFAMVLLIFPAILSMDLYRREDRRLDIFCCFTSPCVSRVIQVEPQAYTEPHSNTRYSPPPPYSSHSFAHETHITMQSTVQLRTEYDPHTHVYYTTAEPRSEISVQPVTITQDTLSCQSPESTSSTRDLLSQFSDSSLHCLEPPCTKWTLSSFAEKHYAPFLLRPKAKVVVILLFLGLLGVSLYGTTRVRDGLDLTDIVPRETREYDFIAAQFKYFSFYNMYIVTQKADYPNIQHLLYDLHKSFSSVKYVMLEENKQLPQMWLHYFRDWLQGLQDAFDSDWETGRIMPNNYKNGSDDGVLAYKLLVQTGSRDKPIDISQLTKQRLVDADGIINPSAFYIYLTAWVSNDPVAYAASQANIRPHRPEWVHDKADYMPETRLRIPAAEPIEYAQFPFYLNGLRDTSDFVEAIEKVRVICNNYTSLGLSSYPNGYPFLFWEQYISLRHWLLLAISVVLACTFLVCAVFLLNPWTAGIIVMVLALMTVELFGMMGLIGIKLSAVPVVILIASVGIGVEFTVHVALAFLTAIGDKNHRAMLALEHMFAPVLDGAVSTLLGVLMLAGSEFDFIVRYFFAVLAILTVLGVLNGLVLLPVLLSFFGPCPEVSPANGLNRLPTPSPEPPPSVVRFAVPPGHTNNGSDSSDSEYSSQTTVSGISEELRHYEAQQGTGGPAHQVIVEATENPVFARSTVVHPDSRHQPPLNSRQQPHLDSGSLSPGRQGQQPRRDPPREGLRPPPYRPRRDAFEISTEGHSGPSNRDRSGPHGARSHNPRNPTSTAMGSSVPSYCQPITTVTASASVTVAVHPPPGPGRNPRGGPCPGYESYPETDHGVFEDPHVPFHVRCERRDSKVEVIELQDVECEERPWGSSSN
Protein: Probable acyl-activating enzyme 18, peroxisomal (EC 6.2.1.-) (Q84P17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the peroxisomal activation of 2,4-dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that inhibit root growth.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19043666}.
Interaction partners:
- At4g25315
- Similarity to Ta11-like non-LTR retroelement protein
- WAT1-related protein At5g40240
- At4g01000
- Phosphoribosylaminoimidazole-succinocarboxamide synthase, chloroplastic
- Aldehyde dehydrogenase family 3 member H1
- Vacuolar protein sorting-associated protein 20 homolog 1
- ACT domain-containing protein ACR8
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 2 member C4
Sequence:
MWKSIGELSCDDYVKAGLTLEDAKEFDKLVSDVITKAIETDPRDQWKALVDESVLKPWHPHPLHQLLYYSVYSNWDSSVHGPPLYWFPSLSQSKSTNLGKLMEYHGPRLLGPSYKNPLESFELFRRFSVEHPEVYWSFVIDELSLVFHTPPRCILNKSKPEGTWLPDAVLNIAECCLMPSSHPKKEDDSVAVVWRNEGFDDSPVNRMTIKELREQVMLVANAISGSFEKGDTIAIDMPMTVDAVIIYLAIILAGCIVVSIADSFAAKEIATRLKISKAKGIFTQDYILRGGRRFPLYSRVVEAAPSKVIVLPASGTELHVQLREQDVSWMDFLSNAKPHSSGENYYRPIYLPVESVINILFSSGTTGEPKAIPWTQLSPIRSACDGWAHLDVQVGHTYCWPTNLGWVMGPTLMFSCFLTGATLALYSGSPLGRGFGKFVQDAGVTVLGTVPSLVKTWKRTNCMEGLNWTKIKFFATTGEASNVDDVLWLSSKADYKPVIECCGGTELASSYIIGSPLQPQAFGAFSTPSMTTRIIIFDENGVPYPDDQPCTGEVGLFPQHLGATDRLLNANHDEVYFKGMPMYKETRLRRHGDIVKRTVGGYYNVQGRADDTMNLGGIKTSSIEIERVCDQADECISETAAVTLTPPNGGPELLVIFAVLKEGFKQQSGEELKMKFSRTIQKDLNPLFKVSFVKIVPEFPRTASSKLLRRVLRDQIKQELLSLRSRI
Protein: Enriched in surface-labeled proteome protein 12 (Q57UQ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVMKAFPLSLLAATTVLLLLLPVPGRCADCFAHSNDYSTPGEPFGKSKHTITLSGGNWGTVIGSDGNALKTALLLDIYAQILRRHAFNTSVTVDDMRQGEHGMEAEVTVTQVLLTDVPRADLQHTWNPNEITSLLMQGVYKHTKDKHDPHSDVHLVSVRLPAATTELHKCGKACWTVRLIGIFIGIAMILIAAYTIFITRKWEKQAEKEPDDDSSREPLPEQEQRRSRTRV
Protein: Squalene synthase BSS (EC 2.5.1.21) (Q9SDW9)
Organism: Botryococcus braunii (Green alga)
Function: Converts farnesyl diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in eukaryotes. Does not possess botryococcene synthase activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGMLRWGVESLQNPDELIPVLRMIYADKFGKIKPKDEDRGFCYEILNLVSRSFAIVIQQLPAQLRDPVCIFYLVLRALDTVEDDMKIAATTKIPLLRDFYEKISDRSFRMTAGDQKDYIRLLDQYPKVTSVFLKLTPREQEIIADITKRMGNGMADFVHKGVPDTVGDYDLYCHYVAGVVGLGLSQLFVASGLQSPSLTRSEDLSNHMGLFLQKTNIIRDYFEDINELPAPRMFWPREIWGKYANNLAEFKDPANKAAAMCCLNEMVTDALRHAVYCLQYMSMIEDPQIFNFCAIPQTMAFGTLSLCYNNYTIFTGPKAAVKLRRGTTAKLMYTSNNMFAMYRHFLNFAEKLEVRCNTETSEDPSVTTTLEHLHKIKAACKAGLARTKDDTFDELRSRLLALTGGSFYLAWTYNFLDLRGPGDLPTFLSVTQHWWSILIFLISIAVFFIPSRPSPRPTLSA
Protein: mRNA export factor (Immediate-early protein IE63) (Infected cell protein 27) (ICP27) (VMW63) (P28276)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Also stimulates translation of viral transcripts. Independently, plays a role in the regulation of virion release. Also plays a role in the inhibition of host innate immune response by targeting host IRF3 and therby preventing production of beta-interferon. Silences the 3' splice site of the host promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus. Suppresses also splicing of the viral ICP34.5 mRNA, allowing the virus to express a variant form of ICP34.5.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:25540385}. Host nucleus {ECO:0000269|PubMed:25540385}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:25540385}.
Interaction partners:
Sequence:
MATDIDMLIDLGLDLSDSELEEDALERDEEGRRDDPESDSSGECSSSDEDMEDPCGDGGAEAIDAAIPKGPPARPEDAGTPEASTPRPAARRGADDPPPATTGVWSRLGTRRSASPREPHGGKVARIQPPSTKAPHPRGGRRGRRRGRGRYGPGGADSTPKPRRRVSRNAHNQGGRHPASARTDGPGATHGEARRGGEQLDVSGGPRPRGTRQAPPPLMALSLTPPHADGRAPVPERKAPSADTIDPAVRAVLRSISERAAVERISESFGRSALVMQDPFGGMPFPAANSPWAPVLATQAGGFDAETRRVSWETLVAHGPSLYRTFAANPRAASTAKAMRDCVLRQENLIEALASADETLAWCKMCIHHNLPLRPQDPIIGTAAAVLENLATRLRPFLQCYLKARGLCGLDDLCSRRRLSDIKDIASFVLVILARLANRVERGVSEIDYTTVGVGAGETMHFYIPGACMAGLIEILDTHRQECSSRVCELTASHTIAPLYVHGKYFYCNSLF
Protein: Baculoviral IAP repeat-containing 3 (Q5XIW4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNMVQGSAFLAKLMKSADTFELKYDFSCELYRLSTYSTFPAGVPVSERSLARAGFYYTGVNDKVKCFSCGLMLDNWKQGDSPIEKHRKLYPSCSFVQTLNPANSLEASPQPPLPSTATSTMPSGFAASESTGYFSGSYSSFPSDPVNFRANQDCPAFSTSPYHFAMNTEKARLLTYQTWPLSFLSPAELAKAGFYYTGPGDRVACFACGGKLSNWDRKDDPLSEHRRHFPSCPFLKDVGQFTSQYTVSNLSMQTHAARVRTFSTWPSSALVHPQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLIRIKGQEFVGQVQAGYPHLLEQLLSTSDSPEDETGEAAIVHLGPGENWEDAVMMNTPVVKAALDMGFSRSLVRQTVQRQILATGENYRTVSDLVIGLLDAEDEMREEQTEQEAEEEESDDLTLIRKNKMVLLQHLTPVTPILDCLLSARVITEQEYDAVKQKPHTLQARTLIDTVLAKGNTAATSFRNSLQEIDPGLYRDIFVRQNIRSLPTDDIAALPMEEQLRKLQEERTCKVCMDREVSLVFIPCGHLVVCKECAPSLRKCPICRGTIKGTVRTFLS
Protein: Metallocarboxypeptidase inhibitor b (MCPI) [Cleaved into: Metallocarboxypeptidase inhibitor d (Carboxypeptidase inhibitor d) (NvCId)] (C0HJE8)
Organism: Nerita versicolor (Four-tooth nerite) (Sea snail)
Function: Metallocarboxypeptidase inhibitor. Has an inhibitory effect on bovine CPA1 and porcine CPB1. Does not inhibit D.melanogaster svr (carboxypeptidase D). Shows no activity against serine proteases subtilisin or bovine trypsin, cysteine protease papain, and aspartyl protease porcine pepsin.
Interaction partners:
Sequence:
FHVPDDRPCIKPGRCPLVPDATCTFVCKAADNDFGYECQHVWTFEGQRVGCYA
Protein: Dynein axonemal assembly factor 1 (Leucine-rich repeat-containing protein 50) (Q8NEP3)
Organism: Homo sapiens (Human)
Function: Cilium-specific protein required for the stability of the ciliary architecture. Plays a role in cytoplasmic preassembly of dynein arms. Involved in regulation of microtubule-based cilia and actin-based brush border microvilli.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:18385425}. Cytoplasm {ECO:0000269|PubMed:18385425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18385425}. Note=In HEK293T cells, it is diffusely cytoplasmic and concentrates at the mitotic spindle poles, while in MDCK cells, it localizes in the cilium. In vivo, this protein is probably restricted to the cilium.
Interaction partners:
- Dynein axonemal intermediate chain 2
- Axonemal dynein light intermediate polypeptide 1
- Dynein axonemal heavy chain 5
- Dynein axonemal intermediate chain 1
- Radial spoke head protein 4 homolog A
- Protein kintoun
- Radial spoke head protein 9 homolog
- Dynein axonemal heavy chain 11
- Dynein axonemal assembly factor 3
- Thioredoxin domain-containing protein 3
Sequence:
MHPEPSEPATGGAAELDCAQEPGVEESAGDHGSAGRGGCKEEINDPKEICVGSSDTSYHSQQKQSGDNGSGGHFAHPREDREDRGPRMTKSSLQKLCKQHKLYITPALNDTLYLHFKGFDRIENLEEYTGLRCLWLQSNGIQKIENLEAQTELRCLFLQMNLLRKIENLEPLQKLDALNLSNNYIKTIENLSCLPVLNTLQMAHNHLETVEDIQHLQECLRLCVLDLSHNKLSDPEILSILESMPDLRVLNLMGNPVIRQIPNYRRTVTVRLKHLTYLDDRPVFPKDRACAEAWARGGYAAEKEERQQWESRERKKITDSIEALAMIKQRAEERKRQRESQERGEMTSSDDGENVPASAEGKEEPPGDRETRQKMELFVKESFEAKDELCPEKPSGEEPPVEAKREDGGPEPEGTLPAETLLLSSPVEVKGEDGDGEPEGTLPAEAPPPPPPVEVKGEDGDQEPEGTLPAETLLLSPPVKVKGEDGDREPEGTLPAEAPPPPPLGAAREEPTPQAVATEGVFVTELDGTRTEDLETIRLETKETFCIDDLPDLEDDDETGKSLEDQNMCFPKIEVISSLSDDSDPELDYTSLPVLENLPTDTLSNIFAVSKDTSKAARVPFTDIFKKEAKRDLEIRKQDTKSPRPLIQELSDEDPSGQLLMPPTCQRDAAPLTSSGDRDSDFLAASSPVPTESAATPPETCVGVAQPSQALPTWDLTAFPAPKAS
Protein: ATP-sensitive inward rectifier potassium channel 15 (Inward rectifier K(+) channel Kir4.2) (Potassium channel, inwardly rectifying subfamily J member 15) (O88932)
Organism: Mus musculus (Mouse)
Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q91ZF1}.
Interaction partners:
- Inward rectifier potassium channel 16
Sequence:
MDAIHLGMSSAPLVKHTNGVGLKAHRPRVMSKSGHSNVRIDKVDGIYLLYLQDLWTTVIDMKWRYKLTLFAATFVMTWFLFGVVYYAIAFIHGDLQLGESNSNHTPCIMKVDSLTGAFLFSLESQTTIGYGVRSITEECPHAIFLLVAQLVITTLIEIFITGTFLAKIARPKKRAETIKFSHCAVISKQNGKLCLVIQVANMRKSLLIQCQLSGKLLQTHVTKEGERILLNQATVKFHVDSSSESPFLILPMTFYHVLDETSPLRDLTPQNLKEKEFELVVLLNATVESTSAVCQSRTSYIPEEIYWGFEFVPVVSLSKNGKYVADFSQFEQIRKSPDCTFYCADSEKQKLEEQYRQEDQRERELRSLLLQQSNV
Protein: Tubulin beta chain (A0A1D8PC97)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Dynein heavy chain, cytoplasmic
- Tubulin alpha chain
- Calmodulin
- Kinesin-like protein
- Uncharacterized protein
- Actin
- TOG domain-containing protein
- Mlc2p
- Microtubule-binding protein
- Spindle assembly checkpoint component MAD2
Sequence:
MREIIHLSTGQCGNQIGAAFWETICGEHGLDNNGTYVGNNELQKSKLDVYFNEATSGKYVPRAVLVDLEPGTIDNVKTSQIGNLFRPDNFIFGQSSAGNVWAKGHYTEGAELVDSVLDVVRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVVPSPKVSDTVIEPYNATLSVHQLVENSDETFCIDNEALYNICQNTLKLPQPSYAELNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTSMGSKSFRSVTVPELTQQMFDAKNMMAASDPRNGRYLTVAAFFRGKVSVKEVDDEMHKIQTRNSSYFVDWIPNNVQTAVCSVPPKDLDMSATFIGNSTSIQELFKRVGDQFSAMFRRKAFLHWYTSEGMDEMEFTEAESNMNDLVSEYQQYQEASIDEEELEYADEIPLEDAAME
Protein: UDP-glucuronosyltransferase 2B11 (UDPGT 2B11) (EC 2.4.1.17) (O75310)
Organism: Homo sapiens (Human)
Function: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Subcellular location: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 3A4)
- Cytochrome P450 2D6
- Cytochrome P450 1A1
- Cytochrome P450 2A6
- Cytochrome P450 2E1
- Cytochrome P450 3A5
- Beta-glucuronidase
- Cytochrome P450 2A13
- UDP-glucose 6-dehydrogenase
- Aldehyde oxidase
Sequence:
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSASILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELYDIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTIERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVLGRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTMSSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAAHDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Protein: 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) (Global regulator YmdB) (O31775)
Organism: Bacillus subtilis (strain 168)
Function: Plays a central, regulatory role in the late adaptive responses and affects the levels of many genes. May act via regulation of cAMP levels. Decreases the expression of motility genes and induces genes involved in biofilm formation, by controlling the expression of SlrR. Required for formation of intercellular nanotubes that bridge neighboring cells to allow molecular exchange. Plays a key role in directing the early stages of colony development. In vitro, has a metal-dependent phosphodiesterase activity against 2',3'-cAMP and 2',3'-cGMP. Has also 3',5'-cyclic-nucleotide phosphodiesterase activity, but cannot use cyclic di-AMP or cyclic di-GMP, and does not have phosphatase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26906740}. Note=Localizes to the cytoplasm, cell periphery and nanotubes. {ECO:0000269|PubMed:26906740}.
Interaction partners:
- Ribonuclease Y
- Uncharacterized protein YuxH
- Putative triphosphatase YjbK
- HTH-type transcriptional regulator SlrR
- HTH-type transcriptional regulator SinR
- Protein SinI
- Bifunctional protein FolD
Sequence:
MRILFIGDVVGSPGRDMVKEYVPKLKTKYKPHFTIINGENAAHGKGLTEKIYHSLIQSGADAITMGNHTWDKKEIFDFIDDVPNLVRPANFPEGTPGKGITYVKANGKELAVINLQGRTFLPPLDDPFLKADELIAEAAKRTPYIFIDFHAEATSEKLALGWYTDGRASAVVGTHTHVQTADNRILPKGTAYITDVGMTGPYDGILGMDRETIIKRFKTNLPVRFTVAEGKTTLSGVVIDIDDQTKKAVKIERILINDDHMFFE
Protein: Dorsal interacting protein 3 (RE40480p) (Q7JZD5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00371}.
Interaction partners:
- Embryonic polarity protein dorsal
Sequence:
MSRKNGNQDTFPKTEKMQRYYAERETTGPEFDDRLIKLVRANPAIYDVSHPHYRRNPVRVDIWDRIANELGASSRFLQTKWKNIRYNYLQEVKAIETGQANPNVRKRRFTEDLSFLQNTAQTYNVKKSQSYVAQQNGMGSDNDSNSFLYPDPEHLKIDASEGYDIIELDNSDDGSNSDDNEIVPELQLVMGESKQQLSLPTTLNGTSSSNHSHEHDQASSPASSPLLTPMVVMGNGYGQEVHLEQQQTQEQKPFKNSSLSNGEVTIEPIYKPAAIRRALPSDFLTNPFKRKATQAPLQTQVTSSFNDPIELYCLSLVDTLRSMRRSERERVKFEFANILKDAKYKDES
Protein: Cysteine-rich hydrophobic domain-containing protein 2 (BrX-like translocated in leukemia) (Q9UKJ5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:11257495}. Cytoplasmic vesicle {ECO:0000269|PubMed:11257495}. Note=Also present at a Golgi-like vesicular compartment and at scattered vesicles.
Interaction partners:
- Transcription factor ETV6
- Pre-mRNA 3'-end-processing factor FIP1
Sequence:
MADFDEIYEEEEDEERALEEQLLKYSPDPVVVRGSGHVTVFGLSNKFESEFPSSLTGKVAPEEFKASINRVNSCLKKNLPVNVRWLLCGCLCCCCTLGCSMWPVICLSKRTRRSIEKLLEWENNRLYHKLCLHWRLSKRKCETNNMMEYVILIEFLPKTPIFRPD
Protein: Adenylyl cyclase-associated protein 2 (CAP 2) (P40123)
Organism: Homo sapiens (Human)
Function: May have a regulatory bifunctional role.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Cofilin-1
- Twinfilin-2
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Drebrin
- Adenylyl cyclase-associated protein 1
- Glutaredoxin domain-containing cysteine-rich protein 1
- Drebrin-like protein
- Profilin-4
- Cofilin-2
Sequence:
MANMQGLVERLERAVSRLESLSAESHRPPGNCGEVNGVIAGVAPSVEAFDKLMDSMVAEFLKNSRILAGDVETHAEMVHSAFQAQRAFLLMASQYQQPHENDVAALLKPISEKIQEIQTFRERNRGSNMFNHLSAVSESIPALGWIAVSPKPGPYVKEMNDAATFYTNRVLKDYKHSDLRHVDWVKSYLNIWSELQAYIKEHHTTGLTWSKTGPVASTVSAFSVLSSGPGLPPPPPPLPPPGPPPLFENEGKKEESSPSRSALFAQLNQGEAITKGLRHVTDDQKTYKNPSLRAQGGQTQSPTKSHTPSPTSPKSYPSQKHAPVLELEGKKWRVEYQEDRNDLVISETELKQVAYIFKCEKSTIQIKGKVNSIIIDNCKKLGLVFDNVVGIVEVINSQDIQIQVMGRVPTISINKTEGCHIYLSEDALDCEIVSAKSSEMNILIPQDGDYREFPIPEQFKTAWDGSKLITEPAEIMA
Protein: CBL-interacting serine/threonine-protein kinase 11 (EC 2.7.11.1) (SNF1-related kinase 3.22) (SOS2-like protein kinase PKS5) (SOS3-interacting protein 4) (O22932)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Acts as a negative regulator of the plasma membrane proton pump AHA2 by preventing its interaction with 14-3-3 protein.
Interaction partners:
- Calcineurin B-like protein 2
- Calcineurin B-like protein 3
- Calcineurin B-like protein 9
- Calcineurin B-like protein 10
- Calcineurin B-like protein 4
- Calcineurin B-like protein 5
- Calcineurin B-like protein 1
- Calcineurin B-like protein 7
- ATPase 2, plasma membrane-type
- ATPase 5, plasma membrane-type
Sequence:
MPEIEIAAGSGDNNDALFGKYELGKLLGCGAFAKVFHARDRRTGQSVAVKILNKKKLLTNPALANNIKREISIMRRLSHPNIVKLHEVMATKSKIFFAMEFVKGGELFNKISKHGRLSEDLSRRYFQQLISAVGYCHARGVYHRDLKPENLLIDENGNLKVSDFGLSALTDQIRPDGLLHTLCGTPAYVAPEILSKKGYEGAKVDVWSCGIVLFVLVAGYLPFNDPNVMNMYKKIYKGEYRFPRWMSPDLKRFVSRLLDINPETRITIDEILKDPWFVRGGFKQIKFHDDEIEDQKVESSLEAVKSLNAFDLISYSSGLDLSGLFAGCSNSSGESERFLSEKSPEMLAEEVEGFAREENLRMKKKKEEEYGFEMEGQNGKFGIGICISRLNDLLVVVEARRRGGDGDCYKEMWNGKLRVQLIRVCDQTSSTNAAI
Protein: tRNA ligase phosphodiesterase domain-containing protein (Q581X4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMGCGGSKLSAKSKQADADPPKPSDPADAHRFERICTLPLHDGEKPMIFGAIMINDLAAVRSLVPADYLEGKNMQDEFHITTIYLGGKPPQDDELFKKLQTLEGTSIQVAPVRIASDAKATAIEIRNNNEFPCQNVHPHITIATAPGVPAKYSNELLSKVSTETSDIKVMELSPDVSISGVFQFVR
Protein: GTPase-activating protein GYP3 (Multicopy suppressor of bud emergence 3) (Protein MSB3) (P48566)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates exocytosis by functioning as a GAP for SEC4. Stimulates specifically the GTPase activity of YPT6. Also required for efficient polarization of the actin patches.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10679030}. Bud {ECO:0000269|PubMed:10679030}. Bud neck {ECO:0000269|PubMed:10679030}. Note=Localizes to the presumptive bud site, the bud tip and the mother-bud neck.
Interaction partners:
- Protein BNI1
- Bud site selection protein 6
- Protein SPA2
- Protein PEA2
- GTPase-activating protein MSB4
- Ras-related protein SEC4
- Cell division control protein 42
- Vacuolar protein sorting-associated protein 21
- GTPase-activating protein GYP1
- GTPase-activating protein GYP7
Sequence:
MQNDQQRFSLQNRTVLAHPYKRLGGAFTVKSPSVPNFHDKMHSDHSSSDSALVNGSFRANDHRSVEPSCLGQASPSEHDGNLSVIDLYGDEVESQRAEGEDDDDNNGDNGNEDLEEVHSDDLDLVPDDDNRQRVELEGAASATSANSNGINNTHFDRYGFKKQNNYISEAEYDKWWVEYSQYCVRRKHKWQLLLEKSGLPVTDDSPSRFPSKSERLKRYVRKGIPAEWRGNAWWHFARGQEKLNKNKGVYSQLLRKMKQIKKQNPNEKQVQDLDIIERDLNRTFPDNIHFQSSLHNKEGPPIIKSLRRVLVAFSLYNPKIGYCQSMNFLAGLLLLFLDEERAFWMLVIITSRYLPGVHNINLEGVNIDQGVLMLCVKEYIPEVWSYIKPSIDHHQKNNKTFSPSNKKVLFNMQKNEFLYRLPPITLCTASWFMSCFVGVVPIETTLRIWDCLFYEESHFLFKVSLAVLKLSEHDLSKIKPRNNSLNYSWGSNLNQRGGSMGQEDSDMEIFQVIQTFPKTLLNPNEIFEKIIFKRRFNLNRLDQDEIDRCRKFVAAQRLKFKTYGELLGNSTSEADLPINDNTDNKGIHITSDAVNEALSSEVYGFKKSLAGVHWNNSIKEKVKQMRKKKDKGD
Protein: Xyloglucan 6-xylosyltransferase 4 (EC 2.4.2.39) (Putative glycosyltransferase 4) (AtGT4) (EC 2.4.-.-) (Q9M9U0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Xylosyltransferase specific to UDP-D-xylose that accepts cellohexaose as substrate to produce xyloglucan.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- DNAJ heat shock N-terminal domain-containing protein
- Probable glycosyltransferase At3g42180
- Probable glycosyltransferase At5g11130
- L-arabinokinase
Sequence:
MFQDGSRSSGSGRGLSTTAVSNGGWRTRGFLRGWQIQNTLFNNIKFMILCCFVTILILLGTIRVGNLGSSNADSVNQSFIKETIPILAEIPSDSHSTDLAEPPKADVSPNATYTLEPRIAEIPSDVHSTDLVELPKADISPNATYTLGPRIAEIPSDSHLTDLLEPPKADISPNATYTLGPKITNWDSQRKVWLNQNPEFPNIVNGKARILLLTGSSPGPCDKPIGNYYLLKAVKNKIDYCRLHGIEIVYNMANLDEELSGYWTKLPMIRTLMLSHPEVEWIWWMDSDALFTDILFEIPLPRYENHNLVIHGYPDLLFNQKSWVALNTGIFLLRNCQWSLDLLDAWAPMGPKGKIRDETGKILTAYLKGRPAFEADDQSALIYLLLSQKEKWIEKVYVENQYYLHGFWEGLVDRYEEMIEKYHPGLGDERWPFVTHFVGCKPCGSYADYAVDRCFKSMERAFNFADNQVLKLYGFSHRGLLSPKIKRIRNETVSPLESVDKFDIRRMHMETKP
Protein: Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) (E1JHN2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03190}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03190}.
Interaction partners:
Sequence:
MMRNALLVSGKLRHLLSCSIGRNSTRSSSTAKSLDAGTQKEVRHHENHASEWWNQNGTMGALHALNEIRVPFIRDGIVSRGTVKPGYVNTTKVLLGQNILEVGCGGGLLTEHLARLGAQVAGIDLGEKLIEAAREHLKCSSPELASNVVYKIEPVDQHAKANCECYDAVIVSEVLEHVKDKVSLLEASVRSLKPGGSIFITTLNKTIPSWFGGVLLSEYVLNLVPRGTHHWDKMISPLDVQRILDTMNCQTVLVNGSTYDFWSNTWRWINNNQMCYALQAVKQAQREYN
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (N-ethylmaleimide-sensitive fusion protein) (NEM-sensitive fusion protein) (Vesicular-fusion protein NSF) (Q94392)
Organism: Caenorhabditis elegans
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Alpha-soluble NSF attachment protein
- Vesicle-trafficking protein SEC22b
- Sec1 family domain-containing protein 1
- Syntaxin-1A homolog
- Putative syntaxin-5
- YKT6
- t-SNARE coiled-coil homology domain-containing protein
- Synaptobrevin-1
- t-SNARE coiled-coil homology domain-containing protein
- BET1 homolog
Sequence:
MSPVPCLSTCCCFRKIVEYSTMSWFRKSANDSLLETNHDRIPVAPPREVRAPSPRLPPSYQTSNEKMFRVRKAPSEEHTLANYAYVNRSDFDDKQIKHVRVNPGPAHHYIFSIRNDGSIKPGEIAFGVPHRKWAALSLDQEVRVTPFTFQQSEYVGSMILTADFNAKKNVTSEPLNADLMAREFSIQFGGQAFSKGMQMAFRFEDKEKNKTHTLSLVVKSIEGFDIGKAAAAASGASNTDSSATKPKQIEAGELLPNSVIVFDKEEGSMLNLIGKSKGKSAYRSIINPDWDFQQMGIGGLDTEFSHIFRRAFASRVFPPEFIEQLGMKHVRGILLFGPPGTGKTLMARQIGKMLNAREPKIVNGPQILDKYVGESESNVRKLFADAEEEWRRCGANSGLHIIIFDEIDAICKQRGSMAGSSSVHDTVVNQLLSKMDGVEQLNNILVIGMTNRRDMIDEALLRPGRLEVQMEVSLPDETGRLQILKIHTARMREYNKMDPNVDLEDISKRTKNFSGAELEGLVRAAQSSAMNRLVKAGGKAQADPDAIEKLAINSGDFDYALENDIKPAFGRSDESLNRFLSRGMIVWGPEVTKILDEGSLLAATVKNPENSGFRTVVLAGAAKTGKTSLAAQMAKSSDFPFVKVISPEDTVGFSESAKCMALKKAFEDAKRSKLSVLLIDNLERLIDYHPVGPRYSNLVIQALLVLLNAPPPAGHRLFVIATSSDRMFLRDMGLMDVFGDVIDIPKLTTAGQMMNVIQESNIYSDDQLPMIEQKLASICRGEGFHGVGIKHLLELIESARQCEADYRVPTLLNMMEGLALNLYR