wanglab/gogpt-training-data huggingface dataset:
Protein: Caveolin-2 (Q2IBC5)
Organism: Rattus norvegicus (Rat)
Function: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression.
Subcellular location: Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and, in response to insulin, is translocated to the nucleus in complex with MAPK1. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. The CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. The Ser-36-phosphorylated form resides in intracellular compartments (By similarity). {ECO:0000250}.
Interaction partners:
- Caveolin-1
- Caveolin-3
- Proto-oncogene tyrosine-protein kinase Src
- Receptor protein-tyrosine kinase
- Tyrosine-protein kinase Fyn
- Integrin beta-1
- Major prion protein
- Integrin beta-4
- Integrin beta
- Integrin beta-6
Sequence:
MGLETEKADVQLFMADDAYSHHSVVDYTDPEKYVDSSQDRDPHQLNSHLKLGFEDLIAEPPTTHSFDKVWICSHALFEISKYVIYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVVIGPLCTSVGRIFSSVSMQLSHD
Protein: Acclimation of photosynthesis to environment (At5g38660) (Q2HIR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGSITVAPGTTVLFSSRRLDLCGRRHENLSVVSSSQPSLMPKQRWLYIPETRLKREVLKLDVVGRAADSTSSSPSVASGDRTLIPDDEFTLAKISFGVIGLGLGVSLLSYGFGAYFTILPGTEWSAIMLTYGFPLSIIGMALKYAELKPVPCLSYSDAVKLRESCATPILTQVRNDVTRYRYGDEQHLEEALKRIFQYGLGGGIPRRSAPILQLIREEVLTDGRYCVVLVFEAKALTLSDFEKRQAKFTSFFGPNITAEVGKGESENLYEVRLISNLSTNSVSSTS
Protein: Xylan 1,3-beta-xylosidase (EC 3.2.1.72) (A9ZND1)
Organism: Vibrio sp
Function: Beta-1,3-xylosidase that hydrolyzes beta-1,3-xylooligosaccharides to D-xylose.
Interaction partners:
Sequence:
MTTTIQNPILKGFNPDPSIVRVGDDYYIATSTFEWFPGIQLHHSRDLINWRLVGHALTRTSQLNMMGMDNSEGVYAPALTYSDGTFWLCFSNVHSCRGGNWMATPSYVVTADSIEGPWSEPVPIGNYGFDPSLFHDDDGKKYMLNMIWGGRAKTNFFGGIIMQEFDADEGKLVGAPKTVFEGTELGCTEGPQLLKKDDYYYLITAEGGTERNHAVTVCRSKHIWGPYEVHPENPILTSRFQEHAELSRAGHGFLVETQTGEWYMSHLCGRRIPNPEGYQFMPKYDNGFSILGRESALQKAHWQDDWPYIATGKTPVVEVEAPNLPLHPWPESPARDEFIDPTLSLISTLREPVSEKWLSLSERPGFLRLKGRHYLYSRYEQSMVARRFQAHNATVETKLEFKPNTPYEMAGLCAYYARNGHYFLKMTANDLGERVLQVVGNINDVYGEYSNDVVIGDADTVYMRLELKTQWYQYSYSLDGVDWYEIGPALNSTPLSDEGGPDIFRFTGSFAALFVADITGQKRHADFDYFEYLEH
Protein: Regulator of chromosome condensation (Q57YT1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRRLHTRILGMGSVCGMPPSPMAEVFLKSLPPPAQVDLVKYHRFEQEEANRMRVPRCTTSPEPFYDIQSGAAGHKHVVLITREGNLITFGENRYGQSAAPGESVRGGGRLGENRQQPLAKHSDQHVSAAPMYVDLDGAFAGGNKSVACGSNYTIVYQPGGRRAIGFGNNHMGQLGIGHKKQVDASRGFAEWDPTAAWWGGNTNVIRTITCGFNHTILQLSSGELLSFGSNTWGELGIGSTVSPMQPTPIRFFEEKGIVVVKTVAGNSFTLFLTADGRVYGCGATNAGQLPANVFEPAPVLLTRSFQQGCKVVPGRVHGGPTQPKLIRIKDIACVGSMAVYASRKNELFVQGALPDYGYQVPSPRFQLVDQQPAIDYLTEMMEHNKKKGGTRWMDDKGSEAHTGFDIVRLVQGPSTLLVIYKNGCVAGLGANAEGQLQNIRRSQKGKEVNLAKAFTANGLLPVCFPSKPYEAGGKQTAALPWFTCGAGFTLLFDNNEVYDDGGQVKPIELPPPAPTSRRGAAAALRSMR
Protein: ATP-dependent RNA helicase DDX25 (EC 3.6.4.13) (DEAD box protein 25) (RNA helicase DEADSouth) (Xcat3) (Q9DGP9)
Organism: Xenopus laevis (African clawed frog)
Function: ATP-dependent RNA helicase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10906480, ECO:0000269|PubMed:11784096}. Nucleus {ECO:0000250|UniProtKB:Q9QY15}. Note=Also detected in chromatoid bodies of round spermatids. {ECO:0000250|UniProtKB:Q9QY15}.
Interaction partners:
Sequence:
MAAKFLPRFWRSGSQAELLDFQNNNVVAEGKLDFEHGTLKGKSGRYGDDEEDVRRGHIEDLANHSLLNKLLRRTLVDSPHNVEVLQRDPTSPLFSVKSFEELHLKNELLRGIYAMGFNRPSKIQENALPMMLADPPQNLIAQSQSGTGKTAAFVLAMLSRVDANKKYPQCICLSPTFELALQTGKVVEEMGKFCAGIEVIYALRGNRPGKGSRLEAQIVIGTPGTVLDWCFKLRLITVENISVFVLDEADVMINVQGHSDHSVRVKRSMPKSCQMLLFSATFEDSVWAFAERIVPDPNIIKLKKEELTLKNIQQFYDQCENKEQKYSALCNLYGVITIAQAIVFCQTRKIASWLSQKLSDDGHQVALLSGELPVYDRADMIQRFREGREKVLVTTNVCARGIDVEQVSIVVNFDLPVNVDGSVDFETYLHRIGRTGRFGKKGIAVSLIENFFVYMLKEIEDHFNTKITKLNSMDMDEMGKIWK
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Q7ZVQ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTVEQNVLQQHSQKHQQTLLNQLREVTGTTDVQLLQQALQVSNGDLVEAVAFLTEKNAKVPQQDEATYYQTAQITNDRYISVGSQADTNVIDLTGDDKDDLQRAIALSLEESNRAFRETGITDEEQAISRVLEASIAENKASLKRTHTEVWSDSPNPHERKRMENCPVGLKNVGNTCWFSAVIQSLFNLLEFQRLVLHYSPPARMQDLPRNQKEHRNLPFMQELRHLFSLLVGSKRKYVDPSGAVEILKDAFKSSESQQQDVSEFTHKLLDWLEDAFQIKAEEDREGEKPKNPMVELFYGRFLAVGVLEGKKFENTEMFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSAENSAKSGQEHWFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPSMLYMDSYMDRNREITRIKREEIRRLKEHLTVLQQRLERYLSYGSGPKRFPLADVLQYAMEFASSKPVCTSPVEDIDTTAPPGGTIAQLPPPASAGEQPDACVSAEGSGSGLQASQQQQQRVSIHKPFTQSRVPPDLPMHPAPRHITEEELRVLESCLHRWRSEVENDTRDLQASISRIHRTIELMYSDKSMMQVPYRLHAVLVHEGQANAGHYWAYIYDRHHQRWMKYNDIAVTKSSWEELVRDSFGGYRNASAYCLMYIDDKKPFLIQEEFDKETGQMLSGLDKLPPDLKVFVEADNKLFEREMEEWDALQARKLQQEKLALAAAAAAAAAASVAVQPMSTEPCSPDNTAPQHDPEYMEQQSPSGDSKHLQEDTERAISKAAAEHDEKSPEALLNTAMKVEYTRLLRLAQEDTPPERDYRLQHVIVFFIHNEAPKKIVERTLLMQFADRNLGFDERCKSIMKVARAKLELIKPDEVNMEEYEMWHQDYRIFRETSVFLLIGLELFMKKSFVEALMYLIYAYQYNKELLAKGPYRGHDEELIAHYRRECLLKLNEYAAALFETGEEAKVNTGLSIMNDLVVPCLPLLLVDEMEEKDMVAVEDMRNRWCSYLGQEMEPNLQEKLTDFLPKLLDCSTEIKSFHEPPKLPSYSTLELFERFGRVMTSLTMGRTPADGR
Protein: Antiholin (Lysis inhibitor S-107) (P03705)
Organism: Escherichia phage lambda (Bacteriophage lambda)
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. Determines the precise timing of host cell lysis. Participates with the endolysin and spanin proteins 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:0000269|PubMed:2137120}; Multi-pass membrane protein {ECO:0000269|PubMed:19897658}. Note=Classified as a class I holin. {ECO:0000305}.
Interaction partners:
Sequence:
MKMPEKHDLLAAILAAKEQGIGAILAFAMAYLRGRYNGGAFTKTVIDATMCAIIAWFIRDLLDFAGLSSNLAYITSVFIGYIGTDSIGSLIKRFAAKKAGVEDGRNQ
Protein: Vacuolar protein sorting-associated protein 54 (Q22639)
Organism: Caenorhabditis elegans
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 51 homolog
- Vps54_N domain-containing protein
- EARP-interacting protein 1
- Putative syntaxin 6
- t-SNARE coiled-coil homology domain-containing protein
- Vacuolar protein sorting-associated protein 35
- Exocyst complex component 6
- Exocyst complex component 3
Sequence:
MKSMDDRTVGLISASSSRASLKIQPEIGYPRICDYCQPIIELMTASEFARHIRQDHTTKEGGSFLCRYGEHGVCQKLPLEGVCDLDFEAHIRRCHTSSQPAGYSSPTSSLVASYTEDSEETASLRSIRLTSDRDTPTIEKKKFTLHSFTQNLSAVLADPSRSRSDLTTFFTRHWGDSFVPTQPVPQSKRLARLADSAFDSYCQSAGESYRRYQAIKRALRLSHADGGVGIGDERQDAEDLPTIFIDPRFTLGDSSTFSDVFTVPANDDLDALKQTLSGRNVIPATPLEIATNRKPGEFRDYEALQNRLEMMHDVVDGRLAGKLVAKTDDFWQVVRSYSGLQEQLANALQCVMVVRKNLKRVDELVCDQSKKIVEVHERYEQKKKLLAKLHDISCLREAQSTVQMMLSQGDYPKAIECIETSLDVLSKELNGVTCFRHLASQLRELYTVIGRMMNEDFASLIQKELGVKPEAGTMIQAEGELSAVLLGLMRMRKYSFIAVLREEIIEGVKSVMRQVIKNQILNNGVDLNDFDPSLTQLGEPVRRMKHADFLKTVKAVMDEEFYFCKRLEALQDILLETVERANPLHRHGSEDIIVERIEEAKDIHESESDDEVGTTFSKSASSGGFSVGGSALSSNASATTLLSIEVRSEAFLRHVLPLIAEFGHQCAQQRISRLLIARAKNASVTEATTPTQLSECIKLVKEFQSKCDKEGWYSTQNQKVGGLGRSVNKLSMDYIEKFHAARKIRIGNMLDTELWKATDVSIVDQNIVDMAMETGQLRNTKRIDDGPIKKSFKRTESAVTIDSTTSTSNQIQGVIVDEENYVVVGSSITMIQLLSDYCEAISEMPSFSQDWNSRVVELLKTFNSRCCQLILGAGALQLVGLKTISVRNLALAGRSLELVCRFIPMVHDEMDRVLPENRKSLLRYFKQVESEYRDHVNEIAAKLISVIAHYTTNCLGMWDVKGVIPSPEFQQICRHMLKFHNGLVGIMPRDQIEALFRQVHENFKANLREHVTGMGITPHDPLKYGYVTKDYMFYQQNVKNMESCRNLELESLNDIMFE
Protein: Homeobox protein Hox-D13 (D4ACD0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Sonic hedgehog protein
- Nuclear pore complex protein Nup98-Nup96
Sequence:
MSRSGTWDMDGLRADGGAAGAAPASSSSSVAAPGQCRGFLSAPVFAGTHSGRAAAAAAAAAAAAAAASSFAYPGTSERTGSSSSSSSSAVIATRPEAPVAKECPAPAAAATAAAPPGAPALGYGYHFGNGYYSCRMSHGVGLQQNALKSSPHASLGGFPVEKYMDVSGLASSSVPTNEVPARAKEVSFYQGYTSPYQHVPGYIDMVSTFGSGEPRHEAYISMEGYQSWTLANGWNSQVYCAKDQPQGSHFWKSSFPGDVALNQPDMCVYRRGRKKRVPYTKLQLKELENEYAINKFINKDKRRRISAATNLSERQVTIWFQNRRVKDKKIVSKLKDTVS
Protein: Microtubule-associated protein (Q9VB13)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU000686}.
Interaction partners:
Sequence:
MADVLEKSSLLDAVPPLGDPHPPLPHQQLQQEAAAAAAANAAPPAPPQQQQPPPHQLQQQQPQQQQLQQKPANARANQDQKEGDNDSGVDESTQEKDRNGPNSPSSPVKTPTSTSSKPDKSGTSRPPSATPSNKSAPKSRSASKNRLLLKTPEPEPVKKVPMNKVQVGHAPSPNLKAVRSKIGSLDNATYKPGGGHVKIESKKIDIKAAPRIEAKNDKYMPKGGEKKIVTTKLQWNAKSKIGSLENAAHKPGGGDKKIETLKMDFKDKAKPKVGSTANVKHQPGGGDIKIQTQKLEIKAQSKVGSLDNVKHKPGGGEKKIFDDKDYLKNVEHSVALTTPPTQSPLPSMTASGADENLNQQS
Protein: Cathelicidin-related antimicrobial peptide Bf-CRAMP (Cathelicidin-BF) (Vipericidin) (B6D434)
Organism: Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
Function: Potent antimicrobial peptide against most of Gram-negative bacteria, some Gram-positive bacteria (Bacillus) and some fungi (C.albicans, P.pastoris, A.terreus, A.nidulans, and C.globosum). Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells.
Subcellular location: Secreted {ECO:0000269|PubMed:18795096}. Target cell membrane {ECO:0000269|PubMed:18795096}. Note=Forms a helical membrane channel in the prey.
Interaction partners:
Sequence:
MEGFFWKTLLVVGALAIAGTSSLPHKPLIYEEAVDLAVSIYNSKSGEDSLYRLLEAVSPPKWDPLSESNQELNFTMKETVCLVAEERSLEECDFQEDGVVMGCTGYYFFGESPPVVVLTCKPVGEEGEQKQEEGNEEEKEVEEEEQEEDEKDQPRRVKRFKKFFRKLKKSVKKRAKEFFKKPRVIGVSIPF
Protein: Solute carrier family 43 member 1a (F2Z4V7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Large neutral amino acids transporter small subunit 2
Sequence:
MKGMAPSLEQAFRRRWWMAVTAVLENLLCSAVLLGWGSLLIMLKREGFYSHLCTENKTVNATGEEDKWLSCVEQEEMLNLGFTIGSFLLSAATLPLGILMDRFGPRPLRLTGSACFALSCVMMSVSAYQPEVLSAIIFLALSFNGFGGICLTFTSLTLPNMFGSLSSTVMSLMIGSYASSAVTFPGVKLIYDAGVSFTLIMWMWAGLAGLVFLNCFFNWPEKGFATPEEIETKKMHEAENHKLTPAEEATGETKKPALPQETQTASVPFRRSVFSPIFLWSLITMGMTQLRIIFFMGAMNKMLEFMVTHGDPHPSEELQYTAKKNVSFYSSIFGTLQLLCLVTCPLIGYIMDWKMKECEVDQAVDGEKRAVAVPKRDGKIQKLTNAMRAFIFTNILLILFGILSLINNLPLQILTFILHTMVRGFIHSCCGGMYAAVYPSNHFGTLTGLQSMISAVVALLQQPLFMIMVGPLNGDAFWINLGLLIFSFTGFLLPGYLFYHRRQLQIQAKGKTSTHTPDENQALTNGHSNGHVPQEA
Protein: Fructose-bisphosphate aldolase (EC 4.1.2.13) (Aldolase-1) (P07764)
Organism: Drosophila melanogaster (Fruit fly)
Function: May take part in developmental stage-specific or tissue -specific sugar-phosphate metabolisms. Protein acts on two substrates fructose 1,6-bisphosphate and fructose 1-phosphate (like other class I aldolases).
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Enolase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Triosephosphate isomerase
- Fructose-1,6-bisphosphatase isozyme 2
- Glyceraldehyde-3-phosphate dehydrogenase
- transketolase
- Probable transaldolase
Sequence:
MTTYFNYPSKELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAKKNTPEEIALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKANGDAAQGKYVAGSAGAGSGSLFVANHAY
Protein: Multiple C2 domain and transmembrane region protein 2 (Q9FI32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:29259105}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- 16 kDa phloem protein 2
Sequence:
MRNTTKLVVHVVDAQYLMPRDGQGSASPFVEVDFLNQLSKTRTVPKSLNPVWNQKLYFDYDQSVINQHNQHIEVSVYHERRPIPGRSFLGRVKISLCNIVYKDDQVYQRFTLEKKWLLSSVKGEIGLKFYISSSEEDQTFPLPSKPYTSPTQASASGTEEDTADSETEDSLKSFASAEEEDLADSVSECVEGKKSEEVKEPVQKLHRQEVFARPAPMQSIRLRSRENPHEAQKPMSRGANQLHPQNPNHLQSYGDTDLDDFKVKDMNLDLGERWPNPNAGERFTGTYDLVEQMFYLYVRVVKAKELPPGSITGGCDPYVEVKLGNYKGRTKIFDRKTTIPEWNQVFAFTKERIQSSVLEVFVKDKETLGRDDILGKVVFDLNEIPTRVPPNSPLAPQWYRLEDWRGEGKVVRGEIMLAVWMGTQADEAFPEAWHADSASVHGEGVFNIRSKVYVSPKLWYLRVNVIEAQDMIPSDRNRLPDVFVKASVGMQTLKTSICSIKTTNPLWKEDLVFVVAEPFEEQLVISVEDRVHTSKDEVIGKITLPMNVFEKRLDHRPVHSRWFNLDKYGTGVLEPDARRKEHKFSSRIHLRICLEGGYHVMDESTMYISDTRPTARQLWKQPVGMLEIGILGANGLVPMKLKDGRGSTNAYCVAKYGQKWVRTRTILDTLSPRWNEQYTWEVYDPCTVITLGVFDNSHLGSAQSGTADSRDARIGKVRIRLSTLEAHKIYTHSFPLLVLQPHGLKKTGDLQISVRFTTLSLANIIYNYGHPLLPKMHYLFPFTVNQVDGLRYQAMNIVSTRLGRAEPPLRKEVVEYMLDVDSHLWSMRRSKANFFRIMSLLSGYFLVGKWLEDVCNWRYPVTSVLVNVLFFILVMYPELILPTMFLYMFFIGLWNFRSRPRHPPHMDMKLSWAEAVGPDELDEEFDTFPTSRSQELVRLRYDRLRSVAGRIQTVVGDIAAQGERIQSLLSWRDPRATSLFILFCLAASVVLYAMPFKAIALASGLYYLRHPKFRSKLPSLPSNFFKRLPSSTDSLL
Protein: GRB2-associated-binding protein 1 (GRB2-associated binder 1) (Growth factor receptor bound protein 2-associated protein 1) (Q13480)
Organism: Homo sapiens (Human)
Function: Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR). Involved in the MET/HGF-signaling pathway.
Interaction partners:
- Growth factor receptor-bound protein 2
- Epidermal growth factor receptor
- Tyrosine-protein phosphatase non-receptor type 11
- SHC-transforming protein 1
- Crk-like protein
- Son of sevenless homolog 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Hepatocyte growth factor receptor
- Son of sevenless homolog 2
- Adapter molecule crk
Sequence:
MSGGEVVCSGWLRKSPPEKKLKRYAWKRRWFVLRSGRLTGDPDVLEYYKNDHAKKPIRIIDLNLCQQVDAGLTFNKKEFENSYIFDINTIDRIFYLVADSEEEMNKWVRCICDICGFNPTEEDPVKPPGSSLQAPADLPLAINTAPPSTQADSSSATLPPPYQLINVPPHLETLGIQEDPQDYLLLINCQSKKPEPTRTHADSAKSTSSETDCNDNVPSHKNPASSQSKHGMNGFFQQQMIYDSPPSRAPSASVDSSLYNLPRSYSHDVLPKVSPSSTEADGELYVFNTPSGTSSVETQMRHVSISYDIPPTPGNTYQIPRTFPEGTLGQTSKLDTIPDIPPPRPPKPHPAHDRSPVETCSIPRTASDTDSSYCIPTAGMSPSRSNTISTVDLNKLRKDASSQDCYDIPRAFPSDRSSSLEGFHNHFKVKNVLTVGSVSSEELDENYVPMNPNSPPRQHSSSFTEPIQEANYVPMTPGTFDFSSFGMQVPPPAHMGFRSSPKTPPRRPVPVADCEPPPVDRNLKPDRKVKPAPLEIKPLPEWEELQAPVRSPITRSFARDSSRFPMSPRPDSVHSTTSSSDSHDSEENYVPMNPNLSSEDPNLFGSNSLDGGSSPMIKPKGDKQVEYLDLDLDSGKSTPPRKQKSSGSGSSVADERVDYVVVDQQKTLALKSTREAWTDGRQSTESETPAKSVK
Protein: Subtilisin-like protease 3 (EC 3.4.21.-) (Subtilisin-like protease III) (P25036)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine protease with unknown substrate.
Interaction partners:
- Cerevisin
- Uncharacterized protein YHR202W
Sequence:
MKFSTILPILWANCCLCMIIPDFDGIVRFIENIDGTRSVRAGEGLGQHDPGNFHTEHQHVAHKTEFLPYRYVIVFNEDISLQQIQSHMQVVQKDHSTSVGKLTENDAFWRVISSSVSSKSQFGGIDNFFDINGLFRGYTGYFTDEIIKIISQDPIIKFVEQETTVKISNSSLQEEAPWGLHRVSHREKPKYGQDLEYLYEDAAGKGVTSYVLDTGIDTEHEDFEGRAEWGAVIPANDEASDLNGHGTHCAGIIGSKHFGVAKNTKIVAVKVLRSNGEGTVSDVIKGIEYVTKEHIESSKKKNKEFKGSTANLSLGSSKSLAMEMAVNAAVDSGVHFAIAAGNEDEDACLSSPAGAEKSITVGASTFSDDRAFFSNWGTCVDVFAPGINIMSTYIGSRNATLSLSGTSMASPHVAGILSYFLSLQPAPDSEFFNDAPSPQELKEKVLKFSTQGVLGDIGDDTPNKLIYNGGGKKLDGFW
Protein: Kinesin-like protein KIF1B (Klp) (EC 5.6.1.3) (O60333)
Organism: Homo sapiens (Human)
Function: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. Isoform 2 is required for induction of neuronal apoptosis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q60575}. Note=Has a plus-end-directed microtubule motor activity and therefore associates with microtubules. {ECO:0000250|UniProtKB:Q60575}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q60575}. Note=Associates with synaptic vesicles and mediates their anterograde transport along axonal microtubules. {ECO:0000250|UniProtKB:Q60575}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion {ECO:0000269|PubMed:16225668}. Note=Associates with mitochondria and mediates their movement along microtubules. {ECO:0000250|UniProtKB:Q60575}.
Interaction partners:
- KIF-binding protein
- Transmembrane protein 127
- Kinesin-like protein KIF1C
- Kinesin-like protein KIF1A
- Mitofusin-2
- Kinesin light chain 2
- Kinesin light chain 1
- Kinesin-like protein KIF13B
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- mRNA cap guanine-N
Sequence:
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKHDNETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLIDDYSGSGSKYLKDFQNNKHRYLLASENQRPGHFSTASMGSLTSSPSSCSLSSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERSNSGEVIVTLEPCERSETYVNGKRVSQPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKKEKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPLPPELLPTEMEKTHEDRPFPRTVVAVEVQDLKNGATHYWSLEKLKQRLDLMREMYDRAGEMASSAQDESETTVTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDEMEDFDDEAFVDDAGSDAGTEEGSDLFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSVAMTRSGLSLEELRIVEGQGQSSEVITPPEEISRINDLDLKSSTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLAFYHVQNIAVEITESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPCRRFFPPPMPLSKPVPATKLNTMSKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKYLKSSHNSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRSLFGSGYSKSPDSNRVTGIYELSLCKMSDTGSPGMQRRRRKILDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSLSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSGDIESLVDREKELATKCLQLLTHTFNREFSQVHGSVSDCKLSDISPIGRDPSESSFSSATLTPSSTCPSLVDSRSNSLDQKTPEANSRASSPCPEFEQFQIVPAVETPYLARAGKNEFLNLVPDIEEIRPSSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQSKY
Protein: Two-component-system connector protein SafA (Regulatory protein b1500) (Sensor associating factor A) (P76136)
Organism: Escherichia coli (strain K12)
Function: Connects the signal transduction between the two-component systems EvgS/EvgA and PhoQ/PhoP, by directly interacting with PhoQ and thus activating the PhoQ/PhoP system, in response to acid stress conditions.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17998538}; Single-pass type II membrane protein {ECO:0000269|PubMed:17998538}.
Interaction partners:
- Sensor protein PhoQ
- HTH-type transcriptional regulator YdeO
- DNA-binding transcriptional activator EvgA
- Sensor protein EvgS
- Transcriptional regulatory protein PhoP
- PhoP/PhoQ regulator MgrB
- Anti-adapter protein IraM
- Protein YdeP
Sequence:
MHATTVKNKITQRDNYKEIMSAIVVVLLLTLTLIAIFSAIDQLSISEMGRIARDLTHFIINSLQG
Protein: Histone deacetylase (EC 3.5.1.98) (Q7KTS4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037913}.
Interaction partners:
- Smrter, isoform G
- F-box-like/WD repeat-containing protein ebi
- Paired amphipathic helix protein Sin3a
- Protein MBD-R2
- Chromatin assembly factor 1 p55 subunit
- NuA4 complex subunit EAF3 homolog
- FI07430p
- LD41464p
- PHD finger protein 12
- histone deacetylase
Sequence:
MTDRRVSYFYNADVGNFHYGAGHPMKPQRLAVTHSLVMNYGLHKKMKIYRPYKASAQDMLRFHSDEYIAYLQQVTPQNIQCNSVAYTKYLAHFSVGEDCPVFDGLFDFCAMYTGASLEGAQKLNHNHSDICINWSGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDVHHGDGVQEAFYLTDRVMTASFHKYGNYFFPGTGDMYEIGAESGRYYSVNVPLKEGIDDQSYFQVFKPIISAIMDFYRPTAIVLQCGADSLAGDRLGCFSLSTKGHGECVKFVKELNVPTLVVGGGGYTLRNVARCWTHETSLLVDQDIENDLPATEYYDFFAPDFTLHPEINSRQDNANSKQYLELIVKHVYENLKMCQHSPSVQMVQTPPDVDLEELRSNREEASDPDVRISVADEDKLVDAKNEFYDGDQDQDKPDSAES
Protein: Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12] (P55213)
Organism: Rattus norvegicus (Rat)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P42574}.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Caspase-9
- Caspase-8
- Apoptotic protease-activating factor 1
- Poly [ADP-ribose] polymerase 1
- Cytochrome c, somatic
- Actin, cytoplasmic 1
- FAS-associated death domain protein
- RING-type E3 ubiquitin transferase
- Mitogen-activated protein kinase 3
Sequence:
MDNNETSVDSKSINNFETKTIHGSKSMDSGIYLDSSYKMDYPEMGLCIIINNKNFHKSTGMSARNGTDVDAANLRETFMALKYEVRNKNDLTREEIMELMDSVSKEDHSKRSSFVCVILSHGDEGVIFGTNGPVDLKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTDDDMACQKIPVEADFLYAYSTAPGYYSWRNSRDGSWFIQSLCAMLKLYAHKLEFMHILTRVNRKVATEFESFSLDATFHAKKQIPCIVSMLTKELYFYH
Protein: Four and a half LIM domains 1 (A0A0D9SGB2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGT