wanglab/gogpt-training-data huggingface dataset:
Protein: Testis-specific serine/threonine-protein kinase 1 (TSK-1) (TSK1) (TSSK-1) (Testis-specific kinase 1) (EC 2.7.11.1) (Serine/threonine-protein kinase 22A) (Q9BXA7)
Organism: Homo sapiens (Human)
Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-288' of TSKS. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250}. Note=In spermatozoa, present in the sperm head and in the flagellum. {ECO:0000250}.
Interaction partners:
- Testis-specific serine kinase substrate
- Fibrillin-1
- Sorting nexin-24
Sequence:
MDDAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQPQAQPETKPEGTAMQMSRQSEILGFPSKPSTMETEEGPPQQPPETRAQ
Protein: Telomerase reverse transcriptase (EC 2.7.7.49) (Telomerase catalytic subunit) (Q383R0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU365061}. Chromosome, telomere {ECO:0000256|RuleBase:RU365061}.
Interaction partners:
- PIH1D1/2/3 CS-like domain-containing protein
- Nucleolar protein 10
- Centromere/microtubule binding protein cbf5, putative
- Guanine nucleotide-binding protein subunit beta-like protein
- 50S ribosomal protein L7Ae, putative
- KU80 protein
- KU70 protein
- Uncharacterized protein
- H/ACA ribonucleoprotein complex subunit
- Integral membrane bound transporter domain-containing protein
Sequence:
MAQMFPSVPGYDGPFSLKDFLHNYIGLQLRWSTPQENSTTLPPSNSNVVVVPPTGNFHVVVYVSRSAPPPQRSVRSVAVLSSCSNKMDGDHPQPSVPTHFHGRPLTSSVLKHPFWDALFSQIGPTAVSFIVLWAPIVVQFEASGGGLQVLGPPLKRSASCAVKRQPGAGWWEGKLKVSRTETLTQNDPHCFCIEGTSSPVALYRLNVPRLHLVEQSPLRSTADARHAVTLILEQLWIEHHKSSCSPSSDRDISQRLCGVATGSATNCCGDSCVVLAQARNQVNAVFPYTLLPVHDDAVSGNGTVKEYLIHVLHCALGSVCRMNIRGAAIKHTEFLEKRGKSVTSISQKAQTAGQENKMRAIPVGELTVPEPVVASYLETLFNMMWWRVPPRFVGGAVTADRVKFWGEEGTVLTRLREVTVDWLCCGRHEVFLLSHFLDGVPVSRIPWLRGFYTKEPARKRRSMIQQRVFLQLVLFLYQCVVPFLIRRSFHVACTSKSPYIFFFIPRAVWVRLTRREMRRVCIRRVKRMRSDTLSDPQMRGHAGLPPMALERVTSEGLMQLIGPSSQPVGDDSGGVSDVCKLRDSSSPLLYSDVRFLVDGSKLRPIARPRFGWQRSLLKAADGVGSSTLASALAKAGKYLATDGKAMWPSPNSAVLRDALRCLDAGVEERRITTGARQRAIGSHNDEYIEVRSFIQCARQFCTIPTLVQGETSAALLADATAVTMVRGDAARCYDHLPQEAVVNIMRGLVTHETYYSLKLTVVTLTTVKNVSKKTRSSHAESQLSSMKETNGSTVKHRKLQLSKRVKLVPGRYVQEGVLYGIARGCIAYEEQSVGSDSLVSGEEIRSVLQKHLQSHLVMLNGKMYIQRMGINQGSAVAMLLCDQLLERVDAALSSILSEHEEPALLLRRVDDVLVVTLSRAAASRCEDALRSGWSEIGFFCQEEKLRRVTCGQPVRWCGLLWDPVTLEFAVDWARLAKMMPYLAVRPRTGCEPLLSSLRFIRILRLRTPMTALCRQINSKSRVVQTLYEIGLLWSRFFLDKLKANAAFFRPHVRTILQPLALATATLRRLVRKHSFDLQRLGSFCDVTDVEVRLCISAALYHTLHQRLAFMIGRMSSVGKKKFLILMTAVLKRKMGELGSRINRNNQMESSLPSAADLLLVEGGDGVVSRGLAAVRFRPVETVRFQGCATRSA
Protein: Trafficking protein particle complex subunit 9 (A0A8I6GM01)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSVPDYMQCAEDHQTLLVVVQAVGIVSEENFFRIYKRICSVSQLSVRDSQRALFIRYRHHYPPENNEWGDFQTHRKVVGLITITDCFSPKDWPQTFEKFHVQKEIYGSTLYDSRLFVFGLQGDVAEQPRPDVAFYPNYDDCDSVEKRIEDFIESLFIVLESKRLDRATDKSGDKIPLLCVPFEKKDFVGLDTDSRHYKKRCQGRMRKHVGDLCLQAGMLQDALVHYHMSVELLRSVNDFLWLGAALEGLCSASVIYHYPGGTGGKTGARRLPGNSLPSEAANRHRPGALTTNGINPDTSTEIGRAKNCLSPEDIIDKYKEAISYYSKYKNAGVIELEACVKAVRVLAIQKRGMEASEFLQNAVYINLRQLSEEEKIQRYSILSELYELIGFHRKSAFFKRVAAMQCVAPSIAEPGWRACYKLLLETLPGYSLSLDPKDFNKGTHDDLGLGWRLLYFHLACHGFHRTSDVPRSMGFVPTFYFVSSSEKKDVTQSLENYTAKCPGTMEPITLPDGLTLPPVPFTKLPIVRCVKLLSLPTSLRPQKVKSLLGQSMSTKSPFIYSPIIAHNRGEERNKKIDFQWVQGDVCEVQLMVYNPMPFELRVENMGLLTSGVEFESLPAALSLPAESGLYPVTLVGVPQTTGMITVNGYHTTVFGVFSDCLLDNLPGLKTSGSTVEVIPALPRLQISTSLPRSAHSLQPSAGDEIATNVSVQLFNGETQQLAITLENIGLEPLEQLEVTSKLLTTKEKLYGDFLSWKLEETLAQFPLQPGKVATFTINIKAKLDFSCQENLLQDLSDDGISVSGFPLSSPFRQVVRPRVESRPTNPSEGSKTGDLGHVKVSPSVEVQAARVGSPGFCWSTFQLAFGVPF
Protein: Cyclin-dependent protein kinase complex component, putative (AFU_orthologue AFUA_2G07660) (C8V078)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Cyclin dependent kinase inhibitor Pho81, putative
Sequence:
MNSGVGEGEGEPSLDATNAQQVLGLLPLPKEVKYDPNFHRPHISAIRPENAMELLCIAVDMLLAMSTTRALSGDASESGVRNEVSSGENTPTRVEELRFHPHGHDLTQQSLLCKRFLSKREPPITLKEYLTRFHHYCPLSTGVYIAASLYITRIAVVDSVISVNRKNMHRLVLAGLRVAMKTVEDLVYPHSRVAKVGGVTERELTRLEISFCFLADFDLRVDEQTLDNQAGILHWYMEHPT
Protein: Protein SAMBA (Q9C613)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in organ size control. Acts as negative regulator of the anaphase-promoting complex/cyclosome (APC/C). Regulates cell proliferation during early development by targeting CYCA2-3 for APC/C-mediated degradation. Required for mitosis I during pollen microspore development.
Interaction partners:
- Anaphase-promoting complex subunit 10
- Cell division cycle protein 27 homolog B
- Cell division cycle protein 27 homolog A
- Anaphase-promoting complex subunit 13
- Protein POLYCHOME
- AAA-type ATPase family protein
- At4g28230
- Nuclear pore complex protein NUP50B
- KIN14B-interacting protein At4g14310
- Cyclin-dependent protein kinase inhibitor SMR6
Sequence:
MNGASPAHSLVSTTAVAGGGGSSGAAAGLDDFHFPPDIPSMQERKDEAMRVLKADLMTELDKEVKSLEEDSWMFEGPRSRIHLISRRGNFLKKGGEVKLW
Protein: E3 ubiquitin-protein ligase HERC1 (Q8BNF7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MATMVPPVKLKWLEHLNSSWITEDSESIATREGVTVLYSKLISNKEVVPLPQQVLCLKGPQLPDFERESLSSDEQDHYLDALLSSQLALAKMVCSDSPFAGAIRKRLLVLQRVFYALSNKYHDKGKVKQQQHSPESSSGSADVHSVSERPRSSTDALIEMGVRTGLSLLFALLRQSWMMPVSGPGLSLCNDVIHTAIEVVSSLPPLSLANESKIPPMGLDCLSQVTTFLKGVTIPNSGADTLGRRLASELLLGLPAQRGSLRYLLEWIEMALGASPVVYTMEKNKLLSSQEGMISFDCFMAILMQMRRSLGSSADRSQWREPTRTSEGLCSLYEAALCLFEEVCRMASDYSRTCASPDSIQTGDAPIVSETCEVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVISTDGSVRACGKGSYGRLGLGDSNNQSTLKKLTFEPHRSIKKVSSSKGSDGHTLAFTTEGEVFSWGDGDYGKLGHGNSSTQKYPKLIQGPLQGKVVVCVSAGYRHSAAVTEDGELYTWGEGDFGRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGRTVWSFGGGDNGKLGHGDTNRVYKPKVIEALQGMFIRKVCAGSQSSLALTSTGQVYAWGCGACLGCGSSEATALRPKLIEELAATRIVDISIGDSHCLSLSHDNEVYAWGNNSMGQCGQGNSTGPITKPKKVSGLDGIAIQQISAGTSHSLAWTALPRDRQVVAWHRPYCVDLEESTFSHLRSFLERYCDKINSEIPPLPFPSSREHHNFLKLCLKLLSNHLALALAGGVATSILGRQAGPLRNLLFRLMDSTVPDEIQEVVIETLSVGATMLLPPLRERMELLHSLLPQGPDRWESLSKGQRMQLDIILTSLQDHTHVASLLGYSSPSDAADLSTVCMGYGNLSDQPYGSQICHPDTHLAEILMKTLLRNLGFYTDQAFGELEKNSDKYLLGTSSSENSQPAHLHELLCSLQKQLLAFCHINNVTENSSSVALLHKHLQLLLPHATDIYSRSANLLKESPWNGSVGEKLRDVIYVSAAGSMLCQIVNSLLLLPVSVARPLLSYLLDLLPPLDCLNRLLPAAALLEDQELQWPLHGGPEVIDPAGVPLPQPAQSWVWLVDLERTIALLIGRCLGGMLQGSPVSPEEQDTAYWMKTPLFSDGVEMDTPQLDKCMSCLLEVALSG
Protein: Tropomodulin, isoform C (Tropomodulin, isoform J) (Q9VA58)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MADTAKDKDVIDQEDVEVEEQEETTTTTTTTKKTSQWHKTRTTKTSATTKTTTLTTPAKLYGKDLSEYDDVDVESLLAQLSPEEITILAKEVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQPEFEPFVQGKVRGKKWVPPPRDARDIEAEEQIAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQDQYHASLLNKGQPVGLGWDGITKSTQQKLFPMDPPNNTDVEESIKRVKDDDSKLIDLNLNNIKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFRASNQRSAVLGNKIEMEITDLVEKNSSLLRLGLHLEFNDARHRVAAHLQRNIDRIRVKRLNQRK
Protein: Alpha-tocopherol transfer protein (Alpha-TTP) (P49638)
Organism: Homo sapiens (Human)
Function: Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7887897}.
Interaction partners:
- Caytaxin
- Protein prune homolog 2
- Sodium- and chloride-dependent GABA transporter 3
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 2
- Frataxin, mitochondrial
Sequence:
MAEARSQPSAGPQLNALPDHSPLLQPGLAALRRRAREAGVPLAPLPLTDSFLLRFLRARDFDLDLAWRLLKNYYKWRAECPEISADLHPRSIIGLLKAGYHGVLRSRDPTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIFDLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSMEDICQEWTNFIMKSEDYLSSISESIQ
Protein: Sorting nexin-21 (Sorting nexin L) (SNX-L) (Q969T3)
Organism: Homo sapiens (Human)
Function: Binds to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate. May be involved in several stages of intracellular trafficking.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q3UR97}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane {ECO:0000250|UniProtKB:Q3UR97}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q3UR97}; Cytoplasmic side {ECO:0000250|UniProtKB:Q3UR97}.
Interaction partners:
Sequence:
MHRGTQEGAMASRLLHRLRHALAGDGPGEAAASPEAEQFPESSELEDDDAEGLSSRLSGTLSFTSAEDDEDDEDEDDEEAGPDQLPLGDGTSGEDAERSPPPDGQWGSQLLARQLQDFWKKSRNTLAPQRLLFEVTSANVVKDPPSKYVLYTLAVIGPGPPDCQPAQISRRYSDFERLHRNLQRQFRGPMAAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLPELRRAQSLTCTGLYREALALWANAWQLQAQLGTPSGPDRPLLTLAGLAVCHQELEDPGEARACCEKALQLLGDKSLHPLLAPFLEAHVRLSWRLGLDKRQSEARLQALQEAGLTPTPPPSLKELLIKEVLD
Protein: Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (JV18-1) (Mad-related protein 2) (hMAD-2) (SMAD family member 2) (SMAD 2) (Smad2) (hSMAD2) (Q15796)
Organism: Homo sapiens (Human)
Function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:9865696}. Nucleus {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:21599657, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:9865696}. Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 or with IPO7 (PubMed:21145499, PubMed:9865696). On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (PubMed:16751101, PubMed:19289081). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm at the blastocyst and epiblast stages (By similarity). {ECO:0000250|UniProtKB:Q62432, ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:19289081, ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:9865696}.
Interaction partners:
- Forkhead box protein H1
- Ski-like protein
- E3 ubiquitin-protein ligase TRIM33
- Mothers against decapentaplegic homolog 3
- Zinc finger FYVE domain-containing protein 9
- Mothers against decapentaplegic homolog 4
- TGF-beta receptor type-1
- E3 ubiquitin-protein ligase SMURF2
- Catenin beta-1
- TGF-beta receptor type-2
Sequence:
MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
Protein: Polyprenal reductase (EC 1.3.1.22) (EC 1.3.1.94) (H0ZB17)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367081}.
Interaction partners:
- dolichol kinase
- 3-oxo-5-alpha-steroid 4-dehydrogenase
- 3-oxo-5-alpha-steroid 4-dehydrogenase
- Aromatase
- Hydroxysteroid 17-beta dehydrogenase 2
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Aldo-keto reductase family 1 member D1
- Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
- GDT1 family protein
Sequence:
MLAALAAAWALLAAAFLAALLLLRRAPAPQPAGFGLVISGLFQDLIRYGKTKRGCGQLPGWLRLLQVPKRWFTHFYVVSVLWNGFLLICLFRAEFLGESFPSWIQDMHHALGRDSQNKDMDSEHFSALLVLLLLWLHSCRRLAECLWISVFSSGVIHIVQYCFGLGYYIAVGSTVLCQVPTNVRNGKKLSVQICWYHVIGVTMYIWASLHQHRCLAILANLRKSRTGKVVSVSHSVPFGDWFESVSCPHYFAELLIYVSMAITLGIHNVTWWCVVMYVLSNQALAAVLCHEFYQKNFSSYPKHRKAFIPLVF
Protein: Protein NDRG1 (Differentiation-related gene 1 protein) (DRG-1) (N-myc downstream-regulated gene 1 protein) (Nickel-specific induction protein Cap43) (Reducing agents and tunicamycin-responsive protein) (RTP) (Rit42) (Q92597)
Organism: Homo sapiens (Human)
Function: Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy.
Subcellular location: Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cell membrane. Note=Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactating mammary gland. Translocated to the nucleus in a p53/TP53-dependent manner. In prostate epithelium and placental chorion, located in both the cytoplasm and in the nucleus. No nuclear localization in colon epithelium cells. In intestinal mucosa, prostate and renal cortex, located predominantly adjacent to adherens junctions. Cytoplasmic with granular staining in proximal tubular cells of the kidney and salivary gland ducts. Recruits to the membrane of recycling/sorting and late endosomes via binding to phosphatidylinositol 4-phosphate. Associates with microtubules. Colocalizes with TUBG1 in the centrosome. Cytoplasmic location increased with hypoxia. Phosphorylated form found associated with centromeres during S-phase of mitosis and with the plasma membrane.
Interaction partners:
- N-myc proto-oncogene protein
- Serine/threonine-protein kinase 38-like
- Cellular tumor antigen p53
- CCN family member 4
- Protein NDRG2
- Serine/threonine-protein kinase Sgk1
- Myc proto-oncogene protein
- Large neutral amino acids transporter small subunit 1
- Heat shock protein HSP 90-alpha
- Cadherin-1
Sequence:
MSREMQDVDLAEVKPLVEKGETITGLLQEFDVQEQDIETLHGSVHVTLCGTPKGNRPVILTYHDIGMNHKTCYNPLFNYEDMQEITQHFAVCHVDAPGQQDGAASFPAGYMYPSMDQLAEMLPGVLQQFGLKSIIGMGTGAGAYILTRFALNNPEMVEGLVLINVNPCAEGWMDWAASKISGWTQALPDMVVSHLFGKEEMQSNVEVVHTYRQHIVNDMNPGNLHLFINAYNSRRDLEIERPMPGTHTVTLQCPALLVVGDSSPAVDAVVECNSKLDPTKTTLLKMADCGGLPQISQPAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLDGTRSRSHTSEGTRSRSHTSEGTRSRSHTSEGAHLDITPNSGAAGNSAGPKSMEVSC
Protein: Taste receptor type 2 member 114 (T2R114) (Taste receptor type 2 member 5) (T2R5) (Q9JKT8)
Organism: Rattus norvegicus (Rat)
Function: Putative taste receptor which may play a role in the perception of bitterness.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Olfactory receptor
- Olfactory receptor.
- Olfactory receptor.
Sequence:
MLGAMEGVLLSVATSEALLGIVGNTFIALVNCMDCTRNKNLYNIGFILTGLAISRICLVWILITEAYIKIFSPQLLSPINIIELISYLWIITSQLNVWFATSLSIFYFLKIANFSHHIFLWLKRRINIVFAFLIGCLLMSWLFSFPVVVKMVKDKKMLYINSSWQIHMKKSELIINYVFTNGGVFLLFIIMLIVCFLLIISLWRHSKWMQSNESGFRDLNTEVHVKTIKVLLSFIILFILHLIGITINVICLLVPENNLLFVFGLTIAFLYPCCHSLILILANSRLKRCFVRILQQLMCSEEGKEFRNT
Protein: Neuropeptide CCHamide-2 (Q8SXL2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ligand for the CCHamide-2 receptor CCHa2-R. In one study, shown to be an orexigenic peptide which induces appetite and stimulates food intake, leading to the release of insulin-like peptides which stimulate growth. In another study, shown to be a nutrient-sensitive peptide derived from peripheral tissues which controls growth by directly regulating the production and release of insulin-like peptides.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Neuropeptide CCHamide-2 receptor
- Neuropeptide CCHamide-1
- GEO12066p1
Sequence:
MKSTISLLLVVICTVVLAAQQSQAKKGCQAYGHVCYGGHGKRSLSPGSGSGTGVGGGMGEAASGGQEPDYVRPNGLLPMMAPNEQVPLEGDFNDYPARQVLYKIMKSWFNRPRRPASRLGELDYPLANSAELNGVN
Protein: Lysophospholipase D GDPD3 (EC 3.1.4.-) (Glycerophosphodiester phosphodiesterase 7) (Glycerophosphodiester phosphodiesterase domain-containing protein 3) (Q99LY2)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylcholine (lyso-PC) and N-acylethanolamine lysophospholipids. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25528375}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25528375}; Multi-pass membrane protein {ECO:0000305}. Note=Partially colocalized with CANX (PubMed:25528375). {ECO:0000269|PubMed:25528375}.
Interaction partners:
- Glycerophosphocholine cholinephosphodiesterase ENPP6
- Autotaxin
- Lysophospholipase D GDPD1
- Lysophospholipid acyltransferase LPCAT4
- Lysoplasmalogenase TMEM86B
- Cytosolic phospholipase A2
- Lysophosphatidic acid receptor 1
- Phospholipase A2 group V
- Cytosolic phospholipase A2 zeta
- Cytosolic phospholipase A2 beta
Sequence:
MIPLLYFVLPTLGSYVMLSIFFLRRPHLLHTPRAPVFPIRLAAHRGGSGERLENTMEAVENSMAQRADLLEFDCQLTRDGVVVVSHDKNLSRQSGLNKDVNTLDFEELPLYKEELEIYFSPGHFAHGSDRHMISLEDVFQKFPRTPMCLEVKERNEELIHKVANLTRRFDRNEITIWAAEKSSVMKRCRAANPEMPMAFTIWRSFWILLLYYLGLLPFVSIPEKFFFCFLPTIINRTYFPFRCGWMNQLSATITKWIIMRKSLIRHLQDRGVQVLFWCLNEESDFEVAFSLGANGVMTDYPTALRHYLDKQEEETQPPQPEALSCLSLKK
Protein: CAP, isoform D (A1Z872)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIHQTLAPHRSKSSSYSKSKAVHWRQKLHSSCNDLELEDEPFPEPQGMWHSQEINENPWQRPQSSGADGSSNNNVCDIPNCGKILWIHRREYDYNRSAPLRPPSPSNYHGVPSAVGYHVVGLPLTPQPNQRQAYLANQHAIGATMPLLLWQQQQQLLQQQRQHQQNLQQLQHRKYQNMQHRWPSNVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Alpha-galactosidase 3 (EC 3.2.1.22) (Alpha-D-galactoside galactohydrolase 3) (Melibiase 3) (Q92451)
Organism: Hypocrea jecorina (Trichoderma reesei)
Function: Alpha-galactosidase involved in the degradation of simple oligosaccharides like melibiose, raffinose and stachyose, and of polymeric galacto(gluco)mannans.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MSPSAAVLIPLAAAVLLRPVVGQTQCGGNLYTPGTLNFTLECYNAFQDCVAQFEANASQVDCNDGKGNLFMQQQANLGASPGSQNNDAIIAFQDIRDLCLLSGSTTATWGYSDNQWYWAAAEDACYTNDPTRTDVVKTHPAPFCIQNRDSSLPECYPQPDATPPGGPLKVIKTAKTRNGFKSSARGWNTYGVQALVNGSQVVPSFAGQSGLFYTQKFVETQCGVLARPEFKKAGYDLCSLDSGWQATTAVDQHGRIIYNTTRFNLPELASWLHKRDLKLGVYITPGVPCLAHNQTILGTNIKIKDVLNGNNDQINCDFDFRKDGVQQWHDSVVAQWASWGVDMLKLDFLTPGSPSNGANLACDSSDAVRAYQKAIKKSGRKIRLDISWKLCRNETWLPIWSDLAESMRTDQDLDNYGTNTLMAWQVGQRAIENYRQYIGLQAQRNVPLTIYPDMDALFTVNPEHLAGVNDTIRYTVQNHWLGAGANLIIGGDMEQVDALGLKLTTSKQSIDAADFFAKYPMQPRNPGTGSNAAKQLQAWIGGPSDDHEAYVLIVNYGPDLGNGGFSTKLYGKQKVTVSLKDLGISGSAWTFTDIWSGKSSRVTGSYSAWLTEGESQLLRLKRTH
Protein: 40S ribosomal protein S8 (Q5JR94)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGISRDNWHKRRKTGGKRKPYHKKRKYELGRPAANTKIGPRRIHTVRVRGGNKKYRALRLDVGNFSWGSECCTRKTRIIDVVYNASNNELVRTKTLVKNCIVLIDSTPYRQWYESHYALPLGRKKGAKLTPEEEEILNKKRSKKIQKKYDERKKNAKISSLLEEQFQQGKLLACIASRPGQCGRADGYVLEGKELEFYLRKIKARKGK
Protein: Inhibitor of nuclear factor kappa-B kinase epsilon subunit homolog 1 (EC 2.7.11.1) (P32742)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase, which plays a role in regulating allophagy, an autophagic process in which paternal organelles, including mitochondria and membranous organelles, are degraded in embryos. Phosphorylates the allophagy receptor allo-1, which is required for allophagy.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29255173}. Note=Localizes to cytoplasmic puncta in oocytes. After fertilization, localizes to paternal organelles during meiosis I and meiosis II. Co-localizes with allo-1 in embryos and oocytes. {ECO:0000269|PubMed:29255173}.
Interaction partners:
- Allophagy receptor allo-1
- ANK repeat-containing protein nipk-1
Sequence:
MAVSPHKTYPIVITHGEKYTLFNDESIGKGAYSEVYRGRTESGRLVAVKTACKKLEVAAIGIEIEILKKLKGASNIVQYFGSNHTKMAPGSVTSETISFAMEYASSSLEAEMRRPKNHRGLSSNALIDLVVDCSMALSALREHNIAHRDIKHMNILLFPGTPTRGRRSTHLFKLCDMGCSKSLSENSSHEMRTLVGTPNLLHPFLAHEMVDPLMAQNRHNWKTKSAYTSEQCDLWALGCTLYFCATGKFPFEHERNNKSLYHKAVVALTQNPDAIAMVLVQKGRDPGRRTDIFEFQPVTELPAKFTRYPKWLVSTMTCLLRSFFHEPSIEYYAKVADAMRNSKRRTFSSVDQMSIVEHTDMSNVPHLGFSIPSISKCLGYPEGTDILLLSNTSTHYLDSKQKSVDGLPDDLYLVVPQTSHVDMRKILARNIEFHEFDDMTDRKLSEIRIKKCYEGLSMLTEIDEYLALFDRVSTILSTQFSLLVQELSQFERVQTASRFAVYVDMASVPLMLFDEANPETKMISDQCIQQAKRAREELERHAKVSMDIEACAKQLSKDAEDLRLEDMDLPGICEEIESYVFYDKQAILSTQKYSQELVELCLKRRNNIMEQIFNSPDRINKSKLNKAMNLAASLSQLRSNYRKLQDMISECVDLLEKPFQEMKDTVNRYLQAQGCSRNTMQKSMHLLRPEFHESQIRIKKTTKSCRKLIDQLNIELDQLGFVRLGDILIKAESEQTLTRSEEIQETQVVSFFCQAESSPNKEQFPKPEQDSILESSIDEGSTSFESTPPSSPPDVGSNNYFQAVFQYFAKPTSSPSSSAK
Protein: Endophilin-B2 (SH3 domain-containing GRB2-like protein B2) (Q5PPJ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NR46}.
Interaction partners:
- E3 ubiquitin-protein ligase CBL-B
- E3 ubiquitin-protein ligase CBL-C
- E3 ubiquitin-protein ligase CBL
- Endophilin-B1
- Caspase-3
- Trafficking protein particle complex subunit 6A
Sequence:
MDFNMKKLASDAGIFFTRAVQFTEEKFGQAEKTELDAHFENLLARADSTKNWTERILRQTEVLLQPNPSARVEEFLYEKLDRKVPSRVTNGELLAQYMAEAASELGPNTPYGKTLMKVSEAEKRLGAAERDFIHTASLSFLTPLRNFLEGDWKTISKERRLLQNRRLDLDACKARLKKAKAAEAKATCEGDTVPDFQETRPRNYILSASASALWNDEVDKAEQELRAAQTEFDRQAEVTRLLLEGISSAHVNHLRCLHEFVKSQTTYYAQCYRHMLDLQKQLGSSQGAIFPGTFVGTTEPASPPLSSTSPTTTAATMPVVPTGAGLAPPEEAALCLEEVAPPASGTRKARVLYDYEAADSSELALLADELITVYSLPGMDPDWLIGERGNKKGKVPVTYLELLS
Protein: C2H2-type domain-containing protein (Q9W1W2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVFMNGLGSDPLSAKEAEGPPVQVEPVDLSLRSPRASTSHGSSSSSYKFSSANKAVGYSNGKPGGSSGSSSSSGFGAGSAGSSSLGAFAAQQQQQLYASSGVSKLPFSPFFAASPFFFTYRRISGSGSGNGTGSVSVKQEDNNNSCSYNNGSSSGGAGSAANSMQDYESKFSLLSLFKNPYKFAGGDGQASRKTSPTGGSSKPLASNSSPSWKSYAGSGSPHAALNPAFGGMGRGATRKDNSSFSGINFGGGGSAFGFTTSSDSMANGGYNDLSKNRKVHKCDTEGCDKVYTKSSHLKAHKRTHTGEKPYVCTWEGCIWRFARSDELTRHYRKHTGVKPFRCQLCTRSFSRSDHLSLHMRRH