wanglab/gogpt-training-data huggingface dataset:
Protein: CD48 antigen (BCM1 surface antigen) (BLAST-1) (HM48-1) (MRC OX-45 surface antigen) (SLAM family member 2) (SLAMF2) (Signaling lymphocytic activation molecule 2) (sgp-60) (CD antigen CD48) (P18181)
Organism: Mus musculus (Mouse)
Function: Glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that interacts via its N-terminal immunoglobulin domain with cell surface receptors including 2B4/CD244 or CD2 to regulate immune cell function and activation. Participates in T-cell signaling transduction by associating with CD2 and efficiently bringing the Src family protein kinase LCK and LAT to the TCR/CD3 complex. In turn, promotes LCK phosphorylation and subsequent activation. Induces the phosphorylation of the cytoplasmic immunoreceptortyrosine switch motifs (ITSMs) of CD244 initiating a series of signaling events that leads to the generation of the immunological synapse and the directed release of cytolytic granules containing perforin and granzymes by T-lymphocytes and NK-cells (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1383383}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1693656}. Membrane raft {ECO:0000250|UniProtKB:P09326}. Secreted {ECO:0000250|UniProtKB:P09326}.
Interaction partners:
- Natural killer cell receptor 2B4
- Proto-oncogene tyrosine-protein kinase LCK
- Receptor-type tyrosine-protein phosphatase C
- CAMPATH-1 antigen
- SLAM family member 6
- Leukocyte surface antigen CD53
- Killer cell lectin-like receptor subfamily B member 1C
- Mast/stem cell growth factor receptor Kit
- Interleukin-7 receptor subunit alpha
- CD226 antigen
Sequence:
MCFIKQGWCLVLELLLLPLGTGFQGHSIPDINATTGSNVTLKIHKDPLGPYKRITWLHTKNQKILEYNYNSTKTIFESEFKGRVYLEENNGALHISNVRKEDKGTYYMRVLRETENELKITLEVFDPVPKPSIEINKTEASTDSCHLRLSCEVKDQHVDYTWYESSGPFPKKSPGYVLDLIVTPQNKSTFYTCQVSNPVSSKNDTVYFTLPCDLARSSGVCWTATWLVVTTLIIHRILLT
Protein: Zinc finger protein ZAT8 (Q9LX85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may be involved in stress responses.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- C2H2 and C2HC zinc fingers superfamily protein
- C2H2-type zinc finger family protein
- Ac-like transposase
- HAT family dimerization domain-containing protein
- Small polypeptide DEVIL 23
Sequence:
MVARSEEVEIVEDTAAKCLMLLSRVGECGGGGEKRVFRCKTCLKEFSSFQALGGHRASHKKLINSSDPSLLGSLSNKKTKTATSHPCPICGVEFPMGQALGGHMRRHRSEKASPGTLVTRSFLPETTTVTTLKKSSSGKRVACLDLDSMESLVNWKLELGRTIS
Protein: Protein transport protein Sec24A (C0H5J6)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}.
Interaction partners:
- Protein transport protein SEC23
- Protein transport protein SEC13
- Protein transport protein SEC31
- Protein transport protein Sec24B, putative
- Protein transport protein SEC22
- Small GTP-binding protein sar1
Sequence:
MQPYDYNRGLNNNNTANYNNQNNANAPINNPFLHNNDIGNNNNMKTNEGPYNAPTYYNPGQHQQQQQQQQQQGPPLHQGYQHSGVYGMNQGNYKTNNIGENMYNQDGHNNTSYINQGQPYRNVTSQFIPVSSNNTLKAGGNMLGYDNMGNINHVQPIINDTYQEFLQFNAFSHFVKSSVSYMPANTTLKQKAYVPLGFVIQPLAPIPDGYPELASVNFGNSTVVRCKKCRTYINPFVRFEAGGKKWNCNMCYNINDTPQFYFVPLDEKGKRKDLFQRPELCTGSVEFIAPSDYMIRPPQPSVYLFLIDVTVTSVNSGLLDVVCSTIKSLLPKNNDSTENNNQNDNNNNNNNNNSKNLKSFDSRTLIGIMTFDSTIHFYNLNSNLKQTQMMVVPDIQDIFIPLPEDILVNVHECQNVIDVLLDNLPGMWRNNKISDCCAGNALKAAFMVLKKVGGKLLFFLSSVPNIGDLTVSVNRDNKDKSKYKNIYSSSSSGNNVVDSKLREVELLNPCNNLYAELAQNITQYQIAVDLFACPLYNLDLASIYPLIKNSGGSLYYYPQFNVHQYNDKLRQELLFALTTETAWESVMRIRISRGWKITNWYGNYQFRGADLLALPNCHSGQNFSIIVDLEENVVQDSIVYVQSALLYTNSNGERRIRLHTYALPITQNIKTITDSINPQVVVSLLAHQSIDISKKGKIADGRNLIQNLCSQVLSSQLLQSECARLLSLYILGMLKSIAFRDSGDVPPDLRIYHWYRLENIPVESVEANFYPRMFSLHNLEKHHGHLDENNNIVFPDALNLTCENMTQDGCYIVEDGETIVMWIGRSINPQWIYAVFGVQTIDQLNTEYAENHLGSTGNPFGVQILNIINALRKIRTPCYMKLLVVKQGDPLEYKFFSYLIEDRSQHMMLSLKEFLAKICPKFPQFTPSMTTNPLATQHGR
Protein: ERO1-like protein alpha (ERO1-L) (ERO1-L-alpha) (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase alpha) (Endoplasmic reticulum oxidoreductin-1-like protein) (Global ischemia-induced protein 11) (Oxidoreductin-1-L-alpha) (Q8R4A1)
Organism: Rattus norvegicus (Rat)
Function: Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96HE7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96HE7}; Lumenal side {ECO:0000250|UniProtKB:Q96HE7}. Golgi apparatus lumen {ECO:0000250|UniProtKB:Q96HE7}. Secreted {ECO:0000250|UniProtKB:Q96HE7}. Cell projection, dendrite {ECO:0000269|PubMed:12694393}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (By similarity). In neurons, it localizes to dendrites (PubMed:12694393). {ECO:0000250|UniProtKB:Q96HE7, ECO:0000269|PubMed:12694393}.
Interaction partners:
- Protein disulfide-isomerase A4
- Protein disulfide-isomerase
- Protein disulfide-isomerase A6
- Thioredoxin domain-containing protein 5
- Endoplasmic reticulum resident protein 29
- Endoplasmic reticulum protein 44.
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A3
- Glutathione peroxidase
- Glutathione peroxidase
Sequence:
MGRGWGLLVGLLGVVWLLRSGQGEEQQQETAAQRCFCQVSGYLDDCTCDVETIDKFNNYRLFPRLQKLLESDYFRYYKVNLRKPCPFWNDINQCGRRDCAVKPCHSDEVPDGIKSASYKYSKEANLLEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDSFCEVDDIQSPDAEYVDLLLNPERYTGYKGPDAWRIWSVIYEENCFKPQTIQRPLASGQGKHKENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQDNWLEKKWGHNVTEFQQRFDGVLTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKVQDVENKELLLEILHEVKSFPLHFDENSFFAGDKNEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFQLTRQEIVSLFNAFGRISTSVRELENFRHLLQNVH
Protein: Cleavage and polyadenylation specificity factor subunit 4 (Cleavage and polyadenylation specificity factor 30 kDa subunit) (CPSF 30 kDa subunit) (O19137)
Organism: Bos taurus (Bovine)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MQEIIASVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEFFLKAACGKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVNYLVGFCPEGPSCKFMHPRFELPMGTTEQPPLPQQTQPPTKRTPQVIGVMQSQNSSAGSRGPRPLEQVTCYKCGEKGHYANRCTKGHLAFLSGQ
Protein: Aldo-keto reductase family 1 member B1 (EC 1.1.1.21) (EC 1.1.1.300) (EC 1.1.1.372) (EC 1.1.1.54) (Aldehyde reductase) (Aldose reductase) (AR) (P15121)
Organism: Homo sapiens (Human)
Function: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal. Catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides. Plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls).
Subcellular location: Cytoplasm.
Interaction partners:
- Sorbitol dehydrogenase
- Carbonyl reductase 1])
- Sepiapterin reductase
- Dihydrofolate reductase
- Dihydrofolate reductase 2, mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- L-xylulose reductase
- Aldehyde dehydrogenase, mitochondrial
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
Sequence:
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF
Protein: UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2 (Beta-1,3-GalNAc-T2) (EC 2.4.1.313) (Beta-1,3-N-acetylgalactosaminyltransferase II) (Q8NCR0)
Organism: Homo sapiens (Human)
Function: Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum {ECO:0000269|PubMed:23453667}.
Interaction partners:
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannose kinase
- Dystroglycan 1
- Ribitol-5-phosphate xylosyltransferase 1
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Ribitol-5-phosphate transferase FKTN
- Beta-1,4-glucuronyltransferase 1
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Ribitol 5-phosphate transferase FKRP
Sequence:
MRNWLVLLCPCVLGAALHLWLRLRSPPPACASGAGPADQLALFPQWKSTHYDVVVGVLSARNNHELRNVIRSTWMRHLLQHPTLSQRVLVKFIIGAHGCEVPVEDREDPYSCKLLNITNPVLNQEIEAFSLSEDTSSGLPEDRVVSVSFRVLYPIVITSLGVFYDANDVGFQRNITVKLYQAEQEEALFIARFSPPSCGVQVNKLWYKPVEQFILPESFEGTIVWESQDLHGLVSRNLHKVTVNDGGGVLRVITAGEGALPHEFLEGVEGVAGGFIYTIQEGDALLHNLHSRPQRLIDHIRNLHEEDALLKEESSIYDDIVFVDVVDTYRNVPAKLLNFYRWTVETTSFNLLLKTDDDCYIDLEAVFNRIVQKNLDGPNFWWGNFRLNWAVDRTGKWQELEYPSPAYPAFACGSGYVISKDIVKWLASNSGRLKTYQGEDVSMGIWMAAIGPKRYQDSLWLCEKTCETGMLSSPQYSPWELTELWKLKERCGDPCRCQAR
Protein: Sterol 3-beta-glucosyltransferase (EC 2.4.1.-) (EC 2.4.1.173) (Autophagy-related protein 26) (UDP-glycosyltransferase 51) (Q06321)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable sterol 3-beta-glucosyltransferase that is not involved in cytoplasm to vacuole transport (Cvt), pexophagy or nonselective autophagy.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Autophagy-related protein 20
- Sorting nexin-4
- Autophagy-related protein 11
- Autophagy-related protein 9
- Autophagy-related protein 22
- Autophagy-related protein 27
- Serine/threonine-protein kinase ATG1
- RNA polymerase II subunit A C-terminal domain phosphatase
- Autophagy-related protein 19
- Putative lipase ATG15
Sequence:
MPITQIISASDSEAGPKPSISLVPDKPSEPETSPRHHRLSRSLSKFKRWRGRSNSSLSMGSSEQQELQDSPNEARSDDDENGYNNDNADDLAKSKYMMKSIAGLLTTASVYAGMNNAQEMNVLSQVDSEESDSSDSFQENIGRNEVKSKKENLKTKSHPEVPRLDKRKPTLFDFSITREKLSKDNVAKLRQRFCLDEQEPFLNDFPAWLLKDVLVQGHIFITTKHFLFFAYLPKNPRSVKMSGNLNIRTKLIRSTRYWCVLKNHLFSMYTSSTELYFPVLTIDLREVQKIETQKHTLNGSATKTFKLYTDESTFKFNADSEFSAKSWVNALKKEQFAAQNSENNSISLKIPLPNIIEIDDQPIVNKALTLRLRALESSQTYAIDDFMFVFMDGSGSQVKESLGEQLAILQKSGVNTLYYDIPAKKSKSSFGKETPATVEQKNNGEDSKYLNVPTSAVPSSENGKKSRFRFRERSNSWFRRAKPLEDSQVEDVEEIYKDAANDIDSSVHSTIHIHEQEDSQEQTVAWKPSHLKNFAEMWAAKPIHYRNKFIPFQKDDTYLIKETEEVSANERFRYHFKFNKEKSLISTYYTYLNRNVPVYGKIYVSNDTVCFRSLLPGSNTYMVLPLVDVETCYKEKGFRFGYFVLVIVIHGHEELFFEFSTEVARDDIERILLKLLDNIYASSAEGSNISSASLGDVQHNPDSAKLKLFEDKINAEGFEVPLMIDENPHYKTSIKPNKSYKFGLLTIGSRGDVQPYIALGKGLIKEGHQVVIITHSEFRDFVESHGIQFEEIAGNPVELMSLMVENESMNVKMLREASSKFRGWIDALLQTSWEVCNRRKFDILIESPSAMVGIHITEALQIPYFRAFTMPWTRTRAYPHAFIVPDQKRGGNYNYLTHVLFENVFWKGISGQVNKWRVETLGLGKTNLFLLQQNNVPFLYNVSPTIFPPSIDFSEWVRVTGYWFLDDKSTFKPPAELQEFISEARSKGKKLVYIGFGSIVVSNAKEMTEALVEAVMEADVYCILNKGWSERLGDKAAKKTEVDLPRNILNIGNVPHDWLFPQVDAAVHHGGSGTTGASLRAGLPTVIKPFFGDQFFYAGRVEDIGVGIALKKLNAQTLADALKVATTNKIMKDRAGLIKKKISKEDGIKTAISAIYNELEYARSVTLSRVKTPRKKEENVDATKLTPAETTDEGWTMI
Protein: Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1) (Q01147)
Organism: Mus musculus (Mouse)
Function: Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:21728997}.
Interaction partners:
- Histone acetyltransferase p300
- Histone lysine acetyltransferase CREBBP
- CREB-regulated transcription coactivator 2
- Transcription factor Jun
- Methyl-CpG-binding protein 2
- TATA-box binding protein associated factor 4
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Cyclic AMP-dependent transcription factor ATF-2
- Cellular tumor antigen p53
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MTMESGADNQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD
Protein: Type-2 angiotensin II receptor (Angiotensin II type-2 receptor) (AT2 receptor) (P35374)
Organism: Mus musculus (Mouse)
Function: Receptor for angiotensin II, a vasoconstricting peptide. Signals primarily via a non-canonical G-protein- and beta-arrestin independent pathways (By similarity). Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15539617}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P50052}.
Interaction partners:
- Angiotensinogen
- Type-1 angiotensin II receptor A
- Type-1 angiotensin II receptor B
- Guanine nucleotide-binding protein G
- Renin-1
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme 2
- Endothelin-1
- Kininogen-1
- Metalloproteinase inhibitor 3
Sequence:
MKDNFSFAATSRNITSSRPFDNLNATGTNESAFNCSHKPSDKHLEAIPVLYYMIFVIGFAVNIVVVSLFCCQKGPKKVSSIYIFNLALADLLLLATLPLWATYYSYRYDWLFGPVMCKVFGSFLTLNMFASIFFITCMSVDRYQSVIYPFLSQRRNPWQASYVVPLVWCMACLSSLPTFYFRDVRTIEYLGVNACIMAFPPEKYAQWSAGIALMKNILGFIIPLIFIATCYFGIRKHLLKTNSYGKNRITRDQVLKMAAAVVLAFIICWLPFHVLTFLDALTWMGIINSCEVIAVIDLALPFAILLGFTNSCVNPFLYCFVGNRFQQKLRSVFRVPITWLQGKRETMSCRKGSSLREMDTFVS
Protein: Transcription factor LRL1 (Basic helix-loop-helix protein 66) (AtbHLH66) (bHLH 66) (Protein DEFECTIVE REGION OF POLLEN 1) (Protein LJRHL1- LIKE 1) (AtLRL1) (Transcription factor EN 95) (Transcription factor bHLH66) (bHLH transcription factor bHLH066) (Q9ZUG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that regulates the development of root hairs. Transcription factor that regulates the development of sperm cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Homeobox-leucine zipper protein GLABRA 2
- Transcription factor WER
- Extensin-like protein
Sequence:
MMNSSLLTPSSSSSSHIQTPSTTFDHEDFLDQIFSSAPWPSVVDDAHPLPSDGFHGHDVDSRNQPIMMMPLNDGSSVHALYNGFSVAGSLPNFQIPQGSGGGLMNQQGQTQTQTQPQASASTATGGTVAAPPQSRTKIRARRGQATDPHSIAERLRRERIAERMKALQELVPNGNKTDKASMLDEIIDYVKFLQLQVKVLSMSRLGGAASVSSQISEAGGSHGNASSAMVGGSQTAGNSNDSVTMTEHQVAKLMEEDMGSAMQYLQGKGLCLMPISLATAISTATCHSRNPLIPGAVADVGGPSPPNLSGMTIQSTSTKMGSGNGKLNGNGVTERSSSIAVKEAVSVSKA
Protein: Fatty acid-binding protein, heart (Fatty acid-binding protein 3) (Heart-type fatty acid-binding protein) (H-FABP) (Mammary-derived growth inhibitor) (MDGI) (P11404)
Organism: Mus musculus (Mouse)
Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Subcellular location: Cytoplasm.
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Gastrotropin
- Fatty acid-binding protein, liver
- Platelet glycoprotein 4
Sequence:
MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTQSTFKNTEINFQLGIEFDEVTADDRKVKSLVTLDGGKLIHVQKWNGQETTLTRELVDGKLILTLTHGSVVSTRTYEKEA
Protein: Autophagy-related protein 11 (Q5AMN3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for the Cvt vesicles completion (By similarity).
Subcellular location: Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q12527}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12527}.
Interaction partners:
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 9
- Autophagy-related protein 13
- dynamin GTPase
- Autophagy-related protein 17
- Autophagy-related protein 101
- Autophagy-related protein 8
- Actin-related protein 2
- Serine/threonine-protein kinase TOR
- Actin-related protein 3
Sequence:
MSEISYLSINNAHNGIIIKIPKPVRFHTLSEFKKYIQQSYSIDSVDNLFLLTTFGIKLNYNLINEIGEVFVYDKRLFTNIVDQSLIDQYTQSTFRVSEPTHSPLLKSNVGFLKQNLSSNLKINQGWARIITQDGELMDQYCRELIQQINVIFKCLNTIFQFATNFTNEIEKNFSNFFNYVKLINYKTLHKSWITNYKNLKTFPTFKIDNENIKLSDFLEVDRLQSSADYIEKFLPLIVNKLNELKQVIETVNEEKLTVDKFIETSRNESISNFKNVNISNVLSQLQTESQQLTDDIENLHYKNMDEIYRLHRDKLSISIYNNAKDIYKNLNDLQQFKNKLTKASLKAFNTIANLQMKMVGVKTEMKKITTEDETATEDSKVGDVNYKTISNVKKYEDYLSLTIDLPLIFGFSLIEKRRQFEWYDFYSKGIVNNVSEQLSTIIEHEKVFRGIWLKKFGTLLSLINDDPLTPSLPNIDVTLVGNRQNNFSILYDLKIERDDIINYISLIEATNMSKNFVTLLNKNFKDLIASTNNMKKVTKVISSLSTYTTNSADDKSKSSHEEGTEEEIDFDLNLIKGLKSRIKKLENLLHQQQFKNLNNWPVIRNVPSMTNDNRQSTIIQPTVVSPARTNPTQLLSRNPSTTKENTTTNIHNNHQQSEVLDSSVIDKHLDNIRLKKLNNELQTKNTELTNQINSKNETITQQQKEMEHMKLKTEKRVDELMKKLQEKDEECQSLKQENKIKCDEVENLTKKLELSDNHNKELEAKITEYTQKATSKTKEIADLNKTVSNLRSELGDAMHMKNDLLSNLSSKEAEFTKERNQFNNDLKALQLKLDEINEDYENLMELTQAKQKKHDLIINDLNNVIINLMNDIKKTLLSVFEYFLEYCLVLESMGLLLVKEDEIYKIKRVKGLKSKKSIGDGDMSIISNGTPSSKVIEEIENEINIVNNIPPISSILPDSYSSGTESDSVVDRYNDQSMKLISTFNQLFKFNNENENENRIDHILNTLAFKNNVQLQEDSINDTRFFLNAISKRFRDVEGFAKRQAKDNKLKEQEHRKLVHRLNSKISVNGFQEKDLVLFLPTRIDRPNGENIPSNDKIQPWAAFNIGAPHYFLKTEQTKNKEWIIGRVKKITEYKVTEENVQSLESNPFQLSVNVTWYLVEADEE
Protein: Nuclear factor, interleukin 3 regulated, member 5 isoform X1 (Nuclear factor, interleukin 3-regulated, member 5) (F1QZP2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Nuclear receptor subfamily 1 group D member 2a
- Ankyrin repeat and SOCS box protein 15b
- Basic helix-loop-helix family, member e40.
- CLOCK-interacting pacemaker b.
- Circadian locomoter output cycles protein kaput
- Period circadian protein homolog 2
- Period homolog 1b
- Period circadian clock 1a.
- BHLH-PAS transcription factor
Sequence:
MESINLPTQNSGSSLETLETFSNYNESLPSPQMSSPPRQGRLIKPKPNSSCRRKREFISDEKKDASYWEKRRKNNEAAKRSREKRRLNDMVLENRVIALNDENVRLKTELLQLKLRFGLISSASYMEKTQQISNGAEAAANGANGSGATSGNPYFSSSGYSSASQVMMNSDSSEAEQSTRTERHTMLPKYSPRGSLSDMSDGSSRDSPEPINFDIKHESSGMDINRLEASVLNGMFNGHQSLGRLESNQPQEMEQQESVSNPAPPSATPQRSVILFRSGSSSYPVESQRVEDVDQQEASQTQQNGQITHFNQTGCNLPLRHDGLETLSEVAQQLARRSLDSPSYEFTNGKADAGENRRFVIQQQDLTVQGQCRSQVQDSTPNSFAPDLLNEAGKALVYQRTNPYLGTLNEEPPVLTYEGCTRADGFYQEHSSSGKDSSSSDGDPRSSDKEASTDDESPSSSSSDIGGYHATHQSASSPTMVTSDAYQYGDNQGEMKGTALPHKLRLKYRALSNGGSQDVQATTAAMSPESALPQHPYLALAQVNQQQGSSFGNKEGESETADELCTQRSPSRDKDMGWKESGKRSSGGRGNRNKKRD
Protein: Keratin, type II cytoskeletal 2 epidermal (Cytokeratin-2e) (CK-2e) (Epithelial keratin-2e) (Keratin-2 epidermis) (Keratin-2e) (K2e) (Type-II keratin Kb2) (P35908)
Organism: Homo sapiens (Human)
Function: Probably contributes to terminal cornification. Associated with keratinocyte activation, proliferation and keratinization. Required for maintenance of corneocytes and keratin filaments in suprabasal keratinocytes in the epidermis of the ear, potentially via moderation of expression and localization of keratins and their partner proteins (By similarity). Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32179842}.
Interaction partners:
- Keratin, type II cytoskeletal 1
- Keratin, type I cytoskeletal 10
- Keratin, type II cytoskeletal 1b
- Keratin, type II cytoskeletal 5
- Loricrin
- Filaggrin-2
- Serine protease 1
- Sterol O-acyltransferase 2
Sequence:
MSCQISCKSRGRGGGGGGFRGFSSGSAVVSGGSRRSTSSFSCLSRHGGGGGGFGGGGFGSRSLVGLGGTKSISISVAGGGGGFGAAGGFGGRGGGFGGGSSFGGGSGFSGGGFGGGGFGGGRFGGFGGPGGVGGLGGPGGFGPGGYPGGIHEVSVNQSLLQPLNVKVDPEIQNVKAQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNVGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECRMSGDLSSNVTVSVTSSTISSNVASKAAFGGSGGRGSSSGGGYSSGSSSYGSGGRQSGSRGGSGGGGSISGGGYGSGGGSGGRYGSGGGSKGGSISGGGYGSGGGKHSSGGGSRGGSSSGGGYGSGGGGSSSVKGSSGEAFGSSVTFSFR
Protein: Translocator protein PopB (Q9I324)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Host membrane {ECO:0000256|ARBA:ARBA00004301}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
Interaction partners:
- Regulatory protein PcrH
- Translocator outer membrane protein PopD
- Type III secretion protein PcrV
- Regulator in type III secretion
- Exoenzyme T
- Secreted exoenzyme S
- Type III secretion outer membrane protein PopN
- Lipoprotein
- Transcriptional anti-antiactivator ExsC
- Type 3 secretion system needle filament protein
Sequence:
MNPITLERAGLPYGVADAGDIPALGRPVARDVESLRVERLAAPAAASASGTGVALTPPSAASQQRLEVANRAEIASLVQAVGEDVGLARQVVLAGASTLLSAGLMSPQAFEIELAKITGEVENQQKKLKLTEIEQARKQNLQKMEDNQQKIRESEEAAKEAQKSGLAAKIFGWISAIASIIVGAIMVATGVGAAAGALMIAGGVMGVVSQSVQQAAADGLISKEVMEKLGPALMGIEMAVALLAAVVSFGGSAVGGLARLGAKIGGKAAEMTASLASKVADLGGKFGSLAGQSLSHSLKLGVQVSDLTLDVANGAAQATHSGFQAKAANRQADVQESRADLTTLQGVIERLKEELSRMLEAFQEIMERIFAMLQAKGETLHNLSSRPAAI
Protein: Phospholipase-like protein (PEARLI 4) family protein (Putative phospholipase) (Q9C5F6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDFFTSSKAKKDSKKSSGLFGKKTVSKSTPGSPAHPPGARSPPPSYLSNKRAETEYDFPMSNEQRPYWKQPASERVPNSHPRPPVYGYGTPDHRRDHGRERMEAMSYEPETNAPSSPYHPAGNRTPERPRKSTEYRREHQDRMYEADTRSNASPFHPFRSPSPSPFHTPDRRRDHYDMYEPEANTMLQNSAPGSPFHPAGSRSPPPYRTPDRRSNYDKEQFEDLYEQDGDVTPRNSSPPSPFHPAAYKTSDQRSNHGKEQIEDFYEQDDDVTPRNSSPPSPLHPAASHSPPPPQPYRTPDHRRSHQDNEDFEAMYELDGDLIHQKSAPPSPVHGPYYSSSDDDNHSTYLYPEIRSPLRSRIVSENSTPVHHNYQIVAAETYEQDKQFEPPELPDESQSFTMQEITKMRGLKNYESGKEESQSMISEAYVSVANYRVRQSVSETLQAIIDKHGDIAASSKLQAMATRSYYLESLAAVVMELKKTVLRDLTKTRVAEIAAVVKDMESVKINVSWLKTAVTELAEAVEYFGQYDTAKVEKEVCERDLTAKKGEMEEMTAELVKREKEIKECREKVTVVAGRLGQLEMKGSKLNKNLDLFQSKVHKFQGEAVLLHL