wanglab/gogpt-training-data huggingface dataset:
Protein: Subtilisin-like protease SBT1.7 (EC 3.4.21.-) (Cucumisin-like serine protease) (Subtilase subfamily 1 member 7) (AtSBT1.7) (Subtilisin-like serine protease 1) (At-SLP1) (O65351)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position. Essential for mucilage release from seed coats. Triggers the accumulation and/or activation of cell wall modifying enzymes necessary either for the loosening of the outer primary cell wall, or to facilitate swelling of the mucilage.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:12413398, ECO:0000269|PubMed:9188482}. Note=Intracellular spaces and cell wall.
Interaction partners:
- Pectinesterase inhibitor 6
- Beta-galactosidase 6
- Probable galacturonosyltransferase-like 5
- Transmembrane E3 ubiquitin-protein ligase FLY1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- Peroxidase 36
- Transcriptional corepressor LEUNIG_HOMOLOG
- Probable pectinesterase/pectinesterase inhibitor 58
- Subtilisin-like protease
- Acylamino-acid-releasing enzyme
Sequence:
MSSSFLSSTAFFLLLCLGFCHVSSSSSDQGTYIVHMAKSQMPSSFDLHSNWYDSSLRSISDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYELHTTRTPLFLGLDEHTADLFPEAGSYSDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLIGARFFARGYESTMGPIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDRDFPALAILGNGKNFTGVSLFKGEALPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASISILGTVVGVKPSPVVAAFSSRGPNSITPNILKPDLIAPGVNILAAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKTYKDGKPLLDIATGKPSTPFDHGAGHVSPTTATNPGLIYDLTTEDYLGFLCALNYTSPQIRSVSRRNYTCDPSKSYSVADLNYPSFAVNVDGVGAYKYTRTVTSVGGAGTYSVKVTSETTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSKPSGSNSFGSIEWSDGKHVVGSPVAISWT
Protein: SacI homology domain-containing protein / WW domain-containing protein (F4J9G0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDLHPPGGSKKTSVVVVTLDTGEVYVIASLLSKADTQVIYIDPTTGILRYNGKPGLDNFKSEREALDYITNGSRGGVRSSVYARAILGYAVLGSFGMLLVATRLNPSIPDLPGGGCVYTVAESQWVKIPLYNPQPQGKGETKNIQELTELDIDGKHYFCDTRDITRPFPSRMPLQSPDDEFVWNRWLSVPFKNIGLPEHCVILLQGFAEYRPFGSSGQLEGIVALMARRSRLHPGTRYLARGINSCSGTGNEVECEQLVWIPKRNGQSIAFNSYIWRRGTIPIWWGAELKMTAAEAEIYVADRDPYKGSTEYYQRLSKRYDTRNLDAPVGENQKKKAFVPIVCVNLLRSGEGKSECILVQHFEESMNFIKSSGKLPYTRVHLINYDWHASVKLKGEQQTIEGLWMYLKSPTMAIGISEGDYLPSRQRLKDCRGEVICIDDIEGAFCLRSHQNGVIRFNCADSLDRTNAASFFGGLQVFVEQCRRLGISLDTDLGYGHNSVNNQGGYNAPLPPGWEKRADAVTGKSYYIDHNTKTTTWSHPCPDKPWKRLDMRFEEFKRSTILSPVSELADLFLQQGDIHATLYTGSKAMHSQILNIFSEESGAFKQFSAAQKNMKITLQRRYKNAMVDSSRQKQLEMFLGMRLFKHLPSIPVQPLHVLSRPSGFFLKPVPNMSESSNDGSSLLSIKRKDITWLCPQAADIVELFIYLSEPCHVCQLLLTISHGADDLTCPSTVDVRTGRHIEDLKLVVELVQLDYRLPVIMFSGQGASIPRCANGTNLLVPLPGPISSEDMAVTGAGARLHEKDTSSLSLLYDFEELEGQLDFLTRVVAVTFYPAGAVRIPMTLGQIEVLGISLPWKGMFTCERTGGRLAELARKPDEDGSPFSSCSDLNPFAATTSLQAETVSTPVQQKDPFPSNLLDLLTGEDSSSDPFPQPVVECIASGGNDMLDFLDEAVVEYRGSDTVPDGSVPQNKRPKDSGAHLYLNCLKSLAGPNMAKKLEFVEAMKLEIERLRLNISAAERDRALLSIGIDPATINPNSSYDELYIGRLCKIANALAVMGQASLEDKIIASIGLEKLENNVIDFWNITRIGEGCDGGMCQVRAEVNKSPVGSSTKSSRGESGSVFLCFQCMKKACKFCCAGKGALLLSKSYSRDTANGGGSLADVSATSIGSDHYICKKCCSSIVLEALIVDYVRVMVSLRRSGRVDNAGREALNEVFGSNITNHLAVRGQPSPNREDFNFLRQILGKEESLSEFPFASFLHKVETATDSAPFFSLLTPLNLASSNAYWKAPPSADSVEAAIVLNTLSDVSSVILLVSPCGYSDADAPTVQIWASSDINKEARTLMGKWDVQSFIRSSPELSGSEKSGRAPRHIKFAFKNPVRCRIIWITLRLPRLGSSSSVSLDKNINLLSLDENPFAPIPRRASFGATIENDPCIHAKHILVTGNTVRDKTLQSVESMSVRNWLDRAPRLNRFLIPLETERPMENDLVLELYLQPASPLAAGFRLDAFSAIKPRVTHSPSSDVVDIWDPTSVIMEDRHVSPAILYIQVSVLQEQYKMVTIAEYRLPEARDGTKLYFDFPKQIQAQRVSFKLLGDVAAFTDEPAEAVDLSSRASPFAAGLSLANRIKLYYYADPYEVGKWTSLSSV
Protein: Guanine nucleotide-binding protein subunit beta-like protein (Q381D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 50S ribosomal protein L7Ae, putative
- Centromere/microtubule binding protein cbf5, putative
- Nucleolar protein 10
- H/ACA ribonucleoprotein complex subunit
- Integral membrane bound transporter domain-containing protein
- Telomerase reverse transcriptase
Sequence:
MPAKRKGKIATPPVSILETDGFESAIFRRLVAAPDYSLGSGGGEILATWSLQSVPVIAARNVNENSLPRLEYNTPAAWVKLPYPAIDIAWCPFKEGDESASFLTATNSLPLQLWDVEDGALRASYCCSNTMGMPVHPHSILWSTHRELIAAGYGEPHDDVHIRLYDVLREGNCVESSYRSPCSKGIVSALADGPTPYSESLILAGFIRNGNVDIIDTRHCGAAAVLRGLRSGVVQILPHPTVGHLVYAAGRLGENRIVCWDIRKSNDMLLTFERTVRTQQPAMFGFVRRKDGGSQRVDLVSATHSGGVLVFDACTNGKPRGVQSQLGPTAGLTVLSHESPTVAVTVGEARYIVRDRYEENAASPSHINGYGLKRSRSQLRKGDLDTENDSGDEGAGVSTSTLGAAIFNV
Protein: Histone-lysine N-methyltransferase CLF (EC 2.1.1.-) (Polycomb group protein CURLY LEAF) (Protein INCURVATA 1) (Protein SET DOMAIN GROUP 1) (Protein photoperiod insensitive flowering) (P93831)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes, mainly abscisic acid (ABA) responsive elements. Required to regulate floral development by repressing the AGAMOUS homeotic gene in leaves, inflorescence stems and flowers. Together with ATX1, modulates AG nucleosome methylation statement. Regulates the antero-posterior organization of the endosperm, as well as the division and elongation rates of leaf cells. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. Forms a nuclear complex with EZA1/SWN and HXK1 to target common glucose-responsive genes and regulate glucose signaling by glucose-mediated gene repression. Affects the recruitment of HXK1 to the target chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:11691919, ECO:0000269|PubMed:17881378, ECO:0000269|PubMed:35394700}.
Interaction partners:
- Polycomb group protein EMBRYONIC FLOWER 2
- Polycomb group protein VERNALIZATION 2
- Histone-binding protein MSI1
- Polycomb group protein FERTILIZATION-INDEPENDENT ENDOSPERM
- Lysine-specific demethylase ELF6
- Polycomb group protein FERTILIZATION-INDEPENDENT SEED 2
- Putative E3 ubiquitin-protein ligase RING1a
- WD-40 repeat-containing protein MSI4
- Histone H3.1
- Histone H3-like 3
Sequence:
MASEASPSSSATRSEPPKDSPAEERGPASKEVSEVIESLKKKLAADRCISIKKRIDENKKNLFAITQSFMRSSMERGGSCKDGSDLLVKRQRDSPGMKSGIDESNNNRYVEDGPASSGMVQGSSVPVKISLRPIKMPDIKRLSPYTTWVFLDRNQRMTEDQSVVGRRRIYYDQTGGEALICSDSEEEAIDDEEEKRDFLEPEDYIIRMTLEQLGLSDSVLAELASFLSRSTSEIKARHGVLMKEKEVSESGDNQAESSLLNKDMEGALDSFDNLFCRRCLVFDCRLHGCSQDLIFPAEKPAPWCPPVDENLTCGANCYKTLLKSGRFPGYGTIEGKTGTSSDGAGTKTTPTKFSSKLNGRKPKTFPSESASSNEKCALETSDSENGLQQDTNSDKVSSSPKVKGSGRRVGRKRNKNRVAERVPRKTQKRQKKTEASDSDSIASGSCSPSDAKHKDNEDATSSSQKHVKSGNSGKSRKNGTPAEVSNNSVKDDVPVCQSNEVASELDAPGSDESLRKEEFMGETVSRGRLATNKLWRPLEKSLFDKGVEIFGMNSCLIARNLLSGFKSCWEVFQYMTCSENKASFFGGDGLNPDGSSKFDINGNMVNNQVRRRSRFLRRRGKVRRLKYTWKSAAYHSIRKRITEKKDQPCRQFNPCNCKIACGKECPCLLNGTCCEKYCGCPKSCKNRFRGCHCAKSQCRSRQCPCFAADRECDPDVCRNCWVIGGDGSLGVPSQRGDNYECRNMKLLLKQQQRVLLGISDVSGWGAFLKNSVSKHEYLGEYTGELISHKEADKRGKIYDRENCSFLFNLNDQFVLDAYRKGDKLKFANHSPEPNCYAKVIMVAGDHRVGIFAKERILAGEELFYDYRYEPDRAPAWAKKPEAPGSKKDENVTPSVGRPKKLA
Protein: Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase 2) (DAHP synthase 2) (PhDAHP2) (Phospho-2-keto-3-deoxyheptonate aldolase 2) (A0A067XGX8)
Organism: Petunia hybrida (Petunia)
Function: Involved in the production of volatile organic compounds (VOCs). Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24815009}.
Interaction partners:
Sequence:
MALTATATTRGGSALPNSCLQTPKFQSLQKPTFISSFPTNKKTKPRTKHISAVQSPPSTTKWNLESWKTKPAFQLPDYPDKVELESVLKTLSTYPPIVFAGEARNLEEKLGEAALGNAFLLQGGDCAESFKEFSANNIRDTFRVMLQMGVVLMFGGQMPVIKVGRMAGQFAKPRSDPFEEKDGVKLPSYRGDNVNGDAFDEKSRIPDPHRMVRAYTQSVATLNLLRAFASGGYAAMQRVNQWNLDFTDQSEQGDRYRELAHRVDEAMGFMTAAGLTVDHTIMTTTDFWTSHECLLLPYEQALTREDSTSGLYYDCSAHMIWVGERTRQLDGAHVEFLRGIANPLGIKVSHKMDPDELVKLIDILNPQNKPGRITVITRMGADNMRVKLPHLIRAVRGAGQIVTWVSDPMHGNTTKAPCGLKTRSFDSIRAELRAFFDVHEQEGSYPGGVHLEMTGQNVTECVGGSRTITYNDLSSRYHTHCDPRLNASQALELAFAIAERLRRRRLGPKFSL
Protein: Caspase recruitment domain-containing protein 16 (Caspase recruitment domain-only protein 1) (CARD-only protein 1) (Caspase-1 inhibitor COP) (Pseudo interleukin-1 beta converting enzyme) (Pseudo-ICE) (Pseudo-IL1B-converting enzyme) (Q5EG05)
Organism: Homo sapiens (Human)
Function: Caspase inhibitor. Acts as a regulator of procaspase-1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-interleukin-1 beta (IL1B) and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. Also induces NF-kappa-B activation during the pro-inflammatory cytokine response. Also able to inhibit CASP1-mediated neuronal cell death, TNF-alpha, hypoxia-, UV-, and staurosporine-mediated cell death but not ER stress-mediated cell death. Acts by preventing activation of caspases CASP1 and CASP4, possibly by preventing the interaction between CASP1 and RIPK2.
Interaction partners:
- Caspase-1
- Putative caspase recruitment domain-containing protein 17P
- Caspase recruitment domain-containing protein 18
- Plasma serine protease inhibitor
- Caspase recruitment domain-containing protein 8
- Apoptosis-associated speck-like protein containing a CARD
- Serpin B6
- Caspase-5
- G-patch domain and KOW motifs-containing protein
- Kallikrein-8
Sequence:
MADKVLKEKRKLFIHSMGEGTINGLLDELLQTRVLNQEEMEKVKRENATVMDKTRALIDSVIPKGAQACQICITYICEEDSYLAETLGLSAALQAVQDNPAMPTCSSPEGRIKLCFLEDAQRIWKQKLQRCHVQNTIIKWSERYTSGSFEMQWLFLRTNFIERFWRNILLLPLHKGSLYPRIPGLGKELQTGTHKLS
Protein: Alpha/beta-Hydrolases superfamily protein (Esterase/lipase/thioesterase family protein) (Lysophospholipase-like protein) (Q9LFQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
Sequence:
MGLHPVSEANASSPFGSLSAAEFYSRHSVTHSSAYVTNPTGLKLFTQWWTPLNRPPLGLIAVVHGFTGESSWFLQLTSVLFAKSGYLTCAIDHQGHGFSDGLTAHIPNINLIVDDCISFFDDFRKRHASSFLPAFLYSESLGGAIALYITLRQKHQWNGLILSGAMCSISHKFKPPWPLQHLLTLAATLIPTWRVVPTRGSIAGVSFKEPWKRKLAYANPNRTVGKPRAATAYELVRVCEDLQNRFEEVEVPLMIVHGRDDVVCDPASVEELYRRCSSRDKTIKIYPGMWHQLIGESEENVDLVFGDVLDWIKTRSEISTIHGGTKA
Protein: Aspartyl aminopeptidase (EC 3.4.11.21) (E5RIA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGKARKEAVQTAAKELLKFVNRSPSPFHAVAECRNRLLQAGFSELKETEKWNIKPESKYFMTRNSSTIIAFAVGGQYVPGNGFSLIGAHTDSPCLRVKRRSRRSQVGFQQVGVETYGGGIWSTWFDRDLTLAGRVIVKCPTSGRLEQQLVHVERPILRIPHLAIHLQRNINENFGPNTEMHLVPILATAIQEELEKGTPEPGPLNAVDERHHSVLMSLLCAHLGLSPKDIVEMELCLADTQPAVLGGAYDEFIFAPRLDNLHSCFCALQALIDSCAGPGSLATEPHVRMVTLYDNEEVGSESAQGAQSLLTELVLRRISASCQHPTAFEEAIPKSFMISADMAHAVHPNYLDKHEENHRPLFHKGPVIKVNSKQRYASNAVSEALIREVANKVKVPLQDLMVRNDTPCGTTIGPILASRLGLRVLDLGSPQLAMHSIREMACTTGVLQTLTLFKGFFELFPSLSHNLLVD
Protein: Serine/threonine-protein kinase mrck-1 (EC 2.7.11.1) (Myotonic dystrophy kinase-related CDC42-binding kinase homolog) (O01583)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation. Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19675126, ECO:0000269|PubMed:27451898}. Cytoplasm, cell cortex {ECO:0000269|PubMed:27451898}. Note=Enriched in the apical cell cortex specifically in the gastrulating endoderm precursor cells (EPCs), but not in the apical domain of other early embryonic interphase cells (PubMed:27451898). Endoderm cell fate specification is necessary and sufficient for mrck-1 to localize apically (PubMed:27451898). Forms parallel punctate bundles in dorsal and ventral epidermal cells (PubMed:19675126). {ECO:0000269|PubMed:19675126, ECO:0000269|PubMed:27451898}.
Interaction partners:
- Ras-like GTP-binding protein rhoA
- Cell division control protein 42 homolog
- cGMP-dependent protein kinase interacting domain-containing protein
- Ras-related protein ced-10
- Myosin regulatory light chain
- Myosin-11
- Cdc-42 Related Protein
Sequence:
MAEPPPDDSAPVRLKTLENIYMDGPSKKPEALSFETLIDSLICLYDECCNSTLRKEKCIAEFVESVKTVISKAKKLRLSRDDFEVLKVIGKGAFGEVAVVRMRGVGEIYAMKILNKWEMVKRAETACFREERDVLVYGDRRWITNLHYAFQDEKNLYFVMDYYIGGDMLTLLSKFVDHIPESMAKFYIAEMVLAIDSLHRLGYVHRDVKPDNVLLDMQGHIRLADFGSCLRILADGSVASNVAVGTPDYISPEILRAMEDGRGRYGKECDWWSLGICMYEMLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDWVVSEEAKDLIRQLICSSDVRFGRNGLSDFQLHPFFEGIDWNTIRDSNPPYVPEVSSPEDTSNFDVDVCEDDFTPCLQETQPPRVLAAFTGNHLPFVGFSYTHGSLLSDARSLTDEIRAIAQRCQGDAELMEKSVDGFMVELENEKAELVQKLKEAQTIIAQHVAENPRSEEDRNYESTIAQLKDEIQILNKRLEDEALAQQQQKPKDEIVAESEKKLKELKERNKQLVMEKSEIQRELDNINDHLDQVLVEKATVVQQRDDMQAELADVGDSLLTEKDSVKRLQDEAEKAKKQVADFEEKLKEIETEKIALIKKQEEVTIEARKSVETDDHLSEEVVAAKNTIASLQATNEERETEIKKLKQRMDEERASHTAQSEQEMKQLEAHYERAQKMLQDNVEQMNVENRGLRDEIEKLSQQMAALPRGGLNEQQLHEIFNWVSEEKATREEMENLTRKITGEVESLKNNSPLTTSNYIQNTPSGWGSRRMNNVARKDGLDLQRQLQAEIDAKLKLKAELKNSQEQYLTSAARLDDTEKRMASLMREVAMLKQQKNIENSSDSAFSSTMGRGDLMISMNNDYEMSNSSLMRQEMISRQSTPSYENAILLHDHQVPKRVDDLRYKQKPMKTASGIFSPVSISAMERGHNFERMKIKTPTKCGHCTSILIGLDRQGLFCQSCQYACHVSCAERVSQSCPVPEEERRPLGIDPTRGVGTAYEGLVKTPRAGGVRKGWQTAYVVVCDFKLYLYDCTVDRQNKMQDVKNEIRLVLDMRDPDFTVCGVSEADVIHAQKGDIPKIFRVTTTQILNSSSEYSSSSKFYTLFMAETEEEKRKWVVALSELKTLLRRSKLADRKAFLVKEVFDVTTLPSIRVAQCCAIIDRSKIVIGFSDHGLYCIEISRQLLIPVGGEKENKQRCVETVEYDEAEQLLMMIVGPAKDRHVRIVPSAALDGRDLKWIKVNDTKGCHLLAVGTNNPGGRAGFFAVAFKKSVTIFQIDRSEKRHKKWKDLAMPGTPQSIAIFNGRLYVGFSHSFRSWSLVGVDSSPVGSGDASGAVLQHISLVNMEDTSLQFLNQQTSYEAKLIVNVPGSPDEYLLVFNMIGLYVNEMGRRSRLPEVMFPTQAKYFAYHEPYLCVFSENEVDIFNVTLAEWVQTINLRSAKPLSGDGILSTCLCNDSPIFVLLQNVLQDQDSIEVPVNLASGSTDGRKVTRRKFTFRTIGKDDRSASERRSHIQISTPSDFMHIVHMGPAPVMELQQNFIDLQSNHSHTSSDKDSLNRSVNND
Protein: F-box/LRR-repeat protein 12 (F-box and leucine-rich repeat protein 12) (F-box protein FBL12) (Q9EPX5)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia (By similarity).
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
Sequence:
MATLFDLPDLVLLEIFSYLPVRDRIRISRVCHRWKRLVDDRWLWRHVDLTLYTMRPKVMWHLLRRYMASRLYSLRMGGYLFSGSQAPQLSPALMRALGQKCPNLKRLCLHVADLSMVPITSLPSTLRTLELHSCEISMIWLQKEQDPTVLPLLECIVLDRVPAFRDEHLQGLTRFRALRSLVLGGTYRVTETGLDASLQELSYLQRLEVLGCTLSADSTLLAISRHLRDVRKIRLTVGGLSAQGLVFLEGMPVLESLCFQGPLITPDMPTPTQIVSSCLTMPKLRVLEVQGLGWEGQEAEKILCKGLPHCIVIVRACPKESMDWWM
Protein: Leukocyte antigen CD37 (Tetraspanin-26) (Tspan-26) (CD antigen CD37) (P11049)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:17182550, ECO:0000269|PubMed:22624718, ECO:0000269|PubMed:26784544}; Multi-pass membrane protein.
Interaction partners:
- C-type lectin domain family 7 member A
- B-lymphocyte antigen CD19
- Tetraspanin-7
- Leukocyte surface antigen CD53
- CD82 antigen
- Complement receptor type 2
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- T-cell surface antigen CD2
- CD9 antigen
- Tyrosine-protein kinase SYK
Sequence:
MSAQESCLSLIKYFLFVFNLFFFVLGSLIFCFGIWILIDKTSFVSFVGLAFVPLQIWSKVLAISGIFTMGIALLGCVGALKELRCLLGLYFGMLLLLFATQITLGILISTQRAQLERSLRDVVEKTIQKYGTNPEETAAEESWDYVQFQLRCCGWHYPQDWFQVLILRGNGSEAHRVPCSCYNLSATNDSTILDKVILPQLSRLGHLARSRHSADICAVPAESHIYREGCAQGLQKWLHNNLISIVGICLGVGLLELGFMTLSIFLCRNLDHVYNRLARYR
Protein: Aquaporin-7 (AQP-7) (Aquaglyceroporin-7) (Aquaporin adipose) (AQPap) (Aquaporin-7-like) (O14520)
Organism: Homo sapiens (Human)
Function: Forms a channel that mediates water and glycerol transport across cell membranes at neutral pH. The channel is also permeable to urea. Plays an important role in body energy homeostasis under conditions that promote lipid catabolism, giving rise to glycerol and free fatty acids. Mediates glycerol export from adipocytes. After release into the blood stream, glycerol is used for gluconeogenesis in the liver to maintain normal blood glucose levels and prevent fasting hypoglycemia. Required for normal glycerol reabsorption in the kidney (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11952783, ECO:0000269|PubMed:28042826, ECO:0000269|PubMed:30423801, ECO:0000269|PubMed:9405233}; Multi-pass membrane protein {ECO:0000269|PubMed:36737436}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:27832861}; Multi-pass membrane protein {ECO:0000269|PubMed:36737436}. Lipid droplet {ECO:0000305|PubMed:27832861}. Note=Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (By similarity). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (PubMed:27832861). {ECO:0000250|UniProtKB:O54794, ECO:0000269|PubMed:27832861}.
Interaction partners:
- Aquaporin-11
- Putative aquaporin-12A
- Aquaporin-8
- Perilipin-1
- Aquaporin-1
- Aquaporin-5
- Glycerol kinase 2
- Glycerol kinase
- Lens fiber major intrinsic protein
- Aquaporin-2
Sequence:
MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF
Protein: Nuclear protein MDM1 (Mdm4 transformed 3T3 cell double minute 1 protein) (Mouse double minute 1) (Q9D067)
Organism: Mus musculus (Mouse)
Function: Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules.
Subcellular location: Nucleus {ECO:0000269|PubMed:3182840}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TC05}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392}. Note=Localizes to the centriole lumen. {ECO:0000269|PubMed:26337392}.
Interaction partners:
Sequence:
MPVRFKGLSEYQRNFLWKKSYLSESYNPSVGQKYSWAGLRSDQLGITKEPGFISKRRVPYHDPQISKYLEWNGTVRKKDTLVPPEPQAFGTPKPQEAEQGEDANQEAVLSLEASRVPKRTRSHSADSRAEGVSDTVEKHQGVTRSHAPVSADVELRPSSKQPLSQSIDPRLDRHLRKKAGLAVVPTNNALRNSEYQRQFVWKTSKESAPVFASNQVFRNKSQIIPQFQGNTFTHETEYKRNFKGLTPVKEPKSREYLKGNSSLEMLTPVKKADEPLDLEVDMASEDSDQSVKKPASWRHQRLGKVNSEYRAKFLSPAQYFYKAGAWTRVKENLSNQVKELREKAESYRKRVQGTHFSRDHLNQIMSDSNCCWDVSSVTSSEGTVSSNIRALDLAGDLTNHRTPQKHPPTKLEERKVASGEQPLKNSTRRLEMPEPAASVRRKLAWDAEESTKEDTQEEPRAEEDGREERGQDKQTCAVELEKPDTQTPKADRLTEGSETSSVSSGKGGRLPTPRLRELGIQRTHHDLTTPAVGGAVLVSPSKVKPPGLEQRRRASSQDGLETLKKDITKKGKPRPMSLLTSPAAGMKTVDPLPLREDCEANVLRFADTLPVSKILDRQPSTPGQLPPCAPPYCHPSSRIQGRLRDPEFQHNMGKPRTNNLQLHPHDAFNDEDADRLSEISARSAVSSLRAFQTLARAQKRKENFWGKP
Protein: MAM domain-containing protein 2 (MAM domain-containing proteoglycan) (Mamcan) (Q7Z304)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MLLRGVLLALQALQLAGALDLPAGSCAFEESTCGFDSVLASLPWILNEEGHYIYVDTSFGKQGEKAVLLSPDLQAEEWSCLRLVYQITTSSESLSDPSQLNLYMRFEDESFDRLLWSAKEPSDSWLIASLDLQNSSKKFKILIEGVLGQGNTASIALFEIKMTTGYCIECDFEENHLCGFVNRWNPNVNWFVGGGSIRNVHSILPQDHTFKSELGHYMYVDSVYVKHFQEVAQLISPLTTAPMAGCLSFYYQIQQGNDNVFSLYTRDVAGLYEEIWKADRPGNAAWNLAEVEFSAPYPMEVIFEVAFNGPKGGYVALDDISFSPVHCQNQTELLFSAVEASCNFEQDLCNFYQDKEGPGWTRVKVKPNMYRAGDHTTGLGYYLLANTKFTSQPGYIGRLYGPSLPGNLQYCLRFHYAIYGFLKMSDTLAVYIFEENHVVQEKIWSVLESPRGVWMQAEITFKKPMPTKVVFMSLCKSFWDCGLVALDDITIQLGSCSSSEKLPPPPGECTFEQDECTFTQEKRNRSSWHRRRGETPTSYTGPKGDHTTGVGYYMYIEASHMVYGQKARLLSRPLRGVSGKHCLTFFYHMYGGGTGLLSVYLKKEEDSEESLLWRRRGEQSISWLRALIEYSCERQHQIIFEAIRGVSIRSDIAIDDVKFQAGPCGEMEDTTQQSSGYSEDLNEIEY
Protein: Spindle assembly abnormal protein 5 (Q20010)
Organism: Caenorhabditis elegans
Function: Required for centrosome duplication. Essential for daughter-centriole formation. Requires both maternal and partenal expression, suggesting that it regulates centriole duplication during both spermatogenesis and early embryogenesis.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localizes to centrioles. Shuttles between centrioles and the cytoplasm throughout the cell cycle. Requires zyg-1 and dephosphorylation by the PP2A complex for centriole localization.
Interaction partners:
- Spindle assembly abnormal protein 6
- Spindle assembly abnormal protein 4
- Probable serine/threonine-protein kinase zyg-1
- Spindle-defective protein 2
- Spindle assembly abnormal protein 7
- Spindle-defective protein 5
- Serine/threonine-protein kinase plk-1
- Suppressor of zyg-1 protein 20
Sequence:
MNNYDDLPCSIYFKKPTVQEFVDQPRVFEDSEVPAFQEVLQLPQERTKPPVPSTQPIVAAVEVAKKKSCLSAPKPRKEPPSHPALRQKTVAFGKTVNVSQTVEGTSRNSKKVLASTMSAQNTTTTEEQAAENWRDAMKTELQTIRTEIQEETARRQEELNAQNLVKMQELMSNFFQKITIPKQQAIEPVEKDKENFHESPRQSRQQKPASKIASAREVIKRDGVIPPEALTIIEQRLRSDPMFRQQIDNVLADAECDANRAAYSPPPPMSEVRYGSGVNPALMRETLTVERSIRYDNGLASIDSRQWTNERRDNRAPDSYRTYEPDQPCHSLYQKGQSISYYPSEAAGKTTARNNRTGYYVEDSSDHEEDVVVNKRGQNYHEQAVPETPAERERRIREKYARRK
Protein: Non-specific phospholipase C2 (EC 3.1.-.-) (O81020)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phospholipase D beta 1
- Phospholipase D delta
- Choline/ethanolaminephosphotransferase 1
- Phospholipase D alpha 1
- Phosphatase IMPL1, chloroplastic
- Phospholipase D alpha 4
- Triacylglycerol lipase SDP1
- Inositol-phosphate phosphatase
- Phosphatidylinositol 4-kinase beta 1
Sequence:
MSIKAFALIQLLSVTILYNHVHATSPIKTIVVVVMENRSFDHMLGWMKKLNPEINGVDGSESNPVSVSDPSSRKIKFGSGSHYVDPDPGHSFQAIREQVFGSNDTSMDPPPMNGFVQQAYSEDPSGNMSASVMNGFEPDKVPVYKSLVSEFAVFDRWFASVPSSTQPNRMFVHSGTSAGATSNNPISLAKGYPQRTIFDNLDDEEFSFGIYYQNIPAVLFYQSLRKLKYVFKFHSYGNSFKDHAKQGKLPAYTVIEQRYMDTLLEPASDDHPSHDVYQGQKFIKEVYETLRASPQWNETLLIITYDEHGGYFDHVPTPVRNVPSPDGIVGPDPFLFQFNRLGIRVPTIAVSPWIEKGTVVHGPNGSPFPSSEYEHSSIPATVKKLFNLSSPFLTKRDEWAGTFENILQIRKEPRTDCPETLPEPVKIRMGEANEKALLTEFQQELVQLAAVLKGDNMLTTFPKEISKGMTVIEGKRYMEDAMKRFLEAGRMALSMGANKEELVHMKTSLTGRRP
Protein: Small ribosomal subunit protein mS26 (28S ribosomal protein S26, mitochondrial) (MRP-S26) (S26mt) (Q3SZ86)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10751423, ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein mS34
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein mS31
Sequence:
MLRALSTLGARPLGRPPAQFLLLARGRKTRHDPPAKSKIGRVATPPAVDPAEFFVLTERYRQYRQTVRALRQEFVTEVRRKVHEARAGVLAERKALQDAAEHRELMAWNQAENQRLHELRMARLRQEAREQEQWQAEEAAREAREAEAWARLKEQEVLQLQEDAKNFITRENLEARVEEALDSPKSYNWAVTREGQVVTPQHKGS