wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase SH3RF1 (EC 2.3.2.27) (Plenty of SH3s) (Protein POSH) (RING finger protein 142) (RING-type E3 ubiquitin transferase SH3RF1) (SH3 domain-containing RING finger protein 1) (SH3 multiple domains protein 2) (Q7Z6J0)
Organism: Homo sapiens (Human)
Function: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:15659549, ECO:0000269|PubMed:17420289}. Note=Colocalizes, with AKT2, in lamellipodia (By similarity). Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000269|PubMed:17420289}.
Interaction partners:
- Mitogen-activated protein kinase 9
- RAC-alpha serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Mitogen-activated protein kinase kinase kinase 11
Sequence:
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEELPSNILLVRLLDGIKQRPWKPGPGGGSGTNCTNALRSQSSTVANCSSKDLQSSQGGQQPRVQSWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDAGECSSAAAQSSTAPKHSDTKKNTKKRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPSDVPYQAALGTLNPPLPPPPLLAATVLASTPPGATAAAAAAGMGPRPMAGSTDQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQTSRGVTMVSPSTAGGPAQKLQGNGVAGSPSVVPAAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAAGLSPASVGLSHHSLASPQPAPLMPGSATHTAAISISRASAPLACAAAAPLTSPSITSASLEAEPSGRIVTVLPGLPTSPDSASSACGNSSATKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLEVELGSAELPLQGAVGPELPPGGGHGRAGSCPVDGDGPVTTAVAGAALAQDAFHRKASSLDSAVPIAPPPRQACSSLGPVLNESRPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
Protein: Strictosidine-O-beta-D-glucosidase (EC 3.2.1.105) (Q8GU20)
Organism: Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Function: Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the therapy of heart disorders.
Interaction partners:
Sequence:
MDNTQAEPLVVAIVPKPNASTEHTNSHLIPVTRSKIVVHRRDFPQDFIFGAGGSAYQCEGAYNEGNRGPSIWDTFTQRSPAKISDGSNGNQAINCYHMYKEDIKIMKQTGLESYRFSISWSRVLPGGRLAAGVNKDGVKFYHDFIDELLANGIKPSVTLFHWDLPQALEDEYGGFLSHRIVDDFCEYAEFCFWEFGDKIKYWTTFNEPHTFAVNGYALGEFAPGRGGKGDEGDPAIEPYVVTHNILLAHKAAVEEYRNKFQKCQEGEIGIVLNSMWMEPLSDVQADIDAQKRALDFMLGWFLEPLTTGDYPKSMRELVKGRLPKFSADDSEKLKGCYDFIGMNYYTATYVTNAVKSNSEKLSYETDDQVTKTFERNQKPIGHALYGGWQHVVPWGLYKLLVYTKETYHVPVLYVTESGMVEENKTKILLSEARRDAERTDYHQKHLASVRDAIDDGVNVKGYFVWSFFDNFEWNLGYICRYGIIHVDYKSFERYPKESAIWYKNFIAGKSTTSPAKRRREEAQVELVKRQKT
Protein: Signal transduction protein MDG1 (Multicopy suppressor of defective G-protein 1) (P53885)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8914522}; Peripheral membrane protein {ECO:0000269|PubMed:8914522}.
Interaction partners:
- Protein SDS24
- 5'-AMP-activated protein kinase subunit gamma
- Protein SDS23
Sequence:
MQSSLPQFTFKWPKGPEAIILTGTFDDWKGTLPMVKDPSGAFEITLPVTFDSPSSKFYFKFIVDGQWLPSKDYKVNIDEGVENNFITEEDVIKQRENGSSTLVPESAGLAVSKNAPLIEPEAEKRAKKLRKFKIKRVIKTNKQTGERSIFSQEVVELPDSEDETQQVNKTGKNADGLSGTTTIIENNVGVNEEKAIKPYEENHPKVNLVKSEGYVTDGLGKTQSSESRLYELSAEDLEKEEEEEDEDKGGGKDTSTSADAEASEDQNKEPLSKSAKFEKPEEKVPVSSITSHAKETSVKPTGKVATETQTYETKQGAPTAAAKKIEAKKATRPSKPKGTKETPNKGVQKNPAKNGGFFKKLAQLLK
Protein: Uncharacterized protein (Q2U480)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Ribosomal protein S13
- 40S ribosomal protein S3
- Large ribosomal subunit protein uL18 C-terminal eukaryotes domain-containing protein
- 40S ribosomal protein S6
- Large ribosomal subunit protein uL23 N-terminal domain-containing protein
- Small ribosomal subunit protein eS1
- 40S ribosomal protein S14
- Ribosomal protein L21e
- 40S ribosomal protein S24
- Uncharacterized protein
Sequence:
MGYYDDDVSRDGAHHAVRVVEPRSSGRRSADTVPIPCNFIRIGDILILQGRPCQVIRISVSPQTGQHRYLGVDLFTRQLQEESSFVSNPSPSVVVQTMIGPVYKTYRILDIRDNQIVAMTETGDVKQGIPVVPQGELFSKIKAAFEDGHGSVRALVINDGGRELVVDYKVIQSSRL
Protein: Transgelin (Q1HQ70)
Organism: Bombyx mori (Silk moth)
Interaction partners:
Sequence:
MANNRATKSGFAAEAQRKINSKYSEELAHESLEWIRMITGEPENTSGDMDNFYEVLKDGTLLCKLANNIHPNMIKKINTSSMAFKCMENINAFLEAARQLGVPAQETFQTVDLWERQNLNSVVICLQSLGRKAGTYGKPSIGPKEAEKNVRNFSEEQLRAGQGVISLQYGSNKGANQSGINFGNTRHM
Protein: Zinc finger protein 395 (A0A286YDG8)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLSRRLGKRSLLGARVLGPSAAEVPSGATLPLEPQIEVPEGAMSLSPLTSKDPVCQEQPKELLKALGTSGHPQVAFQPGQKVCVWYGGQECKG
Protein: Sodium-dependent phosphate transport protein 2A (Sodium-phosphate transport protein 2A) (Na(+)-dependent phosphate cotransporter 2A) (NaPi-7) (Sodium/phosphate cotransporter 2A) (Na(+)/Pi cotransporter 2A) (NaPi-2a) (Solute carrier family 34 member 1) (Q60825)
Organism: Mus musculus (Mouse)
Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:35428804}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q06496}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the brush border membranes of the proximal tubules. Internalized from the cell surface upon PTH stimulation (PubMed:35428804). {ECO:0000250|UniProtKB:Q06496, ECO:0000269|PubMed:35428804}.
Interaction partners:
- Na
- Na
- Sodium-dependent phosphate transport protein 2C
- Klotho
- Sodium-dependent phosphate transport protein 2B
- Fibroblast growth factor 23
- Uromodulin
- Parathyroid hormone
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Sodium-dependent phosphate transport protein 1
Sequence:
MMSYSERLGGPAVSPLPVRGRHMVHGATFAYVPSPQVLHRIPGTSTYAISSLSPVTLTEHSCPCGEVLECHDPLPTKLAQEEEQKPEPRLSQKLAQVGTKLLKVPLMLAFLYLFVCSLDVLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHVTGLVVASFNIRGGRDAPDLLKVITEPFTRLIIQLDKSVITSIAVGDESLRNHSLIRIWCHPDTTEASTSMSRVEAIGSLANTTMEKCNHIFVDTGLPDLAVGLILLAGSLVVLCTCLILLVKMLNSLLKGQVMSSRRSSTQTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSSFQIALCHFFFNISGILLWYPLPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQAMVGVGTPFGALLAFVVLVNVLQSRSPGHLPKWLQTWDFLPRWMHSLQPLDGLITRATLCYARPEPRSPQLPPRVFLEELPPATPSPRLALPAHHNATRL
Protein: Transforming growth factor beta activator LRRC32 (Garpin) (Glycoprotein A repetitions predominant) (GARP) (Leucine-rich repeat-containing protein 32) (G3XA59)
Organism: Mus musculus (Mouse)
Function: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Able to outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (By similarity). Controls activation of TGF-beta-1 (TGFB1) on the surface of activated regulatory T-cells (Tregs). Required for epithelial fusion during palate development by regulating activation of TGF-beta-3 (TGFB3).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14392}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:Q14392}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-2 proprotein
Sequence:
MSHQILLLLAMLTLGLAISQRREQVPCRTVNKEALCHGLGLLQVPSVLSLDIQALYLSGNQLQSILVSPLGFYTALRHLDLSDNQISFLQAGVFQALPYLEHLNLAHNRLATGMALNSGGLGRLPLLVSLDLSGNSLHGNLVERLLGETPRLRTLSLAENSLTRLARHTFWGMPAVEQLDLHSNVLMDIEDGAFEALPHLTHLNLSRNSLTCISDFSLQQLQVLDLSCNSIEAFQTAPEPQAQFQLAWLDLRENKLLHFPDLAVFPRLIYLNVSNNLIQLPAGLPRGSEDLHAPSEGWSASPLSNPSRNASTHPLSQLLNLDLSYNEIELVPASFLEHLTSLRFLNLSRNCLRSFEARQVDSLPCLVLLDLSHNVLEALELGTKVLGSLQTLLLQDNALQELPPYTFASLASLQRLNLQGNQVSPCGGPAEPGPPGCVDFSGIPTLHVLNMAGNSMGMLRAGSFLHTPLTELDLSTNPGLDVATGALVGLEASLEVLELQGNGLTVLRVDLPCFLRLKRLNLAENQLSHLPAWTRAVSLEVLDLRNNSFSLLPGNAMGGLETSLRRLYLQGNPLSCCGNGWLAAQLHQGRVDVDATQDLICRFGSQEELSLSLVRPEDCEKGGLKNVNLILLLSFTLVSAIVLTTLATICFLRRQKLSQQYKA
Protein: Forkhead box O4 (D4A433)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Cellular tumor antigen p53
- RAC-alpha serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
- Ataxin-3
- Serine/threonine-protein kinase Sgk1
- Ubiquitin carboxyl-terminal hydrolase 7
- Signal transducer and activator of transcription 3
- Tumor necrosis factor ligand superfamily member 6
- Cyclin-dependent kinase 2
Sequence:
MEPENKKSATEAAAIIDLDPDFEPQSRPRSCTWPLPRPELATEPPEPSEVEPSLGQKVPTEGHSEPTLLPSRLPEPAGGPQPEILGAVTGPRKGGSRRNAWGNQSYAELISQAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPDGGKGGKAPRRRAASMDSSSKLLRGRSKGPKKKPSVLPAPPEGATPRSPLGHFAKWSSSPCPRNREEADVWTTFRPRSSSNASTVSTRLSPMRPESEVLAEEEMPASASSYAGGVPPTLSEDLELLDGLNLASPHSLLSRSNLSSFSLQHPGLAGPLHSYGASLFGPIDGSLSAGEGCFSSSQSLEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGMPSSSKLATGVSLCPTPLEGPGPSNLVPTLSVMAPPPVMPGAPIPKVLGTPVLASPTEDFSHDRMPQDLDLDMYMENLECDMDNIISDLMDGEGLDFNFEPDP
Protein: Elongation of fatty acids protein (EC 2.3.1.-) (Q6FKW2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Acyl-CoA desaturase
- Elongation of fatty acids protein
- Candida glabrata strain CBS138 chromosome K complete sequence
- Very-long-chain
- beta-ketoacyl-[acyl-carrier-protein] synthase I
- 3-ketodihydrosphingosine reductase TSC10
- Candida glabrata strain CBS138 chromosome D complete sequence
Sequence:
MTTIIPLLKQYSAPVFERYPVLHNYVPTVEKPFFNINLWENFDHFVTLATNGKFIPSEFQFVAGELPLSELQPVLIAIATYYIVIFGGKFVLSYSKPFKLNGLFQLHNLFLTTISLTLLVLMVEQLTPMIYHHGLFYAICNEGAWTQPMVTLYYMNYIVKFIEFIDTLFLVLKHKKLTFLHTYHHGATALLCYTQLVGTTSISWVPISLNLGVHVVMYWYYFLAARGIRVWWKEWVTRFQIIQFILDIGFIYFAVYQKATHLYFPTLPHCGECVGSTTATFAGCAIISSYLVLFISFYINVYKRKGSKASRVVKRVHGGVAAKVNEYVNVDLQNVSTPSPSPVAKDRRRKR
Protein: MAM domain-containing glycosylphosphatidylinositol anchor protein 1 (Q0PMG2)
Organism: Mus musculus (Mouse)
Function: Required for radial migration of cortical neurons in the superficial layer of the neocortex. Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Associated with lipid rafts. {ECO:0000250|UniProtKB:Q8NFP4}.
Interaction partners:
- Neuroligin-2
- Neuroligin-1
- Neuroligin-3
Sequence:
MEVTCLLLLALIPFHCRGQGVYAPAQAQIVHAGQACVVKEDNISERVYTIRESDTLVLQCLVTGHPRPQVRWTKTAGSASDKFQETSVFNETLRIERIARTQGGRYYCKAENGVGVPAIKSIRVDVQYLDEPVLTVHQTVSDVRGNFYQEKTVFLRCTVSSNPPARFIWKRGSDTLSHSQDNGVDIYEPLYTQGETKVLKLKNLRPQDYASYTCQVSVRNVCGIPDKAITFQLTNTTAPPALKLSVNETLVVNPGENVTVQCLLTGGDPLPQLHWSHGPGPLPLGALAQGGTLSIPSVQARDSGYYNCTATNNVGNPAKKTVNLLVRSLKNATFQITPDMIKESENIQLGQDLKLSCHVDAVPQEKVNYQWFKNGKPARTSKRLLVTRNDPELPAVTSSLELIDLHFSDYGTYLCMASFPGSPVPDLSIEVNISSETVPPTISVPKGRAVVTVREGSPAELQCEVRGKPRPPVLWSRVDKEAALLPSGLALEETPDGKLRLESVSRDMSGTYRCQTARYNGFNVRPREAQVQLTVHFPPEVEPSSQDVRQALGRPVLLRCSLLRGSPQRIASAVWRFKGQLLPPPPVLPAAAVETPDHAELRLDALTRDSSGNYECSVSNDVGSATCLFQVSAKAYSPEFYFDTPNPTRSHKLSKNYSYVLQWTQREPDAVDPVLNYRLSIRQLNQHNAMVKAIPVRRVEKGQLLEYILTDLRVPHSYEIRLTPYTTFGAGDMASRIIHYTEPINLPSLSDNTCHFEDEKICGYTQDLTDNFDWTRQNALTQNPKRSPNTGPPTDISGTPEGYYMFIETSRPRELGDRARLVSPLYNASAKFYCVSFFYHMYGKHIGSLNLLVRSRNKGTLDTHAWSLSGNKGNVWQQAHVPINPSGPFQIIFEGVRGSGYLGDIAIDDVTLKKGECPRRQMDPNKVVVMPGSGAPRLSSLQLWGSMAIFLLALQR
Protein: Zinc finger protein 165 (Cancer/testis antigen 53) (CT53) (LD65) (Zinc finger and SCAN domain-containing protein 7) (P49910)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Mothers against decapentaplegic homolog 3
Sequence:
MATEPKKAAAQNSPEDEGLLIVKIEEEEFIHGQDTCLQRSELLKQELCRQLFRQFCYQDSPGPREALSRLRELCCQWLKPEIHTKEQILELLVLEQFLTILPGDLQAWVHEHYPESGEEAVTILEDLERGTDEAVLQVQAHEHGQEIFQKKVSPPGPALNVKLQPVETKAHFDSSEPQLLWDCDNESENSRSMPKLEIFEKIESQRIISGRISGYISEASGESQDICKSAGRVKRQWEKESGESQRLSSAQDEGFGKILTHKNTVRGEIISHDGCERRLNLNSNEFTHQKSCKHGTCDQSFKWNSDFINHQIIYAGEKNHQYGKSFKSPKLAKHAAVFSGDKTHQCNECGKAFRHSSKLARHQRIHTGERCYECNECGKSFAESSDLTRHRRIHTGERPFGCKECGRAFNLNSHLIRHQRIHTREKPYECSECGKTFRVSSHLIRHFRIHTGEKPYECSECGRAFSQSSNLSQHQRIHMRENLLM
Protein: Transcription factor EB (A0A2R8RRI1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serine/threonine-protein kinase TOR
- Autophagy-related protein 13
- Melanocyte-inducing transcription factor b
- Melanocyte inducing transcription factor a isoform 1
- Regulatory-associated protein of mTOR
- Beclin-1
- Ubiquitin-like modifier-activating enzyme ATG7
- Mucolipin TRP cation channel 1a
- Lysosomal-associated membrane protein 1b
- Ras-related GTP-binding A.
Sequence:
MSSRIGLRLQLMRDQMQQEEQRERQQQQAVSMHYMQHRMPGPPEPTPAISAPTHFQGPMQVPVEVLKVQTHLENPTDYHIRQSQRQQVKEYLSTTYATKQAVHAVTSLVQPSPPPMVQAQTGSAPPNMHSPCMRTEQLMNSAGNSAPNSPMAMLNISSSHENEMDDVIDNIISLQSSYDDIQAYNDPVVQMPNTLPLSSSHLDVYTGPGMSGSAIAMTSNSCPANLAIKRELSDVEARAMAKERQKKDNHNLIERRRRFNINDRIKELGTMIPKTNDLDVRWNKGTILRASVDYIKRMQKDVQRTREVENNFRRMEMANKQLWLRIQELERQAQIHGLPSNSPSGLTNTDHQNPFIKQESSPEENHLQHQSHLPPRYPQQHPQPHPQLHQHQHLHPQPPLQYPAVGSSQHFDLAQSLDLCDGGIPGYQDGLGDLGFLGGGIAQMGKKSELSFLLMEEALSPLGGDPLLSAMSPEASVDSSRRSSFSIEDSDIQ
Protein: Alpha-ketoglutarate-dependent xanthine dioxygenase xan1 (EC 1.14.11.48) (O74885)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate to succinate and CO(2) while hydroxylating xanthine to generate uric acid. Allows xanthine utilization as a nitrogen source.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:C8VSZ2}.
Interaction partners:
- Uricase
- Probable allantoicase
- Urease
- Uncharacterized urease accessory protein ureD-like
Sequence:
MSATATTTVVEPPTTTLTGATEPPFTAYTTSQGLRVSPVPLPEHNTDVGFGALIENVDLNNLSDEQFEDIRKALFEHQVVCFPNQHNLPPETQYAITHRFDPESSTYGHGNRTNQQNNSILHPDLHTLPGVPQVQLIGHGVVKDHYGLEEVRLKHPHHRTFHRDPISEEEEKEKQVTRFYRWHIDAALYDYNPPVVTTLLAVNAPQGTQTLRYDDKSGHEMPVPLGSTAFASGYRMYELLTDEEKKVAARTRVQYFPHAYVTINKARALPNGLGMYSEGLELDKSELPPWEESRVKTFPLLWKNPVTGKLALQTHGCCAEKILIDNEDGTTTVIDDLPKVREILYNYQRPGINPERVYCHDWKNGDFVIFHNRGVTHCITGAYRDDQTRIFHQCNLAASHPPAGPSEEDIAAM
Protein: Septin-7 (CDC10 protein homolog) (O55131)
Organism: Mus musculus (Mouse)
Function: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17546647}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q16181}. Note=Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase (By similarity). Associated with actin stress fibers. Found in the sperm annulus (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q16181}.
Interaction partners:
- Septin-6
- Septin-2
- Septin-9
- Neuronal-specific septin-3
- Septin-11
- Septin-5
- Septin-8
- Septin-4
- Septin-10
- Septin 12
Sequence:
MSVSARSAAAEERSVNCGTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEEEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
Protein: Cysteine-rich DPF motif domain-containing protein 1 (Q6NVV7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASHVECRPLGVFECELCTLTAPYSYVGQKPPNTQSMVLLEESYVMKDPFTSDKDRFLVLGSCCSLCSRLVCVGPECSLFYSKRFCLPCVRENINAFPQEIRQDLEKRKAPSKRTPSQPGSRT
Protein: Eukaryotic translation initiation factor 4E (X5D7E3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLDLTSRGQVGTSRRMAEAACSAHFLETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV
Protein: Protein BRICK1 (BRK1) (Q8WUW1)
Organism: Homo sapiens (Human)
Function: Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-binding protein WASF2
- Nck-associated protein 1
- Abl interactor 1
- Nck-associated protein 1-like
- Cytoplasmic FMR1-interacting protein 2
- Cytoplasmic FMR1-interacting protein 1
- Actin-binding protein WASF1
- Abl interactor 2
- Actin-binding protein WASF3
- Actin-related protein 2/3 complex subunit 3
Sequence:
MAGQEDPVQREIHQDWANREYIEIITSSIKKIADFLNSFDMSCRSRLATLNEKLTALERRIEYIEARVTKGETLT
Protein: 11S globulin (11S legumin) (allergen Jug n 4) [Cleaved into: 11S globulin acidic chain; 11S globulin basic chain] (A0A1L6K371)
Organism: Juglans nigra (Black walnut) (Wallia nigra)
Function: Seed storage protein.
Interaction partners:
Sequence:
MAKPILLSISLCLVALVNGCLAQSGGRQQPRFGECKLKRLVALEPSNRIEAEAGVIESWDPNNQQFQCAGVAVVRRTIEPNGLLLPQYSNAPQLLYIVKGRGITGVLFPGCPETFEESQQGQSRIRPSLRSASFQRDRHQKIRHFREGDVIAFPAGVAHWCYNDGDTPVVAVALMDTTNNANQLDQNPRNFYLAGNPDDEFRPQGQQEYEQHRRQQQHQQRHGEPGQQQRGSGNNVFSGFDADFLADAFNVDTETARRLQSENDHRRSIVRVEGRQLQVIRPRWSREEQEREERKERERERESESERRQSRRGGRDDNGLEETICTLRLRENIGDPSRADIYTEEAGRISTANSHTLPVLRWLQLSAERGALYSDALYVPHWNLNAHSVVYALRGRAEVQVVDNFGQTVFDDELREGQLLTIPQNFAVVKRARNEGFEWVSFKTNENAMVSPLAGRTSAIRALPEEVLANALQIPREDARRLKFNRQESTLVRSRPSSSRSSRSERRAEV
Protein: Syntaxin 16 (F8W9Z6)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004409}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004409}.
Interaction partners:
Sequence:
MALVSGISLDPEAAIGVTKRPPPKWVDGVDEIQYDVGRIKQKMKELASLHDKHLNRPTLDDSSEEEHAIEITTQEITQLFHRCQRAVQALPSRARACSEQEGRLLGNVVASLAQALQELSTSFRHAQSGYLKRMKNREERSQHFFDTSVPLMDDGDDNTLYHRGFTEDQLVLVEQNTLMVEEREREIRQIVQSISDLNEIFRDL
Protein: Oxaloacetate tautomerase FAHD1, mitochondrial (EC 5.3.2.2) (Acylpyruvase FAHD1) (EC 3.7.1.5) (Fumarylacetoacetate hydrolase domain-containing protein 1) (FAH domain-containing protein 1) (Oxaloacetate decarboxylase) (OAA decarboxylase) (ODx) (EC 4.1.1.112) (YisK-like protein) (Q6P587)
Organism: Homo sapiens (Human)
Function: Probable mitochondrial acylpyruvase which is able to hydrolyze acetylpyruvate and fumarylpyruvate in vitro. Also has oxaloacetate decarboxylase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21878618}. Cytoplasm, cytosol {ECO:0000269|PubMed:21878618}.
Interaction partners:
- Fumarylacetoacetase
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Homogentisate 1,2-dioxygenase
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Clustered mitochondria protein homolog
Sequence:
MAASRPLSRFWEWGKNIVCVGRNYADHVREMRSAVLSEPVLFLKPSTAYAPEGSPILMPAYTRNLHHELELGVVMGKRCRAVPEAAAMDYVGGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHKLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIITLEEGDIILTGTPKGVGPVKENDEIEAGIHGLVSMTFKVEKPEY