wanglab/gogpt-training-data huggingface dataset:
Protein: Capsid scaffolding protein (Capsid protein P40) (Protease precursor) (pPR) [Cleaved into: Assemblin (EC 3.4.21.97) (Protease) (Pr); Assembly protein (AP) (Capsid assembly protein)] (P54817)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular location: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.
Interaction partners:
Sequence:
MADAPDGGSADARVDAEPSALARASMPVYVGGYLALYGMGDEGELVLTREQVARALPPAAPLPINIDHASACEVGAVLALADDDAGLFFVGVINCPQLADTLAGVAHPAFFGADAPSLTPRERFLYLVSNYLPSVSLSSRRLAPDEEADGTLFAHVALCVLGRRVGTIVTYDATPDACVAPFRRLSPRARAALLANAEAARAALGDRAWPVPREALAQTLLSTAVNNMLVRDKWDTVSRRRREAGIAGHTYLQASAVFPLPTGGEGPERTGGRERAQKSAVAGGVCIALPVAGGRARQPELPPAPPPPPPPPAMSAAHQAGAASAHPLPAGDYVYVPTAQYNQLVVSQARGAAMTAAPPPAPYFLPAAAAAAAAPPPMPGWYGAAGAAPWHPGYGFPPPGLESQIMALAGAIADGRRVQAHGADGSGYDGPLDRRPLAKRRRYNWDHPRGRSGGGDDDEAYYPGEGAPAELPPHHHSPPPPHPPPSHALSKLASAVSSLQQEVSQLRAGYPYGPAFAAAQHPPAAHLPCLPQQYTAPPRVGAGPAQVPTLAPAQAPAQALSVPAVAAAPATVAAAAAVGPPEEPGVAATVDASAMASLPPAQPPQACDPAEIFVAQMMRQR
Protein: Lysocardiolipin acyltransferase 1 (EC 2.3.1.-) (1-acylglycerol-3-phosphate O-acyltransferase 8) (1-AGP acyltransferase 8) (1-AGPAT 8) (EC 2.3.1.51) (Acyl-CoA:lysocardiolipin acyltransferase 1) (Q6UWP7)
Organism: Homo sapiens (Human)
Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (By similarity). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors (By similarity). Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities. Required for establishment of the hematopoietic and endothelial lineages (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19075029}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Tafazzin
- Cardiolipin synthase
- Lysophospholipid acyltransferase LPCAT4
- Membrane-bound glycerophospholipid O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Lysophosphatidylcholine acyltransferase 2
- Lysophosphatidylcholine acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Phosphatidate cytidylyltransferase 2
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase MBOAT7
Sequence:
MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAMCLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE
Protein: E3 ubiquitin-protein ligase IpaH2.5 (EC 2.3.2.27) (Invasion plasmid antigen 2.5) (A0A0H2USC0)
Organism: Shigella flexneri
Function: E3 ubiquitin-protein ligase effector that inhibits host cell innate immunity during bacterial infection by catalyzing 'Lys-48'-linked polyubiquitination and subsequent degradation of host RNF31/HOIP. Host RNF31/HOIP is the catalytic component of the LUBAC complex, which conjugates linear ('Met-1'-linked) polyubiquitin chains at the surface of bacteria invading the host cytosol to form the ubiquitin coat surrounding bacteria. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8VSC3}. Host cytoplasm {ECO:0000250|UniProtKB:Q8VSC3}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:Q8VSC3}.
Interaction partners:
Sequence:
MIKSTNIQVIGSGIMHQINNIHSLTLFSLPVSLSPSCNEYYLKVWSEWERNGTPGEQRNIAFNRLKICLQNQEAELNLSELDLKTLPDLPPQITTLEIRKNLLTHLPDLPPMLKVIHAQFNQLESLPALPETLEELNAGDNKIKELPFLPENLTHLRVHNNRLHILPLLPPELKLLVVSGNRLDSIPPFPDKLEGLALANNFIEQLPELPFSMNRAVLMNNNLTTLPESVLRLAQNAFVNVAGNPLSGHTMRTLQQITTGPDYSGPQIFFSMGNSATISAPEHSLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLA
Protein: U3 small nucleolar RNA-associated protein 21 (U3 snoRNA-associated protein 21) (U three protein 21) (Q06078)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15590835}.
Interaction partners:
- Pre-rRNA-processing protein PNO1
- U3 small nucleolar RNA-associated protein 15
- Ribosome biogenesis protein BMS1
- Nucleolar protein 56
- rRNA biogenesis protein RRP5
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 11
- U3 small nucleolar ribonucleoprotein protein LCP5
- U3 small nucleolar ribonucleoprotein protein IMP3
- Protein BFR2
Sequence:
MSIDLKKRKVEEDVRSRGKNSKIFSPFRIIGNVSNGVPFATGTLGSTFYIVTCVGKTFQIYDANTLHLLFVSEKETPSSIVALSAHFHYVYAAYENKVGIYKRGIEEHLLELETDANVEHLCIFGDYLCASTDDNSIFIYKKSDPQDKYPSEFYTKLTVTEIQGGEIVSLQHLATYLNKLTVVTKSNVLLFNVRTGKLVFTSNEFPDQITTAEPAPVLDIIALGTVTGEVIMFNMRKGKRIRTIKIPQSRISSLSFRTDGSSHLSVGTSSGDLIFYDLDRRSRIHVLKNIHRESYGGVTQATFLNGQPIIVTSGGDNSLKEYVFDPSLSQGSGDVVVQPPRYLRSRGGHSQPPSYIAFADSQSHFMLSASKDRSLWSFSLRKDAQSQEMSQRLHKKQDGGRVGGSTIKSKFPEIVALAIENARIGEWENIITAHKDEKFARTWDMRNKRVGRWTFDTTDDGFVKSVAMSQCGNFGFIGSSNGSITIYNMQSGILRKKYKLHKRAVTGISLDGMNRKMVSCGLDGIVGFYDFNKSTLLGKLKLDAPITAMVYHRSSDLFALALDDLSIVVIDAVTQRVVRQLWGHSNRITAFDFSPEGRWIVSASLDSTIRTWDLPTGGCIDGIIVDNVATNVKFSPNGDLLATTHVTGNGICIWTNRAQFKTVSTRTIDESEFARMALPSTSVRGNDSMLSGALESNGGEDLNDIDFNTYTSLEQIDKELLTLSIGPRSKMNTLLHLDVIRKRSKPKEAPKKSEKLPFFLQLSGEKVGDEASVREGIAHETPEEIHRRDQEAQKKLDAEEQMNKFKVTGRLGFESHFTKQLREGSQSKDYSSLLATLINFSPAAVDLEIRSLNSFEPFDEIVWFIDALTQGLKSNKNFELYETFMSLLFKAHGDVIHANNKNQDIASALQNWEDVHKKEDRLDDLVKFCMGVAAFVTTA
Protein: Ovalbumin upstream promoter-transcription factor II variant 1 (F1D8R0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MAMVVSTWRDPQDEVPGSQGSQASQAPPVPGPPPGAPHTPQTPGQGGPASTPAQTAAGGQGGPGGPGSDKQQQQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLSYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPTHGQFALTNGDPLNCHSYLSGYISLLLRAEPYPTSRFGSQCMQPNNIMGIENICELAARMLFSAVEWARNIPFFPDLQITDQVALLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDVAHVESLQEKSQCALEEYVRSQYPNQPTRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMAIQ
Protein: SCAN box domain-containing protein (Q9CTS7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
MAVALGCAIQASLNQGSVLQEYDTDCEVFRQRFRQFQYTEAAGPHEAFNKLWELCCQWLKPKMRSKEQILELLVLEQFLTILPTEIETWVREHCPDNRERVVSLIEDLQRELEIPEPQIDMDDMLLEELAPVGTVPMPPNLHLEEPSLQVMEPVQEPPVPDAWIPQAGPQDLNYSADAECQSFLDPGYQLPKLDMNFPLDHREEPWVKDLEDPKEMKQLLDSKIGFEMG
Protein: N-acylneuraminate-9-phosphatase (EC 3.1.3.29) (Haloacid dehalogenase-like hydrolase domain-containing protein 4) (N-acetylneuraminate-9-phosphate phosphatase) (Neu5Ac-9-Pase) (Q5M969)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- N-acetylneuraminate-9-phosphate synthase
- N-acylneuraminate cytidylyltransferase
- Radial spoke head 3
- Cytidine monophospho-N-acetylneuraminic acid hydroxylase, pseudogene
- Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Sequence:
MGLSRVRAVFFDLDNTLIDTAGASRRGMLEVIKLLQSKYHYKEEAEVICDKVQVKLSKECFHPYSTCITDVRTSHWEEAIQETKGGADNRKLAEECYFLWKSTRLQHMTLEEDVKAMLTELRKEVRLLLLTNGDRQTQREKIEACACQSYFDAIVVGGEQKEEKPAPSIFYHCCDLLGVQPGDCVMVGDTLETDIQGGLNAGLKATVWINKSGGVPLTSSPMPHYMVSSVLELPALLQSIDCKVSMSV
Protein: WAP four-disulfide core domain protein 6 (Putative protease inhibitor WAP6) (Q9BQY6)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- WAP four-disulfide core domain protein 8
- Kunitz-type protease inhibitor 4
Sequence:
MGLSGLLPILVPFILLGDIQEPGHAEGILGKPCPKIKVECEVEEIDQCTKPRDCPENMKCCPFSRGKKCLDFRKIYAVCHRRLAPAWPPYHTGGTIKKTKICSEFIYGGSQGNNNNFQTEAICLVTCKKYH
Protein: Pikachurin (EGF-like, fibronectin type-III and laminin G-like domain-containing protein) (Nectican) (Q4VBE4)
Organism: Mus musculus (Mouse)
Function: Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743}. Synaptic cleft {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:30282023}. Presynaptic active zone {ECO:0000269|PubMed:18641643}. Note=Detected in the synaptic cleft of the ribbon synapse around the postsynaptic terminals of bipolar cells (PubMed:18641643). Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic terminals (PubMed:18641643). {ECO:0000269|PubMed:18641643}.
Interaction partners:
- Dystroglycan 1
- G-protein coupled receptor 179
- Dystrophin
- Protein O-mannosyl-transferase 2
- Protein O-mannosyl-transferase 1
- C-terminal-binding protein 2
Sequence:
MDLISTFSLHFLLLACSLPPGAVSLRTALRKSGKVGPPLDIKLGALNCTAFSIQWKTPKRSGSSIIGYTVFYSEVGSDKSLRERSHNVPVGQDTLITEEVIGDLKPGTEYQVSVAAYSQTGKGRLSFPRHVTTLSQDSCLPPAAPQQPHVLVVSDSEVALSWRPGENEGSAPIQSYSVEFIRPDFDKSWTIIQERLQMDSMVIKGLDPDTNYQFAVKAMNAHGFSPRSWPSNTVRTLGPGEAGSGHYGPGYITNPGVSEDDDGSEDELDLDVSFEEVKPLPATKVGNKKFSVESKKTSVSNSVMGSRLAQPTSASLHETTVAIPPTPAQRKGKNSVAMMSRLFDMSCDETLCSADSFCVNDYAWGGSRCHCNLGKGGEACSEDIFIQYPQFFGHSYVTFEPLKNSYQAFQVTLEFRAEAEDGLLLYCGESEHGRGDFMSLALIRRSLHFRFNCGTGIAIIISETKIKLGAWHTVTLYRDGLNGMLQLNNGTPVTGQSQGQYSKITFRTPLYLGGAPSAYWLVRATGTNRGFQGCVQSLSVNGKKIDMRPWPLGKALNGADVGECSSGICDEASCIHGGTCAAIKADSYICLCPLGFRGRHCEDAFALTIPQFRESLRSYAATPWPLEPQHYLSFTEFEITFRPDSGDGVLLYSYDTGSKDFLSINMAAGHVEFRFDCGSGTGVLRSEAPLTLGQWHDLRVSRTAKNGILQVDKQKVVEGMAEGGFTQIKCNTDIFIGGVPNYDDVKKNSGILHPFSGSIQKIILNDRTIHVKHDFTSGVNVENAAHPCVGAPCAHGGSCRPRKEGYECDCPLGFEGLNCQKECGNHCLNTIIEAIEIPQFIGRSYLTYDNPNILKRVSGSRSNAFMRFKTTAKDGLLLWRGDSPMRPNSDFISLGLRDGALIFSYNLGSGVASIMVNGSFSDGRWHRVKAVRDGQSGKITVDDYGARTGKSPGLMRQLNINGALYVGGMKEIALHTNRQYLRGLVGCISHFTLSTDYHISLVEDAVDGKNINTCGAK
Protein: ADP-ribosylation factor-like protein 2-binding protein (ARF-like 2-binding protein) (Binder of ARF2 protein 1) (Q4V8C5)
Organism: Rattus norvegicus (Rat)
Function: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity). {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor-like protein 2
- Cilia- and flagella-associated protein 20
- ADP-ribosylation factor-like protein 13A
Sequence:
MDALEEESFALSFSSASDAEFDAVVGCLEDIIMDAEFQLLQRSFMDKYYQEFEDTEENKLTYTPIFNEYISLVEKYIEEQLLERIPGFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSTPASQNNLRH
Protein: DNA mismatch repair protein (E9PHA6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005813}.
Interaction partners:
Sequence:
MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLERENLRVTEPKDQCLILLTWKRKLRGGKRSACSRPERQNQGSGELS
Protein: Glycerophosphodiester phosphodiesterase domain-containing protein 5 (Glycerophosphocholine phosphodiesterase GDPD5) (EC 3.1.4.2) (Glycerophosphodiester phosphodiesterase 2) (Phosphoinositide phospholipase C GDPD5) (EC 3.1.4.11) (Q3KTM2)
Organism: Gallus gallus (Chicken)
Function: Glycerophosphodiester phosphodiesterase that promotes cell cycle exit and drives spinal motor neuron differentiation. Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane. May contribute to the osmotic regulation of cellular glycerophosphocholine (By similarity).
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:Q640M6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q640M6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q640M6}.
Interaction partners:
Sequence:
MVKHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTKWERLWFLILTSSFFLTLVWFYFWWEVHNDYNEINWFLYNRMGYWSDWSIPILVTTAAGFTYITVLLILALCHIAVGQQMNLHWLHKIGLMTTLITTVVTMSSIAQLWDDEWEMVFISLQATAPFLHIGALAAVTALSWLIAGQFARMEKATSQMLMVTAYLAVVVALYLVPLTISSPCIMEKKALGPKPAIIGHRGAPMLAPENTLMSFQKAVEQKIYGVQADVILSYDGVPFLMHDKTLRRTTNVEEVFPGRAYEHSSMFNWTDLEMLNAGEWFLRNDPFWTAGSLSRSDYLEAANQSVCKLADMLEVIKDNTSLILNFQDLPPDHPYYTSYINITLKTILASGIQQQAVMWLPDTERQLVRQIAPAFQQTSGLKLDAERLREKGIVKLNLRYTKVTNEDVRDYMAANLSVNLYTVNEPWLYSILWCTGVPSVTSDSSHVLRKVPFPIWLMPPDEYRLIWITSDLISFIIIVGVFIFQNYHNDQWRLGSIRTYNPEQIMLSAAVRRSSRDVKIMKEKLIFSEINNGVETTDELSLCSENGYANEMVTPTDHRDTRLRMN
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 (6PF-2-K/Fru-2,6-P2ase 4) (PFK/FBPase 4) (6PF-2-K/Fru-2,6-P2ase testis-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (Q16877)
Organism: Homo sapiens (Human)
Function: Synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- ATP-dependent 6-phosphofructokinase, muscle type
- Fructose-1,6-bisphosphatase isozyme 2
- ATP-dependent 6-phosphofructokinase, platelet type
- Fructose-2,6-bisphosphatase TIGAR
- ATP-dependent 6-phosphofructokinase, liver type
- Fructose-1,6-bisphosphatase 1
- Mannose-6-phosphate isomerase
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- Hexokinase-2
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
Sequence:
MASPRELTQNPLKKIWMPYSNGRPALHACQRGVCMTNCPTLIVMVGLPARGKTYISKKLTRYLNWIGVPTREFNVGQYRRDVVKTYKSFEFFLPDNEEGLKIRKQCALAALRDVRRFLSEEGGHVAVFDATNTTRERRATIFNFGEQNGYKTFFVESICVDPEVIAANIVQVKLGSPDYVNRDSDEATEDFMRRIECYENSYESLDEDLDRDLSYIKIMDVGQSYVVNRVADHIQSRIVYYLMNIHVTPRSIYLCRHGESELNLKGRIGGDPGLSPRGREFAKSLAQFISDQNIKDLKVWTSQMKRTIQTAEALGVPYEQWKVLNEIDAGVCEEMTYEEIQDNYPLEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKAAEQLPYLKCPLHTVLKLTPVAYGCKVESIFLNVAAVNTHRDRPQNVDISRPPEEALVTVPAHQ
Protein: Spindle assembly checkpoint component mad1 (Mitotic arrest deficient protein 1) (P87169)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Central component of the spindle assembly checkpoint. Has a role in the correct positioning of the septum. Required for anchoring mad2 to the nuclear periphery.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mitotic spindle checkpoint component mad2
- WD repeat-containing protein slp1
- Mitotic spindle checkpoint component mad3
- Origin recognition complex subunit 2
- Spindle assembly checkpoint serine/threonine-protein kinase bub1
- Serine/threonine-protein kinase mph1
- Spindle assembly checkpoint protein bub3
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 4
Sequence:
MSSKLTVYQATTSMADSPRDPFQSRSQLPRFLATSVKKPNLKKPSVNSANETKNPKLASLEFQLENLKNDLKRKELEFEREQIELQRKLAEEHEQKNSLQLRLTLVEKQLEEQSTSYQKEIEEVRNEKEATQVKIHELLDAKWKEIAELKTQIEKNDQALSEKNHEVMVSNQALQMKDTNLTNLEKLFADSREQLETKCKELAAAEQQLQELSVHNQQLEESIKQVSSSIELEKINAEQRLQISELEKLKAAQEERIEKLSSNNRNVEILKEEKNDLESKLYRFEEYRDKVATLELENEKIQTELNSWKSLITNELPTPEAVSNKLVFLQNTNANLGERVSSLESQLSNKPANQPLGANEKDAAHITELETKLKELHEQNRRLQRQKSLATQEIDLLRENLKSYDDEEAILSEKNTDMKKLERIEGLVKLVDEYKLKLESMPVSLDVDETSDEVSLQKRRRKNEHKDAGYVTELYRKNQHLLFQVKEKTNIEAFLREQIITLESSIATLRQELAQVTEINSCRVLQHRSNPTLKYERIKAAQLEMLNAENSALKALLEDKKVDCLPIQSFKIAERKALDLKKEVAEREKRIQRLKEIFSVKSLEFREAVFSLFGYKLDFMPNGSVRVTSTYSREDNTAFIFDGESSTMKLVGNPSGPEFERLIRFWCDERKTIPGMLAALTLELLDKND
Protein: Ghrelin O-acyltransferase (EC 2.3.1.-) (Membrane-bound O-acyltransferase domain-containing protein 4) (B1Q006)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (By similarity). In vitro uses also acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}.
Interaction partners:
- Appetite-regulating hormone isoform X1
- Growth hormone secretagogue receptor type 1
- Growth hormone secretagogue receptor type 1
- O-acyltransferase
- Motilin-like
- O-acyltransferase.
- O-acyltransferase
Sequence:
MIDLLWISSDGHPQLFYQFINIPFAFLFHCLSSQGHLSIINRYVYLAMGGFMLAIATMGPYSSLLFLSAIKLLLLIHYIHPMHLHRWILGLQMCWQTCWHLYVQYQIYWLQEAPDSRLLLAISALMLMTQRISSLSLDFQEGTISNQSILIPFLTYSLYFPALLGGPLCSFNAFVQSVERQHTSMTSYLGNLTSKISQVIVLVWIKQLFSELLKSATFNIDSVCLDVLWIWIFSLTLRLNYYAHWKMSECVNNAAGLGVYFHKHSGQTSWDELSDGSVLVTEASSRPSVFARKWNQTTVDWLRKIVFNRTSRSPLFMTFGFSALWHGLHPGQILGFLIWAVTVQADYKLHRFSHPKLNSLWRKRLYVCVNWAFTQLTVACVVVCVELQSLASVKLLWSSCIAVFPLLSALILIIL
Protein: Tyrosine aminotransferase (EC 2.6.1.5) (Q4Q1I5)
Organism: Leishmania major
Interaction partners:
- Aspartate aminotransferase
- S-adenosylmethionine synthase
- Transaminase A
- phenylalanine 4-monooxygenase
- Putative 1,2-Dihydroxy-3-keto-5-methylthiopentene dioxygenase
- Acireductone dioxygenase-requiring))
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Methionine synthase
- Putative homocysteine S-methyltransferase
Sequence:
MTIDAQAAPAAQALKASNSTGSLTEERREVEQRVAENASFRRITSSKHAQRTLQPLNNLADNMKPSRSTKSNLRLSIGDPTVDGNLKIPEIVTEAVVDVVRSGEFNGYPPTVGADNLRQVVSTYWRRFCQTKSRQEALKWENVIITSGVSQAIVLALTALCNEGDNILVCAPSFPHYKSVCESYGIECRYYYLDPSKSWECDLRSAAGAVDRHTKAFVIINPSNPCGSNFSRAHVSDIIDFCQHHQIPLISDEIYAEMVLNNGIFTSVADFDTSVPRLILGGTAKYQVCPGWRVGWSILIDPMNVAGDWAVGMERLTQLIAGVNSICQEAIARTLLKCPTECTEHIVTQLEAGAKVYARLLEHDIGISMDAPQASMFVMLKLNLSYFQDLKSDMEFYEKLLDEENVQVLPGEIFGMSGFIRATISRPSAVLNEAVDRIIEFCERHKK
Protein: Protein MIS12 homolog (Q9H081)
Organism: Homo sapiens (Human)
Function: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis. Essential for proper kinetochore microtubule attachments.
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12515822, ECO:0000269|PubMed:15502821}. Note=Associated with the kinetochore. {ECO:0000269|PubMed:12515822, ECO:0000269|PubMed:15502821}.
Interaction partners:
- Polyamine-modulated factor 1
- Kinetochore-associated protein DSN1 homolog
- Kinetochore-associated protein NSL1 homolog
- Outer kinetochore KNL1 complex subunit KNL1
- Centromere protein C
- Kinetochore protein Spc24
- Kinetochore protein NDC80 homolog
- Outer kinetochore KNL1 complex subunit ZWINT
- Kinetochore protein Nuf2
- Kinetochore protein Spc25
Sequence:
MSVDPMTYEAQFFGFTPQTCMLRIYIAFQDYLFEVMQAVEQVILKKLDGIPDCDISPVQIRKCTEKFLCFMKGHFDNLFSKMEQLFLQLILRIPSNILLPEDKCKETPYSEEDFQHLQKEIEQLQEKYKTELCTKQALLAELEEQKIVQAKLKQTLTFFDELHNVGRDHGTSDFRESLVSLVQNSRKLQNIRDNVEKESKRLKIS
Protein: Short-chain specific acyl-CoA dehydrogenase, mitochondrial (SCAD) (EC 1.3.8.1) (Butyryl-CoA dehydrogenase) (Q3ZBF6)
Organism: Bos taurus (Bovine)
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (By similarity). Among the different mitochondrial acyl-CoA dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 4 to 6 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:6712627}.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- Enoyl-CoA delta isomerase 2
- Acetyl-CoA acyltransferase 1
- Trifunctional enzyme subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Enoyl-CoA delta isomerase 1, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Acetyl-CoA acyltransferase 2
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Ethylmalonyl-CoA decarboxylase
Sequence:
MAATLLARACGLVRGAPWPWGWRRLHTVYQSVELPETHQMLRQTCRDFAEKELFPIAAQVDKEHRFPAAQVKKMGELGLMAMNVPEELSGAGLDYLAYSIAMEEISRGCASTGVIMSVNNSLYLGPILKFGTKEQKQQWVAPFTSGDKIGCFALSEPGNGSDAGAAATTARADGDSWVLSGTKAWITNAWEASAVVVFASTDRSLHNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDRRIPKDSLLGEPGLGFKIAMQTLDTGRIGIASQALGIAQAALDCAVTYAENRSAFGAPLTKLQAIQFKLADMALALESARLLTWRAAMLKDNKKPFTKEAAMAKLAASEAATAITHQAMQILGGMGYVKEMPAERHYRDARITEIYEGTSEIQRLVVAGHLLKSYRS