wanglab/gogpt-training-data huggingface dataset:
Protein: Probable cation-transporting ATPase 13A4 (EC 7.2.2.-) (P5-ATPase isoform 4) (Q5XF90)
Organism: Mus musculus (Mouse)
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGDHLEKSQHALLNEGDENEMEIFGYRTQGCRKALCLIGSIFSLGMLPLVFYWRPAWRVWANCVPCSLQEADVVLLKTTDEFKIYSWKKVIWISLSALSSTSGLTPDHPLITDEGYIINRAIRKPDLKVRYIKVQKIRYVWNNLEGQFQKIGSLEDWLSSAKIHQKFGLGLTSEEQEIRRLICGPNAIDVEITPIWKLLIKEVLNPFYIFQLFSVCLWFSEDYKEYALAIILMSVISIALTVYDLRQQSVKLHHLVESHNSITVSVYERKAGAQDLESRLLVPGDLLILTGSRVQMPCDAILIDGSCVVDEGMLTGESIPVTKTPLSQTASSVPWKMQSEADPRRHVLFCGTEVIQAKAAGSGAVRAVVLQTGFNTAKGDLVRSILYPKPMNFKLYRDAIRFLLCLVGTATIGMVYTLCVYVLSGEPPEEVVRKALDVITIAVPPALPAALTTGIIYAQRRLKKKGIFCISPQRINVCGQLNLVCFDKTGTLTRGGLDPWGVVPCDQNGFQAVHSFASGKALPQGPLCAAMASCHSLILLDGTIQGDPLDLKMFEATKWEMTASGDDLHIKEMLAHTIVVKPTDMVGQVPAEGLAIVHQFPFSSALQRMTVIVQEMGGGRLAFMKGAPERVASFCQPDTVPTSFISELQIYTTQGFRVIALAYKKLEMDCPTTALMREKVESDLVFLGLLILENRLKEETKPVLEELISARIRTVMITGDNLQTAITVARKSGMVSEGQKVILVEANEATGSSSASISWKLVEEKKPGPFGSQDTYINIREEVPENGRDRSYHFALSGKSFHVISQYFSSLLPKILINGTIFARMSPGQKSSLVEEFQKLDYFVGMCGDGANDCGALKMAHVGISLSEQEASVASPFTSKTPNIECVPHLIKEGRAALVTSFCMFKYMALYSMIQYVGVLLLYWKTNSLSNYQFLFQDLAITTLIGVTMNLNGANPKLVPFRPAGRLISPPLLLSVVLNILLSLAMHIVGFILVQKQPWYIMDYHSVCPVRNESASALAASPSVPEKTRSNSTFASFENTTIWFLGTINCIFVALVFSKGKPFRQPTYTNYIFVLVLILQMGVCLFILFADIPEMHRRLDLLCTPVLWRVYILIMISSNFVVSLAVEKAIIENRALWIAVKRCFGYQSKSQYRIWQRNLANDSSWPPLNQTSYSDMQGVSYSNPVFESNEEQL
Protein: Gem-associated protein 4c (Gemin4c) (Q8IRS9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RNA helicase
- Gem-associated protein 5
- Survival motor neuron protein
- Gem-associated protein 4b
- Gem-associated protein 2
- Gem-associated protein 4a
- Ribonucleoside-diphosphate reductase large subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- COMM domain-containing protein 10 homolog Vlet
- LSM12 homolog B
Sequence:
MITAEKHPLDNCQLFVQLKKIFHDNNEQAKCLKDMIYWSGNDEHIEKICDQVTDLLEEHDLIIQPPDTMDPFAMNQLRGLLVYLVLNTAHDYFLCKSQWSANVMHLCNQLPPIPLFLTIAIAVNCCLMEPLEEFLACGPRWLTIQYFEAFNEALSVINSDCVETLPLLSAALRAAGRAIVNCNLPAENKQLLRQIACMEHRHILDSKQRLHTLPRPSTRKIYLAKAMDHLIEVLLYTLNDPLKREKPNCFAVYSQITEDISDSNSSDPMPDLRHFAQILLDVLRRIFQLVSVDTYMYWHEMKSKSALYNCQELICRQTAELLKVLQSDNMLGEHPVCKQMQSFADAAKTLEQRVAEMRMGELLVFLDSGMATDEELLAGLDNLFSRFIAFGNDECVETMANHLIMLTKKHAQIILSFLGQVVESEMVVEDEGISVTEVNQGDDEDETSSNDDYEELLSLVLRPLFMQLNVEDKMEVLLLRDEQNVTQGFNFKAPDHRERRIRFFNQLDYNKRFPITKFLVLCFENARQTWIDFSHLGVTHTRFSKLFWHIAQSCPKHAAFHISACADNILVNEQLLQKPYALQFTLYLYGHRQILNGLYTSARQLCVSLKDGRCPYGEDELRQAQNRFLDACAYGLAKFIEPMNLPSLQLILKLLKQISLGESNLITRGTAELNALEKEHPKLENGDDAPAVKVAKHYTYLNASLPEWRLKHWKLISHVMKTIDALRWDLATFEDFRVDNLELAVWYWQDGLSHLTFLGTECRQRILNQVNSLKHKGFWLIYLKEDTLKDTRSFLKLLTQSSAQEANDLFKKLLKKRADCAVMGDLSDAVVKVNSESAFMAFRFLFREYLIAFRSHAKHNKTITKRQHWDHLMAVVAKAPFSIRNEIMKLASKAFAVRFGINIQEQQAAKC
Protein: Branch point binding protein, putative (Q38A35)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- SURP motif domain-containing protein
- Probable eukaryotic initiation factor 4A
- Cell division control protein, putative
- Splicing factor 3A, putative
- Uncharacterized protein
- Uncharacterized protein
- Splicing factor 3B subunit 1, putative
- Pre-mRNA-splicing factor U5-Cwc21
Sequence:
MGENRRPSRWSSERYTNLFVPNYIPPELMLYDEGQFLRAFLLRVLSIDLNRLIETKRCGDYFINIPLVPEYNSEGQRTNTPDELVAEKRLKVMDELTNLLRQHSELELNAKTQKEVVRKRYFTQEEMDNGAYGAILGARGMVHQELERLTKCKIVLAGRGITNALKDTSANAARVALEDPHARITAPNEQALQHAMERIEWILSDDPEALEFRENNRKRMAQIEGRYDPRTWVSLAERNAKNPRRMGEKREREEEAKEELDADLQEFLDEL
Protein: Palmitoyltransferase (EC 2.3.1.225) (X2J6Q6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}.
Interaction partners:
Sequence:
MLIAFQDRLRLPWRGGAKRISPAAVAPAFIVPLMLGLATLNSKTAIVLMLTLVGFTIWGMELAKRTATRTNFFLSWLVFSVFYMIIIFEFQVPLLELAPEENYALMFFSCAALYCLYSAKALSPLNLVSAQYGTTPKDELPGIAEASSGEEQAEAQTTLQMESVLSLDDDEVGDMDTAERSGLMHGQPNICEICRKVTPRRAYHCPVCGTCVKRRDHHSYWLNCCIGERNYVWYIVGLALSEIALLLGANLTLTSICHPFMVVRPLGYPVLLPDDCSEVFEGFDLGISFVVACYALLISSYIAFILARQAYLWWKGSTLHEYKRTSNAAGRNRIWSNWRAILK
Protein: Transmembrane glycoprotein NMB (Q6P7C7)
Organism: Rattus norvegicus (Rat)
Function: Could be a melanogenic enzyme.
Subcellular location: Cell membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Melanosome membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Early endosome membrane; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:Q14956}.
Interaction partners:
- Receptor protein-tyrosine kinase
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Tyrosine-protein kinase
- Syndecan-4
- Galectin-3
- Triggering receptor expressed on myeloid cells 2
Sequence:
MESLCGVLVFLLLAAGLPLQAAKRFRDVLGHEQYPDHMRENNQLRGWSSDENEWDEQLYPVWRRGEGRWKDSWEGGRVQAALTSDSPALVGSNITFVVNLVFPRCQKEDANGNIVYERNCRSDLELASDPYVYNWTTGADDEDWEDSTSQGQHLRFPDGKPFPRPHGRKKWNFVYVFHTLGQYFQKLGRCSARVSINTVNLTVGPQVMEVIVFRRHGRAYIPISKVKDVYVITDQIPIFVTMYQKNDRNSSDETFLRDLPIFFDVLIHDPSHFLNYSAISYKWNFGDNTGLFVSNNHTLNHTYVLNGTFNFNLTVQTAVPGPCPSPTPSPSSSTSPSPASSPSPTLSTPSPSLMPTGHKSMELSDISNENCRINRYGYFRATITIVDGILEVNIIQVADVPIPTPQPDNSLMDFIVTCKGATPTEACTIISDPTCQIAQNRVCSPVAVDELCLLSVRRAFNGSGTYCVNFTLGDDASLALTSALISIPGKDLGSPLRTVNGVLISIGCLAMFVTMVTILLYKKHKTYKPIGNCTRNVVKGKGLSVFLSHAKAPFSRGDREKDPLLQDKPWML
Protein: Beta-1,3-xylanase TXYA (EC 3.2.1.32) (Endo-1,3-beta-xylanase) (Q9LCB9)
Organism: Vibrio sp
Function: Catalyzes the hydrolysis of beta-1,3-xylan into oligosaccharides, mainly xylotriose and xylobiose with smaller amounts of xylotetraose, xylose, xylopentaose and xylohexaose. Weakly active toward beta-1,3-xylotriose, yielding xylose and xylobiose. Converts beta-1,3-xylotetraose into xylotriose, xylobiose and xylose. Converts beta-1,3-xylopentaose into xylotetraose, xylotriose, xylobiose and xylose. Does not hydrolyze xylobiose, p-nitrophenyl-beta-xyloside, beta-1,4-xylan, curdlan or carboxymethylcellulose.
Interaction partners:
Sequence:
MKKLAKMISVATLGACAFQAHALDGKLVPDQGILVSVGQDVDSVNDYSSAMGTTPAGVTNYVGIVNLDGLSTDADAGAGRNNIVELANQYPTSALIVGVSMNGEVQNVANGQYNANIDTLIRTLGEFDRPVYLRWAYEVDGPWNGHNTEDLKQSFRHVYQRIRELGYADNISMVWQVASYCPTAPGQLGTWWPGDDVVDWVGLSYFAPQDCNWDRVNEAAQWARSHNKPLFINESSPQRYQLADLTYSTDPAKGTNRQAKTDQQIWSEWFEPFFQFMVDNQDILKGFTYINADWDSQWRWAAPYNEGYWGDSRVQVIPYIKQKWQETLSDPKFIRHSDELFAQLGYGNSDGGNGGDNGGDNGGDNGGETPENCTDDFNFNYVSDNEIEVYHVDKGWSAGWNYLCLDDYCLSGTKSNGAFSRSFSAQLGQTYKMTFKVEDITGQGQQIIDKTVTFTNQVCN
Protein: Transcription factor SOX-5 (P35710)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in chondrocytes differentiation and cartilage formation. Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes, such as COL2A1 and AGC1. Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes. Together with SOX6, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts. Binds to the proximal promoter region of the myelin protein MPZ gene.
Subcellular location: Nucleus {ECO:0000269|PubMed:9755172}.
Interaction partners:
- Transcription factor SOX-6
- Transcription factor SOX-9
- Fez family zinc finger protein 2
- Catenin beta-1
- Sulfhydryl oxidase 1
- Collagen alpha-1
- DNA-binding protein SATB2
- Aggrecan core protein
Sequence:
MLTDPDLPQEFERMSSKRPASPYGETDGEVAMVTSRQKVEEEESERLPAFHLPLHVSFPNKPHSEEFQPVSLLTQETCGPRTPTVQHNTMEVDGNKVMSSLSPYNSSTSPQKAEEGGRQSGESVSSAALGTPERRKGSLADVVDTLKQRKMEELIKNEPEDTPSIEKLLSKDWKDKLLAMGSGNFGEIKGTPESLAEKERQLMGMINQLTSLREQLLAAHDEQKKLAASQIEKQRQQMELAKQQQEQIARQQQQLLQQQHKINLLQQQIQVQGQLPPLMIPVFPPDQRTLAAAAQQGFLLPPGFSYKAGCSDPYPVQLIPTTMAAAAAATPGLGPLQLQQFYAAQLAAMQVSPGGKLLGLPQGNLGAAVSPTSIHTDKSTNSPPPKSKDEVAQPLNLSAKPKTSDGKSPASPTSPHMPALRINSGAGPLKASVPAALASPSARVSTIGYLNDHDAVTKAIQEARQMKEQLRREQQALDGKVAVVNSIGLSNCRTEKEKTTLESLTQQLAVKQNEEGKFSHGMMDFNMSGDSDGSAGVSESRIYRESRGRGSNEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKAMTNLEKQPYYEEQARLSKQHLEKYPDYKYKPRPKRTCLVDGKKLRIGEYKAIMRNRRQEMRQYFNVGQQAQIPIATAGVVYPSAIAMAGMPSPHLPSEHSSVSSSPEPGMPVIQSTYGAKGEEPHIKEEIQAEDINGEIYEEYDEEEEDPDVDYGSDSENHIAGQAN
Protein: Protein SPA2 (P23201)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pheromone-induced morphogenesis and efficient mating, perhaps as a cytoskeletal protein.
Subcellular location: Cell tip. Note=Localizes to a sharp patch at the shmoo tip (mating projection) which corresponds to the site of polarized cell growth.
Interaction partners:
- Protein PEA2
- Protein BNI1
- Bud site selection protein 6
- GTPase-activating protein MSB4
- GTPase-activating protein GYP3
- Mitogen-activated protein kinase SLT2/MPK1
- MAP kinase kinase MKK1/SSP32
- Cell division control protein 42
- MAP kinase kinase MKK2/SSP33
- Uncharacterized protein YFR016C
Sequence:
MGTSSEVSLAHHRDIFHYYVSLKTFFEVTGENRDRSNSTRAQKARAKLLKLSSSQFYELSTDVSDELQRRIGEDANQPDYLLPKANFHMKRNQARQKLANLSQTRFNDLLDDILFEIKRRGFDKDLDAPRPPLPQPMKQEVSKDSDDTARTSTNSSSVTQVAPNVSVQPSLVIPKMASIDWSSEEEEEEQVKEKPNEPEGKQTSMDEKKEAKPALNPIVTDSDLPDSQVLARDITSMARTPTTTHKNYWDVNDSPIIKVDKDIDNEKGPEQLKSPEVQRAENNNPNSEMEDKVKELTDLNSDLHLQIEDLNAKLASLTSEKEKEKKEEKEEKEKEKNLKINYTIDESFQKELLSLNSQIGELSIENENLKQKISEFELHQKKNDNHNDLKITDGFISKYSSADGLIPAQYILNANNLIIQFTTRLSAVPIGDSTAISHQIGEELFQILSQLSNLISQLLLSADLLQYKDQVILLKASLSHAITSIRYFSVYGPVLIPKITVQAAVSEVCFAMCNLIDSAKIKSDSNGESTTSNEGNRQVLEYSSPTATTPMTPTFPSTSGINMKKGFINPRKPASFLNDVEEEESPVKPLKITQKAINSPIIRPSSSNGVPTTSRKPSGTGLFSLMIDSSIAKNSSHKEDNDKYVSPIKAVTSASNSASSNISEIPKLTLPPQAKIGTVIPPSENQVPNIKIENTEEDNKRSDITNEISVKPTSSIADKLKQFEQSSEKKSSPKENPIAKEEMDSKPKLSNKFITSMNDVSTDDSSSDGNENDDADDDDDFTYMALKQTMKREGSKIEKNNDSKLPANIVELDLHESPESVKIESPESIKEITSSEMSSEMPSSSLPKRLVEDVEPSEMPEKGASVESVRKKNFQEPLGNVESPDMTQKVKSLGMTGKAVGPESDSRVESPGMTGQIKSLNMAGKVVGPEADSRVESPGMKEQIKSLGMTGKITAQESIKSPEAARKLASSGEVDKIESPRMVRESESLEAVGNTIPSNMTVKMESPNLKGNTVSEPQEIRRDIASSEPIENVDPPKVLKKIVFPKAVNRTGSPKSVEKTPSSATLKKSGLPEPNSQIVSPELAKNSPLAPIKKNVELRETNKPHTETITSVEPTNKDANTSWRDADLNRTIKREEEDEDFDRVNHNIQITGAYTKTGKIDYHKIPVDRKAKSEAEVHTSEEDIDESNNVNGKRADAQIHITERKHAFVNPTENSQVKKTSHSPFLNSKPVQYENSESNGGINNHIKIKNTGETTAHDEKHYSDDDDSSYQFVPMKHEEQEQEQNRSEEEESEDDDEEEEDSDFDVDTFDIENPDNTLSELLLYLEHQTMDVISTIQSLLTSIKKPQVTKGNLRGESNAINQVIGQMVDATSISMEQSRNANLKKHGDWVVQSLRDCSRRMTILCQLTGDGILAKEKSDQDYADKNFKQRLAGIAFDVAKCTKELVKTVEEASLKDEINYLNSKLK
Protein: Gamma-aminobutyric acid receptor subunit pi (GABA(A) receptor subunit pi) (GABAAR subunit pi) (O09028)
Organism: Rattus norvegicus (Rat)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:17003036}; Multi-pass membrane protein {ECO:0000255}. Note=Located on the apical plasma membrane of alveolar epithelial type II cells. {ECO:0000269|PubMed:17003036}.
Interaction partners:
- Huntingtin-associated protein 1
- Inactive phospholipase C-like protein 1
- Trafficking kinesin-binding protein 2
- Vesicle-fusing ATPase
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit alpha-6
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit alpha-5
- Gamma-aminobutyric acid receptor subunit epsilon
- Gamma-aminobutyric acid receptor subunit alpha-1
Sequence:
MSYSLYLAFVCLNLLAQRMCIQGNQFNVEVSRSDKLSLPGFENLTAGYNKFLRPNFGGDPVRIALTLDIASISSISESNMDYTATIYLRQRWTDPRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVTCNMDLSKYPMDTQTCKLQLESWGYDGNDVEFSWLRGNDSVRGLENLRLAQYTIQQYFTLVTVSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLESVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGALLEYAVAHYSSLQQMAVKDRGPAKDSEEVNITNIINSSISSFKRKISFASIEISGDNVNYSDLTMKASDKFKFVFREKIGRIIDYFTIQNPSNVDRYSKLLFPLIFMLANVFYWAYYMYF
Protein: Galactan beta-1,4-galactosyltransferase GALS2 (EC 2.4.1.-) (Beta-1,4-galactan synthase) (Galactan synthase 2) (Q9LTZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of beta-1,4-galactan. Beta-1,4-galactans are abundant polysaccharides in plant cell walls and are found as side-chain of rhamnogalacturonan I, which is a major component of pectin.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:O22807}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein trichome birefringence-like 10
- O-fucosyltransferase 28
- Probable pectin methyltransferase QUA3
- Galacturonosyltransferase 8
- Probable pectin methylesterase CGR2
- Probable pectin methylesterase CGR3
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3
- Probable galacturonosyltransferase 9
Sequence:
MAKERDQNTKDKNLLICFLWNFSAELKLALMALLVLCTLATLLPFLPSSFSISASELRFCISRIAVNSTSVNFTTVVEKPVLDNAVKLTEKPVLDNGVTKQPLTEEKVLNNGVIKRTFTGYGWAAYNFVLMNAYRGGVNTFAVIGLSSKPLHVYSHPTYRCEWIPLNQSDNRILTDGTKILTDWGYGRVYTTVVVNCTFPSNTVINPKNTGGTLLLHATTGDTDRNITDSIPVLTETPNTVDFALYESNLRRREKYDYLYCGSSLYGNLSPQRIREWIAYHVRFFGERSHFVLHDAGGITEEVFEVLKPWIELGRVTVHDIREQERFDGYYHNQFMVVNDCLHRYRFMAKWMFFFDVDEFIYVPAKSSISSVMVSLEEYSQFTIEQMPMSSQLCYDGDGPARTYRKWGFEKLAYRDVKKVPRRDRKYAVQPRNVFATGVHMSQHLQGKTYHRAEGKIRYFHYHGSISQRREPCRHLYNGTRIVHENNPYVLDTTMRDIGLAVKTFEIRTIGDRLLRTRQ
Protein: Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64) (Q28350)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}. Note=Localization to the nucleolus is dependent on HEATR1. {ECO:0000250|UniProtKB:P01106}.
Interaction partners:
- MYC associated factor X.
- Uncharacterized protein.
- Mitogen-activated protein kinase
- Glycogen synthase kinase 3 beta
- Lysine demethylase 5B.
- Ubiquitin specific peptidase 28
Sequence:
MDLLRRVETPAAAMPLNVSFANRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVASFSPRGDDDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPSPARGPGGCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKPCASPDSAAFSPSSDSLLSSAESSPRASPEPLALHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQPPAKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRARLDSGRVLKQISNNRKCASPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLLSEKDLLRKRREQLKHKLEQLRNSGA
Protein: L-type lectin-like domain-containing protein C4F6.05c (O42707)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transmembrane 9 superfamily protein C1105.08
- Uncharacterized protein C7D4.08
- Septin homolog spn7
Sequence:
MKFCSLFHVLSFCCTLAYAVPKSQFLQLHSLSNAIPVEWKWYGSVDEDSGYVYLTSKDSNEARSGSLWSTSVLRQVGWQLSTSFVAHVSENENTFFAIWYTSAVGSEGPVFGASDKWDGLLISQEIDQTGKIFVRGYLNDKSFELAQFTDPDLPPFAKCTIESSPEALNNIILKYGDQSGLELFVNDKPCFQVKDVILPQGYYFGVSSQSTSAKDLVALSNLNILPPDTSNNENLNPTSNTKQSVGDNTSPQTVIDTEGLNAIKADLAKLFNLVESQRQKMDSLHFALTNALERLNDISSTSQFPSERFNALEKLLHDSLSAQSSTADGTSKHLAEFEKEIKKAMGNAYSPYNLTNFMVFLLLGAIVSYGIMLVRRDRRRHKYL
Protein: Isochorismatase domain-containing protein 1 (Q96CN7)
Organism: Homo sapiens (Human)
Interaction partners:
- 5-oxoprolinase
- Nicotinate phosphoribosyltransferase
- Maestro heat-like repeat-containing protein family member 6
Sequence:
MAAAEPAVLALPNSGAGGAGAPSGTVPVLFCFSVFARPSSVPHGAGYELLIQKFLSLYGDQIDMHRKFVVQLFAEEWGQYVDLPKGFAVSERCKVRLVPLQIQLTTLGNLTPSSTVFFCCDMQERFRPAIKYFGDIISVGQRLLQGARILGIPVIVTEQYPKGLGSTVQEIDLTGVKLVLPKTKFSMVLPEVEAALAEIPGVRSVVLFGVETHVCIQQTALELVGRGVEVHIVADATSSRSMMDRMFALERLARTGIIVTTSEAVLLQLVADKDHPKFKEIQNLIKASAPESGLLSKV
Protein: Divalent metal cation transporter MntH (P0A769)
Organism: Escherichia coli (strain K12)
Function: H(+)-stimulated, divalent metal cation uptake system. Involved in manganese and iron uptake. Can also transport cadmium, cobalt, zinc and to a lesser extent nickel and copper. Involved in response to reactive oxygen.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:14607838}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:14607838}.
Interaction partners:
- Transcriptional regulator MntR
- Zinc transporter ZupT
- Probable manganese efflux pump MntP
- Fe
- Superoxide dismutase
- DNA-binding transcriptional dual regulator OxyR
- Magnesium-transporting ATPase, P-type 1
- High-affinity zinc uptake system membrane protein ZnuB
Sequence:
MTNYRVESSSGRAARKMRLALMGPAFIAAIGYIDPGNFATNIQAGASFGYQLLWVVVWANLMAMLIQILSAKLGIATGKNLAEQIRDHYPRPVVWFYWVQAEIIAMATDLAEFIGAAIGFKLILGVSLLQGAVLTGIATFLILMLQRRGQKPLEKVIGGLLLFVAAAYIVELIFSQPNLAQLGKGMVIPSLPTSEAVFLAAGVLGATIMPHVIYLHSSLTQHLHGGSRQQRYSATKWDVAIAMTIAGFVNLAMMATAAAAFHFSGHTGVADLDEAYLTLQPLLSHAAATVFGLSLVAAGLSSTVVGTLAGQVVMQGFIRFHIPLWVRRTVTMLPSFIVILMGLDPTRILVMSQVLLSFGIALALVPLLIFTSDSKLMGDLVNSKRVKQTGWVIVVLVVALNIWLLVGTALGL
Protein: Fork head domain 3F (Q8T9W8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
PKKPPFTYTELIEYALEDKGELTVSGIYQWISDRFPYYKSNDDRWKNSVRHNLSINPHFRKGVKAP
Protein: Kazal-type serine protease inhibitor domain-containing protein 1 (Q96I82)
Organism: Homo sapiens (Human)
Function: Involved in the proliferation of osteoblasts during bone formation and bone regeneration. Promotes matrix assembly (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MLPPPRPAAALALPVLLLLLVVLTPPPTGARPSPGPDYLRRGWMRLLAEGEGCAPCRPEECAAPRGCLAGRVRDACGCCWECANLEGQLCDLDPSAHFYGHCGEQLECRLDTGGDLSRGEVPEPLCACRSQSPLCGSDGHTYSQICRLQEAARARPDANLTVAHPGPCESGPQIVSHPYDTWNVTGQDVIFGCEVFAYPMASIEWRKDGLDIQLPGDDPHISVQFRGGPQRFEVTGWLQIQAVRPSDEGTYRCLGRNALGQVEAPASLTVLTPDQLNSTGIPQLRSLNLVPEEEAESEENDDYY
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FQI8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Serine/threonine-protein kinase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- non-specific serine/threonine protein kinase
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Serine/threonine-protein kinase TEL1
- Peptidyl-prolyl cis-trans isomerase
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MVQIYYNENQALEPMQHNQANGIWKASYMDEANADSKRFAFTNPWGNEKIDEDEAMSYNYSSANSTADVDMNSDMYKRRKSSLVVPPSRAAAPNPFQYETMQNSTGTAQRAMYPESSAYQQQRQIMVPHQQQGQLASRFNSRFVPSLYNPQEFQRRQSLATAQFSTPSSLHGSASNQAFNTGSGNNGVNLNYASANVTTNNSSTYLSAMTPNVPMEMGNIPLASPHRRLSAFPTSGTTNSSLQPPFKQLRRDEGSPRQIVIPQMHRCHSKNDLQPCINPNPKFRRASLHSNTISPLIGLTKSLLTTYALCSPDFTYQTSKNPKRVLTKPSEGKYNNGYDNVNSDYILYVNDVLGTEQNRKYLVLDILGQGTFGQVVKCQNLQTKEIIAVKVVKSRSEYLNQSISEAKILELLNEKIDPNNKHHFLRMHDSFVHKNHLCLVFELLSNNLYELLKQNKFHGLSIQLIRTFTIQILDSLCVLKDSKLIHCDLKPENILLCSPDKPDLKVIDFGSSCEETRTVYTYIQSRFYRAPEIILGIPYSTSIDMWSLGCIVAELFLGIPIFPGSSEFNQLTRIITTLGYPPTWMIDMGKSSHKFLKKLNTLNLDMTNINDVEAQNNNANYTTANRMQKNQPTAKYRLKTIEEFNRDNNASEKVGKQYFKWALLEDIIRNYRIHKNIQKSPELIEQEMKNRECLIHFLKGILNLNPLERWTPQQAAMHPFITQQPFTGKWFPPGSFNTMNTSNFGSQPRQEGNNSNNMKPNSQEGPTKEFTNLKIIED
Protein: Ribostamycin:4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(gamma-L-glutamylamino)-(S)-2-hydroxybutanoate transferase (EC 2.3.2.19) (Acyl carrier protein:aminoglycoside acyltransferase) (Butirosin biosynthesis protein H) (Q4H4E9)
Organism: Niallia circulans (Bacillus circulans)
Function: Aminoglycoside acyltransferase that attaches the (S)-4-amino-2-hydroxybutyrate (AHBA) side chain from the acyl carrier protein BtrI to the aminoglycoside ribostamycin in the biosynthetic pathway of butirosin. The AHBA side chain protects the antibiotic from several common resistance mechanisms.
Interaction partners:
Sequence:
MCLTRYDEKFFDCRKSQIIAYLDSQQVPVIPLFYNSYQSTAEIYRQIFIENKSKWKYSEPSFSDDDLLRKGIRPVRASFPDFSQASDCLKDLLARHKLVFVWGDEYCLPYRKEAFQAIHSTHSLVVTGYDGENKAYYVEDWDGLYGYLPAVHLEAAFDSLSRQMRTLLVLELNDEEMRENKQEDTDLFRKWLQAFEDDYIFYDRVLLDMRDYEENRLISMDHGLRLIAASRHVFSKFLHYIDDAPEEVGLLIRNHQLANHIAAIVRRYIIAKQIDWDGAACKIRQLREQEDDFMRKLKSRYG