wanglab/gogpt-training-data huggingface dataset:
Protein: Pre-B-cell leukemia transcription factor-interacting protein 1 (Hematopoietic PBX-interacting protein) (Q3TVI8)
Organism: Mus musculus (Mouse)
Function: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96AQ6}. Nucleus {ECO:0000250|UniProtKB:Q96AQ6}. Note=Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus. {ECO:0000250|UniProtKB:Q96AQ6}.
Interaction partners:
Sequence:
MASCPDSDNSWVLAGSENLPVETLGPEPRMDPESEGASQALRDSSKADGKELAGTLDGEEKLFQTESSQRETAVLTESAAKGTLGADGHGTEAPGDTVVQEDSQETPVATSLGPDTQDLESEIHPQNLPSSPRAVWKEHRCSSSDDDTDVDVEGLRRRRGREPSSSQPVVPVDVEDQAKGEGIGGELGISLNMCFLGALVLLGLGILLFSGTLLEPETGPMEEAELQVFPETGPETELVETLGNRQDEIEHLQASSVPPDSVPSLQSMGFLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGVDGVCLNWGGDPQDGKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLGSVHWDLQRGLRDAGRGAPAHPGLAELGHMLAQTLQDLENQGINTGRSPNDSEAWHQKKPHTQSPREWGGKEKWRGGQRDQKAEHWKPRKEESGQERQRSWRDEGREHTGRWREDRLRADESGSRKDSKRQDPKVHPRKDGNSHSVERQKHSWGKDNSPDALSSWEELLRRKYRPPQGCSGVADCARQEGLALFGVELAPVRQQELASVLREYLSRLPWAGQLTKQLPLSPAYFGEDGIFRHDRLRFRDFVDALEDSLEEVALKQTGDDDEVDDFEDFVFGHFFGDKALKKRSRKKEKHSWNPRVVGPREEHSRHPHHYHQG
Protein: Obg-like ATPase 1 (F4I3J0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03167}.
Interaction partners:
- Thylakoid lumenal protein TL20.3
- Probable calcium-binding protein CML1
- Nodulin-related protein 1
- Probable calcium-binding protein CML27
Sequence:
MARAACSSVVTAMALLPSKSLLCRNQLLFSGNSKFVGVLTLQKRCFSSKVSMSLKAGIVGLPNVGKSTLFNAVVENGKAQAANFPFCTIEPNVGIVAVPDSRLQVLSKLSGSQKTVPASIEFVDIAGLVKGASQGEGLGNKFLSHIREVDSILQVVRCFEDNDIIHVNGKVDPKSDIDVINLELIFCDLDQIGKRIERLKKGKAKDSQSKVKEEAEKSALERIQEALLEGKPARSVALSDLEMEVVKHLCLLTMKPMIYVANVAETDLAEPEKNAYVEEVKGLSSDLQSGHVVVSAQVESELTELPLEERTEYLNSLGVSESGLGNLIRATYSLLGLQTYFTSGEKETRAWTIHAGMTAPQAAGVIHSDFEKGFIRAETVAYEDFVTAGSIAAAREKGLLRSEGKEYIVKEGDVMLFRFNV
Protein: Stage V sporulation protein M (P37817)
Organism: Bacillus subtilis (strain 168)
Function: Coordinates cortex and coat assembly during sporulation. Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface. May also serve as a competitive inhibitor of FtsH activity during sporulation.
Subcellular location: Forespore outer membrane {ECO:0000269|PubMed:12562810, ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:22463703, ECO:0000269|PubMed:25825747, ECO:0000269|PubMed:29102609}; Peripheral membrane protein {ECO:0000269|PubMed:12562810, ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:25825747}. Note=SpoVM is an atypical amphipathic alpha-helix deeply embedded in the membrane (PubMed:25825747). Proper localization depends on SpoIVA (PubMed:17427285). {ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:25825747}.
Interaction partners:
- Stage IV sporulation protein A
- Stage VI sporulation protein D
- SpoIVD-associated factor A
- Spore coat protein E
- Spore coat protein Z
- Septum site-determining protein DivIVA
- Stress response protein YhaX
Sequence:
MKFYTIKLPKFLGGIVRAMLGSFRKD
Protein: General transcription factor 3C polypeptide 3 (Transcription factor IIIC 102 kDa subunit) (TFIIIC 102 kDa subunit) (TFIIIC102) (Transcription factor IIIC subunit gamma) (TF3C-gamma) (Q9Y5Q9)
Organism: Homo sapiens (Human)
Function: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.
Subcellular location: Nucleus.
Interaction partners:
- General transcription factor 3C polypeptide 5
- General transcription factor 3C polypeptide 4
- General transcription factor 3C polypeptide 1
- Transcription factor IIIB 90 kDa subunit
- General transcription factor 3C polypeptide 2
- DNA-directed RNA polymerase III subunit RPC4
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- General transcription factor 3C polypeptide 6
- Transcription factor IIIB 50 kDa subunit
Sequence:
MSGFSPELIDYLEGKISFEEFERRREERKTREKKSLQEKGKLSAEENPDDSEVPSSSGINSTKSQDKDVNEGETSDGVRKSVHKVFASMLGENEDDEEEEEEEEEEEEEEETPEQPTAGDVFVLEMVLNRETKKMMKEKRPRSKLPRALRGLMGEANIRFARGEREEAILMCMEIIRQAPLAYEPFSTLAMIYEDQGDMEKSLQFELIAAHLNPSDTEEWVRLAEMSLEQDNIKQAIFCYTKALKYEPTNVRYLWERSSLYEQMGDHKMAMDGYRRILNLLSPSDGERFMQLARDMAKSYYEANDVTSAINIIDEAFSKHQGLVSMEDVNIAAELYISNKQYDKALEIITDFSGIVLEKKTSEEGTSEENKAPENVTCTIPDGVPIDITVKLMVCLVHLNILEPLNPLLTTLVEQNPEDMGDLYLDVAEAFLDVGEYNSALPLLSALVCSERYNLAVVWLRHAECLKALGYMERAAESYGKVVDLAPLHLDARISLSTLQQQLGQPEKALEALEPMYDPDTLAQDANAAQQELKLLLHRSTLLFSQGKMYGYVDTLLTMLAMLLKVAMNRAQVCLISSSKSGERHLYLIKVSRDKISDSNDQESANCDAKAIFAVLTSVLTKDDWWNLLLKAIYSLCDLSRFQEAELLVDSSLEYYSFYDDRQKRKELEYFGLSAAILDKNFRKAYNYIRIMVMENVNKPQLWNIFNQVTMHSQDVRHHRFCLRLMLKNPENHALCVLNGHNAFVSGSFKHALGQYVQAFRTHPDEPLYSFCIGLTFIHMASQKYVLRRHALIVQGFSFLNRYLSLRGPCQESFYNLGRGLHQLGLIHLAIHYYQKALELPPLVVEGIELDQLDLRRDIAYNLSLIYQSSGNTGMAQTLLYTYCSI
Protein: Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) (Q13155)
Organism: Homo sapiens (Human)
Function: Required for assembly and stability of the aminoacyl-tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. Nucleus {ECO:0000250|UniProtKB:Q8R010}. Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:Q8R010}.
Interaction partners:
- Lysine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Eukaryotic translation elongation factor 1 epsilon-1
- Bifunctional glutamate/proline--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MPMYQVKPYHGGGAPLRVELPTCMYRLPNVHGRSYGPAPGAGHVQEESNLSLQALESRQDDILKRLYELKAAVDGLSKMIQTPDADLDVTNIIQADEPTTLTTNALDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCEHFRVLSTVHTHSSVKSVPENLLKCFGEQNKKQPRQDYQLGFTLIWKNVPKTQMKFSIQTMCPIEGEGNIARFLFSLFGQKHNAVNATLIDSWVDIAIFQLKEGSSKEKAAVFRSMNSALGKSPWLAGNELTVADVVLWSVLQQIGGCSVTVPANVQRWMRSCENLAPFNTALKLLK
Protein: 60S acidic ribosomal protein P0 (Q53HK9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFSQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD
Protein: Alpha-(1,6)-fucosyltransferase (Alpha1-6FucT) (EC 2.4.1.68) (GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase) (GDP-fucose--glycoprotein fucosyltransferase) (Glycoprotein 6-alpha-L-fucosyltransferase) (Q9VYV5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. The addition is prevented if the GlcNAc residue is already fucosylated.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
Interaction partners:
- Glycoprotein 3-alpha-L-fucosyltransferase A
- Alpha-mannosidase 2
- Alpha-
- Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase a, isoform A
- Alpha-
- Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase b
- Fucosyltransferase
- LP02557p
- GDP-fucose transporter, Golgi
Sequence:
MLLVRQLFGASANSWARALIIFVLAWIGLVYVFVVKLTNTQGQQAAGESELNARRISQALQMLEHTRQRNEELKQLIDELMSDQLDKQSAMKLVQRLENDALNPKLAPEVAGPEPESMFESAPADLRGWNNVAEGAPNDLEAGVPDHGEFEPSLEYEFTRRRIQTNIGEIWNFFSSELGKVRKAVAAGHASADLEESINQVLLQGAEHKRSLLSDMERMRQSDGYEAWRHKEARDLSDLVQRRLHHLQNPSDCQNARKLVCKLNKGCGYGCQLHHVVYCFIVAYATERTLILKSRGWRYHKGGWEEVFQPVSNSCHDAGTANTYNWPGKPNTQVLVLPIIDSLMPRPPYLPLAVPEDLAPRLKRLHGDPIVWWVGQFLKYLLRPQPTTRDFLTSGMRNLGWERPIVGVHVRRTDKVGTEAACHSVEEYMTYVEDYYRTLEVNGSTVARRIFLASDDAQVIEEARRKYPQYQIIGDPEVARMASVSTRYTDTALNGIILDIHLLSMSDHLVCTFSSQVCRVAYEIMQTMYPDAAHRFKSLDDIYYYGGQNAHNRRVVIAHKPRTHEDLQLRVGDLVSVAGNHWDGNSKGKNTRTNQGGLFPSFKVEEKVDTAKLPLYAGI
Protein: 26S proteasome complex subunit SEM1 (O94742)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.
Interaction partners:
- Nuclear mRNA export protein THP1
- Cop9 signalosome complex subunit 12
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit RPN2
- 26S proteasome regulatory subunit 7 homolog
- 26S proteasome regulatory subunit 8 homolog
- Nuclear mRNA export protein SAC3
- 26S proteasome regulatory subunit RPN9
- 26S proteasome regulatory subunit RPN7
- 26S proteasome regulatory subunit 6B homolog
Sequence:
MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIWEENWDDVEVDDDFTNELKAELDRYKRENQ
Protein: Interferon omega-1 (Interferon alpha-II-1) (P05000)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Interferon alpha/beta receptor 2
- Interferon alpha/beta receptor 1
- Interleukin-10 receptor subunit beta
- Interferon lambda receptor 1
- Interleukin-12 receptor subunit beta-1
- Interferon gamma receptor 1
- Cytokine receptor common subunit beta
Sequence:
MALLFPLLAALVMTSYSPVGSLGCDLPQNHGLLSRNTLVLLHQMRRISPFLCLKDRRDFRFPQEMVKGSQLQKAHVMSVLHEMLQQIFSLFHTERSSAAWNMTLLDQLHTGLHQQLQHLETCLLQVVGEGESAGAISSPALTLRRYFQGIRVYLKEKKYSDCAWEVVRMEIMKSLFLSTNMQERLRSKDRDLGSS
Protein: Abscisic acid 8'-hydroxylase CYP707A2 (ABA 8'-hydroxylase CYP707A2) (SlCYP707A2) (EC 1.14.14.137) (Cytochrome P450 707A2) (K4CI52)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Negative regulator of fruit ripening involved in the oxidative degradation of abscisic acid (ABA).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- indole-3-acetaldehyde oxidase
- indole-3-acetaldehyde oxidase
- indole-3-acetaldehyde oxidase
- Abscisic acid 8'-hydroxylase CYP707A1
- 
- 9-cis-epoxycarotenoid dioxygenase NCED1, chloroplastic
- 9-cis-epoxycarotenoid dioxygenase NCED2, chloroplastic
- TF-B3 domain-containing protein
Sequence:
MEFVSMLCLFTFISLTLLLIHSIFKFLAFASKKLPLPPGTLGLPYIGETFQLYSQNPNVFFASKVKKYGSIFKTYILGCPCVMISSPEAAKQVLVTKANLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLQAFKPDSIRNIIPDIESIAITSLESFQGRLINTYQEMKTYTFNVALISIFGKDEFLYREELKKCYYILEKGYNSMPINLPGTLFNKAMKARKELAKIVAKIISTRREMKIDHGDLLGSFMGDKEGLTDEQIADNVIGVIFAARDTTASVLTWILKYLGENPSVLQAVTEEQENIMRKKEVNGEEKVLNWQDTRQMPMTTRVIQETLRVASILSFTFREAVEDVEFEGYLIPKGWKVLPLFRNIHHSPDNFPEPEKFDPSRFEVSPKPNTFMPFGNGVHSCPGNDLAKLEILILVHHLTTKYRWSMVGPQNGIQYGPFALPQNGLPIKLSLKTSST
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38CN2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MDYKDCYGYLAALTFVVSLCSGAPLTDNDPVAEQISDLCKEKFYVETLIQNLKQRVQSTAASIKDMEKLKATWEKAAAATSDAAKKCLFSALEHKADAELLRELPKIEEATEAVTTAQIALSEHVGMLGATITLAKTKLDSGSSNHGNAGTGSIRIALSRTTATTDLCNEPATISDIKPGVSEIQPDKLFKLKLTKPTDLHKHMFVDWLTIGGLTSCTAHTSYDQNFDAALSGCNYKTAATAEAKQATTKPTYGTTEVTLFKNNDPEQQCEVTDLPAGGAADKHKKLQHSLCRALQLGNVNGRSLRQLNGAALQSDHVVANTIRNCDPVFQKLTTATDGEGTTELKKYIKEAYGSSASEFAEKFITNAEKLQMTLRLNDKIETKDLSAVSPGEQTAAALSHIQGLHNKRELEAGKKSTSAAAVDPQKSEDCKGEKDETKCNKKDGCEFKDGECLAKVTTAAGTDGKTNTTGSNSFVIHKTPLLHVCLLL
Protein: Broad-specificity linear acyl-CoA dehydrogenase FadE5 (Long-chain-acyl-CoA dehydrogenase) (EC 1.3.8.8) (Medium-chain-acyl-CoA dehydrogenase) (EC 1.3.8.7) (Short-chain-acyl-CoA dehydrogenase) (EC 1.3.8.1) (O53666)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates.
Interaction partners:
- Probable fatty oxidation protein FadB
- 3-hydroxyisobutyryl-CoA hydrolase
- Electron transfer flavoprotein subunit alpha
- Uncharacterized protein Rv0487
- Electron transfer flavoprotein subunit beta
- Probable acetyl-CoA acyltransferase FadA2
- Probable fatty-acid-CoA ligase FadD36
- Phthioceranic/hydroxyphthioceranic acid synthase
Sequence:
MSHYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPESFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVETGEPGERNGVFVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALAHVSGQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDVTSLYKVGLGSVRFLMSVGDLIIGWLLQRQAAVAVAALDAGATGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMELDEAAF
Protein: Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Q6P6R2)
Organism: Rattus norvegicus (Rat)
Function: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P09622}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P09622}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000250|UniProtKB:P09622}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Ac1164
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
Sequence:
MQSWSRVYCSLAKKGHFNRLSHGLQGASSVPLRTYSDQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIEIPEVRLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAASFGKPINF
Protein: YbtQ (YbtQ protein) (Q9Z375)
Organism: Yersinia pestis
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Irp1 protein
- Putative signal transducer
- Previously sequenced as Yersinia pestis yersiniabactin biosynthetic protein Irp2 TR:Q9Z399
- YbtA
- Salicylate synthetase
- Lipoprotein inner membrane ABC-transporter
- Previously sequenced as Yersinia pestis yersiniabactin biosynthetic protein YbtU TR:Q9Z3C6
- Pesticin receptor
- YbtT protein
- Salicyl-AMP ligase YbtE
Sequence:
MKDNNPADNLAWRVIWRQLISSVGSQARMLRRSMLALLLAAFMQGIAFACLYPIIDALLRGDAPQLLNWAMAFSVAAIVTLVLRWYGLGFEYRGHLAQATHELRLRLGEQLRRVPLEKLQRGRAGEMNALLLGSVDENLNYVIAIANILLLTIVTPLTASLATLWIDWRLGLVMLLIFPLLVPFYYWRRPAMRRQMQTLGEAHQRLSGDIVEFAQGMMVLRTCGSDADKSRALLAHFNALENLQTRTHRQGAGATMLIASVVELGLQVVVLSGIVWVVTGTLNLAFLIAAVAMIMRFAEPMAMFISYTSVVELIASALQRIERFMAIAPLPVAEQSEMPERYDIRFDNVSYRYEEGDGHALNHVSLTFPAASMSALVGASGAGKTTVTKLLMRYADPQQGQISIGGVDIRRLTPEQLNSLISVVFQDVWLFDDTLLANIRIARPQATRQEVEEAARAAQCLEFISRLPQGWLTPMGEMGGQLSGGERQRISIARALLKNAPVVILDEPTAALDIESELAVQKAIDNLVHNRTVIIIAHRLSTIAGAGNILVMEEGQVVEQGTHAQLLSHHGRYQALWQAQMAARVWRDDGVSASGEWVHE
Protein: Drebrin-like protein (Actin-binding protein 1) (Abp1) (SH3 domain-containing protein 7) (Q9JHL4)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes (By similarity). Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23223303}. Cell projection, lamellipodium {ECO:0000269|PubMed:23223303}. Cell projection, ruffle {ECO:0000269|PubMed:23223303}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23223303}. Cytoplasm, cytosol {ECO:0000269|PubMed:23223303}. Cell membrane {ECO:0000269|PubMed:23223303}; Peripheral membrane protein; Cytoplasmic side. Synapse {ECO:0000269|PubMed:15014124}. Perikaryon {ECO:0000250|UniProtKB:Q62418}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q62418}. Cell projection, dendrite {ECO:0000269|PubMed:15014124}. Postsynaptic density {ECO:0000269|PubMed:15014124}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein; Cytoplasmic side. Cell projection, podosome {ECO:0000250|UniProtKB:Q62418}. Early endosome {ECO:0000250|UniProtKB:Q9UJU6}. Note=Associates with lamellipodial actin and membrane ruffles. Colocalizes with actin and cortactin at podosome dots and podosome rosettes. {ECO:0000269|PubMed:23223303}.
Interaction partners:
- Adenylyl cyclase-associated protein 1
- Adenylyl cyclase-associated protein 2
- F-actin-capping protein subunit beta
Sequence:
MAVNLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEELVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACANHVSTMANFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESSCFQDVGPQAPVGSVYQKTNAVSEIKRVGKDNFWAKAEKEEENRRLEEKRRAEEEKQRLEEERRERELQEAARREQRYQEQHRSAGPPSPSSRTGELEQEVVSRSRQEWESAGQQAPHPREIFKQKERAMSTTSVSSSQPGKLRSPFLQKQFTQPEASYGREPTSPVSRPAAGVCEELAPSTPPSAQTDDEPTYEVPSEQETLYEEPPPVQQPGAGSGHIDNYMQSQDLSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE
Protein: Serine protease 41 (EC 3.4.21.-) (Testis serine protease 1) (TESSP-1) (Q920S2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000269|PubMed:15515062, ECO:0000269|PubMed:19798924}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15515062, ECO:0000269|PubMed:19798924}. Note=Localized in the plasma membrane of spermatogonia. Localized in intracellular compartment in spermatocytes, probably in the Golgi apparatus.
Interaction partners:
Sequence:
MGIQGPVLLLLLLCVMLGKPGSREESQAADLKSTDIKLLSMPCGRRNDTRSRIVGGIESMQGRWPWQASLRLKKSHRCGGSLLSRRWVLTAAHCFRKYLDPEKWTVQLGQLTSKPSYWNRKAYSGRYRVKDIIVNSEDKLKSHDLALLRLASSVTYNKDIQPVCVQPSTFTSQHQPRCWVTGWGVLQEDLKPLPPPYHLREVQVSILNNSRCQELFEIFSLHHLITKDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSWGIGCGRPNLPGIYTNVSHYYNWIETMMILNGAVRRDLALPLLSITLLQAPWLLRPT
Protein: Steroid 21-hydroxylase (EC 1.14.14.16) (21-OHase) (Cytochrome P-450c21) (Cytochrome P450 21) (Cytochrome P450 XXI) (Cytochrome P450-C21) (Q64562)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids and glucocorticoids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08686}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08686}. Microsome membrane {ECO:0000250|UniProtKB:P08686}; Peripheral membrane protein {ECO:0000250|UniProtKB:P08686}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Cytochrome P450 11B3, mitochondrial
- Cholesterol side-chain cleavage enzyme, mitochondrial
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- 11-beta-hydroxysteroid dehydrogenase type 2
- 25-hydroxycholesterol 7-alpha-hydroxylase
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Aldo-keto reductase family 1 member C18
- Steryl-sulfatase
Sequence:
MLLPGLLLLLLLLLLAGTRWLWGQWKLWKLRLPPLAPGFLHFLQPNLPVYLFGLAQKLGPIYRIRLGLQDVVVLNSNKTIEEALIQKWVDFAGRPQILDGKMNFDLSMGDYSLTWKAHKKLSRSALVLGMRDSMEPLVEQLTQEFCERMRAQAGASVAIHKEFSLLTCSIISCLTFGDKQDSTLLNATHSCVRDLLKAWNHWSVQILDIIPFLRFFPNPGLWKLKQFQESRDHIVMQELKRHKDSLVAGQWKDMIDYMLQGVEKQRDARDPGQLHERHVHMSVVDLFVGGTETTAATLSWAVAFLLHHPEIQKRLQEELDLKLAPSSQLLYKNRMQLPLLMATIAEVLRLRPVVPMALPHRATKASSISGYDIPKDTIIIPNIQGANLDEMVWELPSKFWPDRFLESGKSPRIPTFGCGARVCLGEPLARLEFFVVLARLLQTFTLLPPPDGTLPSLQPLPYTGINLLIPPFQVRLQPRNLAPQDQGQKSSTG
Protein: SET (cDNA FLJ51749, highly similar to Protein SET) (Q5VXV3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPKRQSPLPPQKKKPRPPPALGPEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEGEEDDDDDEEEEGLEDIDEEGDEDEGEEDEDDDEGEEGEEDEGEDD