wanglab/gogpt-training-data huggingface dataset:
Protein: Synaptonemal complex central element protein 1-like (Meiosis-related protein) (A8MT33)
Organism: Homo sapiens (Human)
Function: May be involved in meiosis.
Interaction partners:
Sequence:
MAGKLKPLNVEAPEATEEAEGQAKSLKTEDLLAMVIKLQKEGSLEPQIEDLISRINDLQQAKKKSSEELRETHSLWEALHRELDSLNGEKVHLEEVLGKKQEALRILQMHCQEKESEAQRLDVRGQLEDLMGQHKDLWEFHMLEQRLAREIRALERSKEQLLSERRLVRAKLREVERRLHSPPEVEGAMAVNDGLKAELEIFGEQVRSAPEVGAGEGEAGPELPRARDEEDPEPPVAAPDAL
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (Reston NP) (rNP) (Q8JPY1)
Organism: Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus)
Function: Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. VP35 binds to and stabilizes monomeric NP, keeping it soluble. Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm. Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid. Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription. Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1.
Subcellular location: Virion {ECO:0000250|UniProtKB:P18272}. Host cytoplasm {ECO:0000250|UniProtKB:P18272}.
Interaction partners:
Sequence:
MDRGTRRIWVSQNQGDTDLDYHKILTAGLTVQQGIVRQKIISVYLVDNLEAMCQLVIQAFEAGIDFQENADSFLLMLCLHHAYQGDYKLFLESNAVQYLEGHGFKFELRKKDGVNRLEELLPAATSGKNIRRTLAALPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKYLLIHQGMHMVAGHDANDAVIANSVAQARFSGLLIVKTVLDHILQKTDQGVRLHPLARTAKVRNEVNAFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLYPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDSLGLDDQERRILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITLASRPNLGSRQDDGNEIPFPGPISNNPDQDHLEDDPRDSRDTIIPNGAIDPEDGDFENYNGYHDDEVGTAGDLVLFDLDDHEDDNKAFEPQDSSPQSQREIERERLIHPPPGNNKDDNRASDNNQQSADSEEQGGQYNWHRGPERTTANRRLSPVHEEDTLMDQGDDDPSSLPPLESDDDDASSSQQDPDYTAVAPPAPVYRSAEAHEPPHKSSNEPAETSQLNEDPDIGQSKSMQKLEETYHHLLRTQGPFEAINYYHMMKDEPVIFSTDDGKEYTYPDSLEEAYPPWLTEKERLDKENRYIYINNQQFFWPVMSPRDKFLAILQHHQ
Protein: Pescadillo ribosomal biogenesis factor 1 (H7C267)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XPQWVFDSVNARLLLPVAEYFSGVQLPPHLSPFVTEKEGDYVPPEKLKLLALQRGEDPGNLNESEEEEEEDDNNEGDGDEEGENEEEEEDAEAGSEKEEEARLAALEEQRMEGKPRVMAGTLKLEDKQRLAQEEESEAKRLAIMMMKKREKYLYQKIMFGKRRKIREANKLAEKRKAHDEAVRSEKKAKKARPE
Protein: Thromboxane A2 receptor (Prostanoid TP receptor) (Q0VAB0)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTRSSFLTFLCGLVLTDFLGLLVTGTIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPLLLGAAMASERYLGLHCPDSAAKPACHEPRRAAVPHHGEGAAHLLARGHLEPDPGPLGVYPVPPRRAPASPASPQHPAQVAVPPAPAHAALRAAVGSGQSAPPAPFRGALGPSDSPSACSEDSGAGGAGWTVGISSRVLG
Protein: Condensin complex subunit 1 (XCAP-D2 homolog) (p128) (O94679)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.
Subcellular location: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Structural maintenance of chromosomes protein 4
- Condensin complex subunit 3
- Condensin complex subunit 2
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 1
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 5
- Kinesin-like protein cut7
- Structural maintenance of chromosomes protein 6
- Aurora kinase
Sequence:
MSLDLLSRLKKYIHDEENSDLDSIYAECENAGLTAVVNDVIDTLLLGTSSCFDEDCLEKLFAICSHFADLSSSVRNKVYDLLTSNISSESAILEDMISANATDFTVPQTNLETTGIAFQLTVNSLSSSNQLSVIRSSTNTVKGRKKNPTTNSNWNGISHVNALLDAIITLFQKKLSRVWTTSSERDMFLSLFLKPIYTLMESEINIKNASFRSRLFNIIGLAVQFHNHTTAAETNIIQNLQYFEHLSEYAADLVHIVTVQFNSVTLAEGIIRTLCSLEFNDNDVKGPKQVALFLVRLSSLIPNLCLKQLTQLVKLLDSESYTLRCAIIEVLANVVIDQIHDEAQNEMSESVPATVQSLMDLLSERLLDISPYCRTKVLHVFIKIFDLPIKYPRKRQEIAELVIRCLQDRSSHVRRNAIKLFSKLLTTHPFSVMHNGLLTRNIWEKGLSIIEEQLNSLQPKQQEKVVDSELEVDENLLEDATMIQDDESHEGESHLENSLSEYVDSVPAEEIVKVNLTKRFYLEALQYIDIVEAGAKIISQLLFAKNKSEVIESMDFFVFCNSFGISSSKLYIKKMIHLIWVKGTSDEGNNIQNHVLSCYKTLFFEPPPNSGTNEAANYIARNLISLTYDASLAELTSLEQMLCILMKDGYFSHLVITKLWQVYSYQKKDISRTQRRGSIIVIGMLALGNTDVVMQGLDHLIQIGLGPPGLEDLVLARYTCIAIKRIGKDASGSSNINFPNSHTLCQKLCMLLLRPSFSEEWFGLEEQAIEAIYAVAKHPDELCTNIILLLTKQLFKPSNHENTTSNDDHAMDEDLDDSPEEETLKDEEEIGIRLAHLIFLVGHVAIKQLVYIEYCEAEFKRRKADAERLAVQNSNNPINGQETSEYDLITGTSEDDFSEAMTFIRERELLYGENSLLSRFAPLVVELCSNHKSHNNQSLLLAASLTLSKFMCLSNNFCMEHLPLLITILEKCDNPIIRNNLVIGLADLTVCFNHFIDEISEYLYRRLMDEESSVKKTCFMTLAFLILAGQIKVKGQLGIMARSLEDEDARISDLARMFFTDFAAKDNSVYNNFIDIFSVLSRSAEEQDEDDAKFKRIIRFLTSFIEKERHTKQLAERLAARLDRCKTQRQWDHVVYALSLLPHKADNIQKLIDDGYHE
Protein: Putative uncharacterized protein YBL100C (P38168)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLFKPKTRAIPSPTARTLPVSFKLASSDTPLILSSKMEETSVGCALVEANLLVEAKAAAAGLAALVELIRVLDRERIAAVRANIIICACFFYLFCYCSCDSYES
Protein: Chitin deacetylase 1 (EC 3.5.1.41) (Q06702)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin to form chitosan and acetate. Chitosan is a component of the spore wall.
Subcellular location: Prospore {ECO:0000305|PubMed:9133736}.
Interaction partners:
- Chitin deacetylase 2
- Endochitinase
- Sporulation-specific chitinase 2
- Chitin synthase 1
- Chitin synthase 2
- Chitin synthase 3
- Guanine nucleotide-binding protein subunit beta
- Chitin synthase export chaperone
- Outer spore wall protein 4
- Transcription factor CSR2
Sequence:
MKIFNTIQSVLFAAFFLKQGNCLASNGSTALMGEVDMQTPFPEWLTEFTNLTQWPGIDPPYIPLDYINLTEVPELDRYYPGQCPKISREQCSFDCYNCIDVDDVTSCFKLSQTFDDGPAPATEALLKKLRQRTTFFVLGINTVNYPDIYEHILERGHLIGTHTWSHEFLPSLSNEEIVAQIEWSIWAMNATGKHFPKYFRPPYGAIDNRVRAIVKQFGLTVVLWDLDTFDWKLITNDDFRTEEEILMDINTWKGKRKGLILEHDGARRTVEVAIKINELIGSDQLTIAECIGDTDYIERYD
Protein: Uncharacterized protein (Q385B3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPTAVRQDSGSSGGPVTAATSQTLTEAVAITEDYVRMLRHTIKQHDAEKLALIERIDSCLKPEQAEAQRLRCEAAQRVEELGKVQRELSETRSMLQEERERANRLMYENVALHAQAGDDRATIAALMKQTAAARSGAQKLPNPTASTSPTRRTTSKRRSGQQTISLRQACATQQHDTTGDEDPYTSNSANELSSPSSALVAALREEVEMLKSLLDAQRAMHETERASRLQEERELERRRTEMTGTHLASIERLHGLHQASLADLIQTRHDMRIENRELRGTVERLQVALSDALATLKEERQKHTVDLQRQRQIADENAKVVTERLRRQLQERRALLITERERYGALLVQRGAELTRLREERTKDKKRLRELEKWRRLEVEGVNSEVNLMRQELRAMQRRMWFSS
Protein: Transcription factor protein (Q4H3W1)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor protein
- Mitogen-activated protein kinase 15
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- BZIP domain-containing protein
- Stress-activated protein kinase JNK
Sequence:
MSEVSDSPSKGDSDETQTSQDTFVCNSAGCNQKFASAKELEVHKCKHQMTLKLGPTKASNLSDVLPIDQTPTPTRFLQFGNQMGLFEELNPFDREFKTAQKETLTSKQRRTANVVHQLQAMNNSTKSKTPTTPNTDANMFQQPVHVITLTPSLSSPVGNLPVGGGQFFVPPLLPSPQGLIPALPGYTASSPMSVPVSMLSPSIMPFAPGLLPMHGMSPGMMADAQRALTKAMFAAVVSASSPTTSNVPLLTNPQDAYNNNNTSISDAASQPIIGNTNANLPRTGSLPSVAYVKQERPQSNSSVKSESTNQMSEVSPPLPAHQSQAMMHENYLQSQSMVMPPSVMVHLPNGQTTCIGIPTTSPPMAAGMVDLTSSITMPTMSNPTMQQALNNHQQANHPTLSMKSSSEFGSNSNLLDAKQKLKETLKSNNPALQHAITTQSMQMSVNSSNNSSSDQPKRRRGRQQQDVDPDIKRQRFLERNRAAASRCRSKKKNWVVGLESKAKTLSQTNVMLQNEITQLKDEIASLKQLLLSHRDCPITKMQQQSMAMAGINLNLEPSTTTTTTSTNNSGVKSENMPENYHQSLTSSLSSNSLDENYHNPNSQSSQHQQQPPVSSGQLYADLMSSSNTATS
Protein: Ruminococcin-A (RumA protein 1/2/3) (P83674)
Organism: Mediterraneibacter gnavus (Ruminococcus gnavus)
Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin exhibiting activity against a wide range of pathogenic clostridia and B.longum.
Subcellular location: Secreted {ECO:0000269|PubMed:11526013}.
Interaction partners:
Sequence:
MRNDVLTLTNPMEEKELEQILGGGNGVLKTISHECNMNTWQFLFTCC
Protein: Ethanolamine ammonia-lyase large subunit (EAL large subunit) (EC 4.3.1.7) (Ethanolamine ammonia-lyase alpha subunit) (Ethanolamine ammonia-lyase heavy chain) (P19264)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (Probable). It is spontaneously inactivated by its substrate and reactivated by EutA (By similarity). May play a role in BMC assembly or maintenance (Probable).
Subcellular location: Bacterial microcompartment {ECO:0000255|HAMAP-Rule:MF_00861, ECO:0000305|PubMed:22428024}. Note=Probably located in the BMC; as EutC is targeted to the BMC interior this subunit should be in the same location (Probable). Has been suggested to be on the exterior of the BMC (PubMed:23585538). {ECO:0000269|PubMed:23585538, ECO:0000305|PubMed:22428024}.
Interaction partners:
- Ethanolamine ammonia-lyase small subunit
- Ethanolamine ammonia-lyase reactivase EutA
- Probable ethanolamine permease EutH
- Bacterial microcompartment shell protein EutL
- Acetaldehyde dehydrogenase
- Bacterial microcompartment shell protein EutS
- HTH-type DNA-binding transcriptional activator EutR
- Corrinoid adenosyltransferase EutT
- Acetate kinase EutQ
- Bacterial microcompartment shell protein EutK
Sequence:
MKLKTTLFGNVYQFKDVKEVLAKANELRSGDVLAGVAAASSQERVAAKQVLSEMTVADIRNNPVIAYEEDCVTRLIQDDVNETAYNRIKNWSISELREYVLSDETSVDDIAFTRKGLTSEVVAAVAKICSNADLIYGGKKMPVIKKANTTIGIPGTFSCRLQPNDTRDDVQSIAAQIYEGLSFGAGDAVIGVNPVTDDVENLTRVLDTVYGVIDKFNIPTQGCVLAHVTTQIEAIRRGAPGGLIFQSICGSEKGLKEFGVELAMLDEARAVGAEFNRIAGENCLYFETGQGSALSAGANFGADQVTMEARNYGLARHYDPFLVNTVVGFIGPEYLYNDRQIIRAGLEDHFMGKLSGISMGCDCCYTNHADADQNLNENLMILLATAGCNYIMGMPLGDDIMLNYQTTAFHDTATVRQLLNLRPSPEFERWLETMGIMANGRLTKRAGDPSLFF
Protein: Mitogen-activated protein kinase 13 (MAP kinase 13) (MAPK 13) (EC 2.7.11.24) (Mitogen-activated protein kinase p38 delta) (MAP kinase p38 delta) (Stress-activated protein kinase 4) (O15264)
Organism: Homo sapiens (Human)
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1 and ATF2. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK13 is one of the less studied p38 MAPK isoforms. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Plays a role in the regulation of protein translation by phosphorylating and inactivating EEF2K. Involved in cytoskeletal remodeling through phosphorylation of MAPT and STMN1. Mediates UV irradiation induced up-regulation of the gene expression of CXCL14. Plays an important role in the regulation of epidermal keratinocyte differentiation, apoptosis and skin tumor development. Phosphorylates the transcriptional activator MYB in response to stress which leads to rapid MYB degradation via a proteasome-dependent pathway. MAPK13 also phosphorylates and down-regulates PRKD1 during regulation of insulin secretion in pancreatic beta cells.
Interaction partners:
- MAP kinase-activated protein kinase 3
- Cyclic AMP-dependent transcription factor ATF-2
- MAP kinase-activated protein kinase 2
- Dual specificity mitogen-activated protein kinase kinase 6
- Dual specificity mitogen-activated protein kinase kinase 3
- Transcription factor Jun
- Heat shock protein beta-2
- Protein c-Fos
- Dual specificity protein phosphatase 1
- Dual specificity mitogen-activated protein kinase kinase 1
Sequence:
MSLIRKKGFYKQDVNKTAWELPKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFYDFYLVMPFMQTDLQKIMGMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEAQQPFDDSLEHEKLTVDEWKQHIYKEIVNFSPIARKDSRRRSGMKL
Protein: Inclusion membrane protein G (A0A0H3MGR4)
Organism: Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
Function: Inclusion membrane protein probably involved in early modification events of the chlamydial inclusion.
Subcellular location: Secreted {ECO:0000305|PubMed:10447885}. Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:11207546, ECO:0000269|PubMed:12065525}; Multi-pass membrane protein {ECO:0000255}. Note=Secreted, probably by a type III secretion system (Probable). Localized in the inclusion membrane (PubMed:10447885, PubMed:11207546, PubMed:11260479, PubMed:12065525). Inclusion membrane staining is punctate (PubMed:10447885). The C-terminus faces the host cytosol (PubMed:11207546). {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:11207546, ECO:0000269|PubMed:11260479, ECO:0000269|PubMed:12065525, ECO:0000305|PubMed:10447885, ECO:0000305|PubMed:12694613}.
Interaction partners:
Sequence:
MICCDKVLSSVQSMPVIDKCSVTKCLQTAKQAVVLALSLFAVFASGSLSILSAAVLFSGTAAVLPYLLILTTALLGCVYAVIVLLRSLSAVVQSCKKRSPEEIEGAARPSDQQESGGRLSEESASPQASPTSSTLRLESAFRSIGDSVSGAFDDINKDNSRSRSRSF
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 (6PF-2-K/Fru-2,6-P2ase 2) (PFK/FBPase 2) (6PF-2-K/Fru-2,6-P2ase heart-type isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (P70265)
Organism: Mus musculus (Mouse)
Function: Synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- Fructose-1,6-bisphosphatase isozyme 2
- 6-phosphofructo-2-kinase/fructose-2, 6-biphosphatase 3 splice variant 2
- Fructose-2,6-bisphosphatase TIGAR
- ATP-dependent 6-phosphofructokinase, liver type
- Fructose-1,6-bisphosphatase 1
- ATP-dependent 6-phosphofructokinase, platelet type
- RAC-alpha serine/threonine-protein kinase
- ATP-dependent 6-phosphofructokinase, muscle type
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1
- RAC-beta serine/threonine-protein kinase
Sequence:
MSENSTFSTEDSCNSSYKPHASNLRRAGKTCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYQSYDFFRHDNEEAMKIRKQCALVALEDVKAYFTEESGQIAVFDATNTTRERRDMILNFAKQNAFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYQPLDPDNYDKDLSFIKVMNVGQRFLVNRVQDYIQSKIVYYLMNIHVHPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAHALKKFLEEQEIQDLKVWTSQLKRTIQTAESLGVTYEQWKILNEIDAGVCEEMTYSEIEQRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNILVISHQAVMRCLLAYFLDKGADELPYLRCPLHIIFKLTPVAYGCKVETITLNVDAVDTHRDKPTHNFPKSQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRALDMQEGADQPKTQVSIPVV
Protein: Sarcoplasmic calcium-binding protein (SCP) (allergen Scy p 4.0101) (I2DDG2)
Organism: Scylla paramamosain (Mud crab)
Function: Like parvalbumins, SCPs seem to be more abundant in fast contracting muscles, but no functional relationship can be established from this distribution.
Interaction partners:
Sequence:
MAYSWDNRVKYVVRYMYDIDNNGYLDKNDFECLALRNTLIEGRGEFNSDAYANNQKIMSNLWNEIAELADFNKDGQVTVDEFKQAVQNLCCGKSFDGFPPCFKTVIGRLFKTIDINGDGLAGVDEYRLDCISRSAFSSVKEIDDAYAKLCTDDDKKAGGISLNRYQELYAQFISNPDEKCNAVYLFGPLKEVQ
Protein: WD repeat-containing protein 18 (U3KQC1)
Organism: Homo sapiens (Human)
Subcellular location: Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190, ECO:0000256|RuleBase:RU369067}. Nucleus, nucleolus {ECO:0000256|RuleBase:RU369067}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369067}. Cytoplasm {ECO:0000256|RuleBase:RU369067}. Note=Mainly found in the nucleoplasm, with low levels detected in the cytoplasmic and chromatin fractions. {ECO:0000256|RuleBase:RU369067}.
Interaction partners:
Sequence:
XAPMEVAVCTDSAAPMWSCIVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSVLQADPSRIPAPRHVWSHHALPITDLHCGFGGPLARVATSSLDQTVKLWEVSSGELLLSVLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVALKGPVTNAAILLAPVSMLSSDFRPSLPLPHFNKHLLGAEHGDEPRHGGLTLRLGLHQQGSEPSYLDRTEQLQAVLCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRPAK
Protein: Apolipoprotein A-IV (Apo-AIV) (ApoA-IV) (Apolipoprotein A4) (P06728)
Organism: Mus musculus (Mouse)
Function: May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons.
Subcellular location: Secreted.
Interaction partners:
- Apolipoprotein A-II
- Apolipoprotein B-100
- Apolipoprotein C-III
- Phosphatidylcholine-sterol acyltransferase
- Apolipoprotein A-I
- Apolipoprotein C-II
- Apolipoprotein E
- Apolipoprotein M
- Beta-2-glycoprotein 1
- Clusterin
Sequence:
MFLKAAVLTLALVAITGTRAEVTSDQVANVVWDYFTQLSNNAKEAVEQFQKTDVTQQLSTLFQDKLGDASTYADGVHNKLVPFVVQLSGHLAQETERVKEEIKKELEDLRDRMMPHANKVTQTFGENMQKLQEHLKPYAVDLQDQINTQTQEMKLQLTPYIQRMQTTIKENVDNLHTSMMPLATNLKDKFNRNMEELKGHLTPRANELKATIDQNLEDLRRSLAPLTVGVQEKLNHQMEGLAFQMKKNAEELQTKVSAKIDQLQKNLAPLVEDVQSKVKGNTEGLQKSLEDLNRQLEQQVEEFRRTVEPMGEMFNKALVQQLEQFRQQLGPNSGEVESHLSFLEKSLREKVNSFMSTLEKKGSPDQPQALPLPEQAQEQAQEQAQEQVQPKPLES
Protein: DNA repair endonuclease XPF (EC 3.1.-.-) (DNA excision repair protein ERCC-4) (DNA repair protein complementing XP-F cells) (Xeroderma pigmentosum group F-complementing protein) (Q92889)
Organism: Homo sapiens (Human)
Function: Catalytic component of a structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair, and which is essential for nucleotide excision repair (NER) and interstrand cross-link (ICL) repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:19596235}. Chromosome {ECO:0000269|PubMed:11790111}. Note=Localizes to sites of DNA damage. {ECO:0000269|PubMed:11790111}.
Interaction partners:
- DNA repair protein complementing XP-A cells
- Structure-specific endonuclease subunit SLX4
- DNA excision repair protein ERCC-1
- Structure-specific endonuclease subunit SLX1
- DNA excision repair protein ERCC-5
- Structure-specific endonuclease subunit MUS81
- UV excision repair protein RAD23 homolog B
- DNA mismatch repair protein Msh2
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
Sequence:
MESGQPARRIAMAPLLEYERQLVLELLDTDGLVVCARGLGADRLLYHFLQLHCHPACLVLVLNTQPAEEEYFINQLKIEGVEHLPRRVTNEITSNSRYEVYTQGGVIFATSRILVVDFLTDRIPSDLITGILVYRAHRIIESCQEAFILRLFRQKNKRGFIKAFTDNAVAFDTGFCHVERVMRNLFVRKLYLWPRFHVAVNSFLEQHKPEVVEIHVSMTPTMLAIQTAILDILNACLKELKCHNPSLEVEDLSLENAIGKPFDKTIRHYLDPLWHQLGAKTKSLVQDLKILRTLLQYLSQYDCVTFLNLLESLRATEKAFGQNSGWLFLDSSTSMFINARARVYHLPDAKMSKKEKISEKMEIKEGEETKKELVLESNPKWEALTEVLKEIEAENKESEALGGPGQVLICASDDRTCSQLRDYITLGAEAFLLRLYRKTFEKDSKAEEVWMKFRKEDSSKRIRKSHKRPKDPQNKERASTKERTLKKKKRKLTLTQMVGKPEELEEEGDVEEGYRREISSSPESCPEEIKHEEFDVNLSSDAAFGILKEPLTIIHPLLGCSDPYALTRVLHEVEPRYVVLYDAELTFVRQLEIYRASRPGKPLRVYFLIYGGSTEEQRYLTALRKEKEAFEKLIREKASMVVPEEREGRDETNLDLVRGTASADVSTDTRKAGGQEQNGTQQSIVVDMREFRSELPSLIHRRGIDIEPVTLEVGDYILTPEMCVERKSISDLIGSLNNGRLYSQCISMSRYYKRPVLLIEFDPSKPFSLTSRGALFQEISSNDISSKLTLLTLHFPRLRILWCPSPHATAELFEELKQSKPQPDAATALAITADSETLPESEKYNPGPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQDELTSILGNAANAKQLYDFIHTSFAEVVSKGKGKK
Protein: Zinc finger protein Elbow (Q9VJS8)
Organism: Drosophila melanogaster (Fruit fly)
Function: May negatively regulate Notch-induced cell proliferation in the eye-head primordium. May act in leg and wing primordia to negatively regulate body-wall specifying genes and thereby promote appendage formation. Required for tracheal development.
Interaction partners:
- Elastin-like, isoform A
- Protein groucho
Sequence:
MLQSSNHHYLRPDYMTAAAAPTAQLDNKSSPLALLAQTCSAIGADTTNPKLLAANIEKSTKQLQHHPKGSSGSGGSGSFGLSQQASMDGSARDKSSPVSSHSSSVSTGSVEQQQLPPAHGSSSSSKPTPTTFKPYEPNNNISNITTAADCGATNLSSNNTSAQQRVKTPKSMTNGGGQRCDSNQSASSQHRESPTAAGSLRRTPTSGLAGGVMQHNGSPGLPPTASTTPGRSNSKESAAMHSPSAAAAAAAAAAQIASSNRLQEAALAAAKEANYVKALHAASQQGSASAAAAAASYYPPGYGSPYSMDLMTASSLMSPHHAMFKASAMNPYLNYARMKGLTEQSMMAATPNVCRDPYCTGCPASPHYINKAAGQPCPAGCPQCEGGGGGGGGSSKSSGSQGGSGGSSSAAAAAAAAAASSYHAQLAALAAASQMPYVCSWIGSDAAYCGKRFGTSDDLFQHLRTHTASVPDAVLSAAAAGGIPPNHPLFQRTYPTPPLSPLSAARYHPYGKPSMLPPSLAPPGMPGLPPHPALAQYFAPYSLYGPRMGSSHP
Protein: Quinone-dependent D-lactate dehydrogenase (EC 1.1.5.12) ((R)-lactate:quinone 2-oxidoreductase) (D-lactate dehydrogenase) (D-LDH) (Respiratory D-lactate dehydrogenase) (P06149)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02092, ECO:0000269|PubMed:1092688}. Note=May bind the membrane through electrostatic rather than hydrophobic forces. {ECO:0000305|PubMed:10944213}.
Interaction partners:
- L-lactate dehydrogenase
- D-lactate dehydrogenase
- Pyruvate dehydrogenase
- Formate acetyltransferase 1
- NADP-dependent malic enzyme
- Pyruvate dehydrogenase E1 component
- Probable pyruvate-flavodoxin oxidoreductase
- Lactaldehyde dehydrogenase
- Pyruvate kinase II
- PFL-like enzyme TdcE
Sequence:
MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE
Protein: Uncharacterized protein Rv2644c (P9WL53)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MSPRRTSGGVVPVDRYRIDEGLIVVLVFAGRDERRRTVCFADKFGCVHIGNPDLYRPQTSLPQPLPISSHAISGSRFVETTNRADQQEPIGPNRAELFDQALHAG