wanglab/gogpt-training-data huggingface dataset:
Protein: Pre-mRNA-splicing factor CWC25 (Complexed with CEF1 protein 25) (P53854)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14690591}.
Interaction partners:
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Splicing factor YJU2
- Pre-mRNA-splicing factor BUD31
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor CWC2
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SNT309
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor 8
Sequence:
MGSGDLNLLKSWNPKLMKNRKKVWETEQDLITEQQKLNTRLKEIEKERELNELLNESSKDKPETLKNDLALKKSGLEWMYQDAKLSDEKEDYLLGKKKLDSSILNQPATPPVRAATTISASGAATSISSQKKKSKLLKDDPMSKFKVTKQQRRTPDSTKKRAMSQRGKPLSKPAPDLDY
Protein: Myotubularin phosphatase domain-containing protein (Q585F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDRTTLPVACPSDTQADGACGVLAGGRDGGEHHQRKQSVQPSNWVASPIEMILLKCVLGEVEGSSEELQWQRMRLSGLGPSLLVLARRVELEDVTETDARCYALEVPPKLEVPPVVRQLLASTLTCGDLRVSLQFHWAHSLETSNTPRRNRMDSPAPRFVFFVKTDRSVTIPTVSSVLLSSDGGSKQEQDTGCGGTDFPSEKFAIGESTRLLLTLLRQTSLWNMAFLNHSGVQGSFCNVIQKLGNHDGKTRQVEQVVQAICYLHRVLKERQQEEGKEVDNLMEIIFGWSQMMHETLSAPISTSAHPATDEISFLHVREPTCYDDCDDFGPPKTLQTGRGTDKGERTSHAKGTMPSVKALTPPSFIPTMLRSVSTWSAATSTLGAEESVGDVSSGQQQQQMQEELGNIADDGRRVPEVKQDKELYPVLSVCTDVLVDAFHLQGNQQHVLKTEWSLGDGRRAGTPESSSAAAYAATSNSLEEQLPAVSKSDSSDDNEKAEHAIAAERGGNTNSTIKTKCSGAITGGFLPSLTLRLASGLFSPDVGRQYRRRLSALARGDFFPSRRAMEKADLLQRRLQKTTKVWFYDLFPQHLLAASDATTNAGGTAALYNSGTGLSPGGVGVKANSGHPCYLYLTETDIILASAFDNINRRQASVGRGEERVALRTEKTSRSNEVTNIKSRVVSDSERSGNSDNTNEGSCEPPFSPYGSDSEDNPTSHFNGDSSDSKDYIRLRLVFPRVSLADVQWLTTRDGTPSTVLLLQTRACRRVWLAFHGIDAVSAVHSELIAPMTSSYGNRLLASARRPWRMVGLVLTAGDVLPNPYTPFYLQVIRNILTAFVDLEERGGQKEEERRDKRECEYECEDSTQGRAHHWWLYSVAEEFERQDIPLKQWRITDINIDHKHFTTYPERFVVPNSLHDDRLLHTARLRGRGRVEALSFYYSASEAGLVRAAQPAVIPALYASAASAKALTDPVEEYRNACMRPVHIFDLRSGIRALSSTLVGGGFSLGENRRFCSLENIHHVRESYDSLCEEIFTHNPNFPTAVMKCATAPKRQNTQAGGPTSSLAQLRAQENQPLGKAKMAWVEHIRGLLRTAEDAARLVAGVSEENALFPAKTDVGTSSTMYMWMRAFHSVCRNIGGVKSAAPLPTESQQIPSYTPLQSRKDARLVMVNCSDGWDRTPQVCALSQLLLDPYYRTVEGFLILVEKEFVAFGHPFATRSTCTATGKKSQWDTQNGSSAVSEGSGNCNNGGGNGDTFDEKESSSPSGSPHTLLGGKQNSPIMLQFIDAVYQLLRIYPHCFEFTENFLLLIVDILNAGIVGTFAVNCEADIKRWGVEKHTLSLSQLIALVLATTIPTEGEQLTSLESSIDVRRAYDDGEYRVTNASVDTEATTSPCSHPIPLQSFFKVGYGGSSIYTPNWCPAVGKFSSLCKPRRLCISSDALMYSGLLNPHFSLADNKECVGPLLDPLPLDGITLWERFFMRYSFCYERPQRLRRFSEQSPSTYHAVTVASLRDSFSSTSQRYFHLAVESEQRHSDEGKRLAATNAGPVECCSCASASHSSPAEGREGLESGQQPFTGCTTNQRITRSQPVIHCGVNRGGGAAFTPPARLAGHHSPVPMGAGDPFLRRSFSHAALCESTYSARGQISRRRSGNNSCGRLEGSECSSGASKSCALRQRDPGQQLTKSRSLPFLDERWSSLQQKAAPAGEESRVGRPFSLTSSLGEGSINSPSGTGTEARRSQQQTPAVTPPEPAAPRLHGGYESLLDELEEAFDI
Protein: KAP NTPase domain-containing protein (Q3V2X2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
TPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHIEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGARVSAVDKKGDTPLHVAIRGRSRRLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTGTDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGQQIEPLFQFSWLIVFLILLLCGGLGLVFAFTVDTNLAIAVSLSFLALLYIFFIVIYFGGRQEGESWNWAWALSTRLARHIGYLELLFKLMFVNPPELPEQTTKALPVRFLFTDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDSQGKKKWKKTCCLPSFIIFLFIVGCIIAGITLLAIFRVDPKHLTVNAILISIASIVGLAFVLNCRTWWQVLDSLLNSQRKRLHSAASKLHKLKSEGFMKVLKCEVELMARMAKTIDSFTQNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLRDSNINGHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDISCSEATGVQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQMQRTITRQMSFDLTKLLVTEDWFSDISPQTMRRLLNIVSVTGRLLRANQITFNWDRLASWINLTEQWPYRTSWLILYLGETEGIPDQMTLKTIYERISKNIPTTKDVEPLLEIDGDIRNFEVFLSSRTPVLVARDVKTFLPCTVNLDPKLREIIADVRAAREQINIGGLAYPPLPLHEAPPRPPSGYSQPASVCSSSASFNGPFPGGVVSPQPHSSYYSGLSGPQHPFYNRPFFAPYLYTPRYYPGGSQHLISRSSVKTSLPRDQNNGLASVPATGTSLLLSSMTVDIVCEKLRQIEGLDQGMLPQYCTTIKKANINGRVLAQCNIDELKKEMAMNFGDWHLFRSMVLEMRSVENQVVPEDPRFLNENSSAPVAHGESARRTSHSELPHTELSSQTPYTLNFSFEELNTLGLDEGAPRHSNLSWQEENAAPVLDRQRFRRSSLN
Protein: Choline transporter-like protein 1 (Solute carrier family 44 member 1) (CD antigen CD92) (Q6X893)
Organism: Mus musculus (Mouse)
Function: Choline transporter. May be involved in membrane synthesis and myelin production.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19357133}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:19357133}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- High affinity choline transporter 1
Sequence:
MGCCSSASAAQSSKREWKPLEDRSCTDIPWLLLFVLFCIGMGFICGFSVATGAAARLVSGYDSYGNICGQRNAKLEAIPNSGLDHTHRKYVFFLDPCNLDLINRKIKSIALCVAACPRQELKTLSDVQKFAEINGSALCSYNIKPSEYTLTSKSSGFCPKLPVPASAPIPFFHRCAPVNISCYAKFAEALITFVSDNSVLHRLISGVMTSKEIILGLCLLSLVLSMILMVIIRYISRVLVWILTVLVILGSLGGTGVLWWLYAKQRRSPKEAVIPEQLQIAEDNLRALLIYAISATVFTVILFLIMLVMRKRVALTIALFHVAGKVFIHLPLLVFQPFWTFFALVLFWAYWIMTLLFLGTTGSAVQNEQGFVEYKISGPLQYMWWYHVVGLIWISEFILACQQMTVAGAVVTYYFTRDKRNLPFTPILASVNRLIRYHLGTVAKGSFIITLVKIPRMVLMYIHSQLKGKENACARCMLKSCICCLWCLEKCLSYLNQNAYTATAINSTNFCTSAKDAFVILVENALRVAAINTVGDFMLFLGKVLIVCSTGLAGIMLLNYQQDYTVWVLPLIIVCLFAFLVAHCFLSIYEMVVDVLFLCFAIDTKYNDGSPGREFYMDKVLMEFVENSRKAMKEAGKGGAADARELKPMLRKR
Protein: Cytoskeleton protein RodZ (P27434)
Organism: Escherichia coli (strain K12)
Function: Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:19008860}; Single-pass type II membrane protein {ECO:0000269|PubMed:19008860}. Note=Forms helical filaments along the long axis of the cell.
Interaction partners:
- Cell shape-determining protein MreB
- Rod shape-determining protein MreD
- Cell shape-determining protein MreC
- Peptidoglycan glycosyltransferase MrdB
- Peptidoglycan D,D-transpeptidase MrdA
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Protein translocase subunit SecA
- Cell division protein FtsZ
- Penicillin-binding protein 1A
- Large ribosomal subunit protein uL29
Sequence:
MNTEATHDQNEALTTGARLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPADLASTFLRGYIRSYARLVHIPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMTFTWLVLFVVIGLSGAWWWQDRKAQQEEITTMADQSSAELSSNSEQGQSVPLNTSTTTDPATTSTPPASVDTTATNTQTPAVTAPAPAVDPQQNAVVSPSQANVDTAATPAPTAATTPDGAAPLPTDQAGVTTPVADPNALVMNFTADCWLEVTDATGKKLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEQSPAQ
Protein: PAC2 family protein (O07213)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MARDQGADEAREYEPGQPGMYELEFPAPQLSSSDGRGPVLVHALEGFSDAGHAIRLAAAHLKAALDTELVASFAIDELLDYRSRRPLMTFKTDHFTHSDDPELSLYALRDSIGTPFLLLAGLEPDLKWERFITAVRLLAERLGVRQTIGLGTVPMAVPHTRPITMTAHSNNRELISDFQPSISEIQVPGSASNLLEYRMAQHGHEVVGFTVHVPHYLTQTDYPAAAQALLEQVAKTGSLQLPLAVLAEAAAEVQAKIDEQVQASAEVAQVVAALERQYDAFIDAQENRSLLTRDEDLPSGDELGAEFERFLAQQAEKKSDDDPT
Protein: Dual specificity protein kinase splA (EC 2.7.10.2) (Non-receptor tyrosine kinase spore lysis A) (Tyrosine-protein kinase 1) (P18160)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Essential for spore differentiation.
Interaction partners:
- BRCA1-associated protein
- Armadillo repeat-containing protein
Sequence:
MNSKNDLFIGFFFFFYNYYYYYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIYIIVIIGLDPQQNHPSLKIPPPPSPTSPYVRRHARQHSRSNSSNSPGELTGGVEIIQQQNSINTQTSPPTSTSPNTVPPPPPTNTTTSSTTITRNSNNINNSNGGIINSSSGSNINNSSSSGVINTNINNSGGNISPTSNSLPSSNNNILYTSSGSNSGNNNNNNNTINISSGSSGINNSSNSNINNNNNNNSSSSSGIHASGSLTAIPTNTNSNSSIFHSSNSVNRINKSNYSADSLVLPPNRISQVPQSQTQPQLQISPSTSFSSQQQQQQQLQQQLQLQQQLQQQIQQQQQIQQQQNLHFTYSKTFTSGQPNTLVNLSSPPPQSKHLHVSSDHSFFNEVLTPTPVIHNSTNQNNQLLFGDSDPLSFLEYNNFINRYQPALKNNQPVSSYRQQQQIQHQIQLQQIQQQQQQQQQIQQQQLQQQQQIQQQQIQQQQQQIQQQQQQQQQQQQQQQQLQQIQPPPTIQPPPQQTTPTLRGNRSSGNLSGLNSFSLKQSTDSLTPPPNSQQSTVSSNSTPIAATPISPLTAPTSPPPPPPPPTNFNSKFNNNNNNNINNSSNNNTTVPPSPPPIIVLPKSPSSRSPRPASAPVPSAPFLVNNRVINTSSSSNISTNNTDLNLSSSSSSSPPLNISTASPSKSEDSPPTVSPSYKQQQQQQQQQQQQQQQLNNSSNSSYSPKPRSPSVSSPPPSSISPNSSPIGSPNISFHHHQQHQIPPPPPVLSNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTNHTNKKEGDSSWFNMSFKFFKKKLVPSNEYRWDLRKSNSLTLNIEDKSRCSYRLPTSGSKGIAKSTQPFSSSFTYFELFITNGNGDKICFGLTTNDHPIEVYPGNYQGSYGYSGDGKCYFGTNEGRVYGPSFSSGDVVGCGYDSSSKTLYFTKNGVYLGVAAQKVNLIGLYPTVGLQNPGESVVINFFGPFSYRGAPEKPSKQSTIKDSGGSSIIPSEDLIPKEEFEVCRWSEKKNYHGKHVVVRNRTAFLPLDSPKDTIGGVRATQPFGEGFCYFEVIIDQLDKGQLSIGLANLEYPTFYHVGWMPRSYGYHNDDGRKFRWREEPGVNEGESYGSSYKKGDIIGCGLSFTSREIFFTKNGMYLGTAFSNVYGVFYPSVAFNEPGISITGVFGPPFKFSQVTLMLKNVNSTSILVPNGNNNNNSNNNNNNNNNNIIGNGKITTTTTTSTSPSSINNNEDISSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNSSNTNNNNINNTTNNNNSNSNNNNNNNNSNSNSNSNNNNINNNNNNNNNNNNIYLTKKPSIGSTDESSTGSLGGNNSSGNNNSSSGSIGNNSSIIKQRSPPHSINGPLMLPPSSTNNNNNIYSSYNSTTAGSSTTILPTLNHPIFGNTTSNNNSSSTLSVGGNNNLLGRHCQSLPITASTNHTLSSSLGVSFSSPSSSPKTSPRKIVNSSEDLGFVQTFQDQDGQPPSAWRRCGKSIKTKDDITLTIIKKKTSVAMADRPFSSNSSSTICYFEVYLEGHDKKGSITVGLSHSTYPFIKHIGREPKSYGFSSEGEKYGGSEIGEPYGPFFFFDGDSIASSCVIGCGINTSTRDIFFTKNGHYLGVAFSRVTSDPLYPSISFRGVVGGLCVATFPGGHFRFNIEDLPGISPSVWTEALGPDRQGSGFKNWAPNDVAIWLESFNYGQYRKNFRDNNISGRHLEGITHAMLKNDLGIEPYGHREDIINRLNRMIQIWNDKSPDSYPKIAIDSSDKIRWPASGGSSGGINISGGVVIGSSSGSDDGITEISSSSKNIRPYKSYTQKEIEDRNRRSTISGGEKKNKYYIDNQMDPHQIGSMDSDGLLPDFGQGPPDEKNSSKTLSNEQIRYLQQRKDEPPIAISSTGNGGSVSSTGGSSGFLTFPSSNSLTHPPQRDKPTQEFTHLPPITSNYKGITNTGQPHKSFDQPLELFPRHSAFSNNGNNGNNNNNNNNNNIKANQQQQQQSSYQQSQTQQQQQHITSTSTSTTNKWIDPFGGWETQSSLSHPPSRPPPPPPPPPQLPVRSEYEIDFNELEFGQTIGKGFFGEVKRGYWRETDVAIKIIYRDQFKTKSSLVMFQNEVGILSKLRHPNVVQFLGACTAGGEDHHCIVTEWMGGGSLRQFLTDHFNLLEQNPHIRLKLALDIAKGMNYLHGWTPPILHRDLSSRNILLDHNIDPKNPVVSSRQDIKCKISDFGLSRLKMEQASQMTQSVGCIPYMAPEVFKGDSNSEKSDVYSYGMVLFELLTSDEPQQDMKPMKMAHLAAYESYRPPIPLTTSSKWKEILTQCWDSNPDSRPTFKQIIVHLKEMEDQGVSSFASVPVQTIDTGVYA
Protein: AP-1 complex subunit sigma-1A (Adaptor protein complex AP-1 subunit sigma-1A) (Adaptor-related protein complex 1 subunit sigma-1A) (Clathrin assembly protein complex 1 sigma-1A small chain) (Clathrin coat assembly protein AP19) (Golgi adaptor HA1/AP1 adaptin sigma-1A subunit) (HA1 19 kDa subunit) (Sigma 1a subunit of AP-1 clathrin) (Sigma-adaptin 1A) (Sigma1A-adaptin) (P61966)
Organism: Homo sapiens (Human)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:9733768}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral membrane protein {ECO:0000269|PubMed:9733768}; Cytoplasmic side {ECO:0000269|PubMed:9733768}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:9733768}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Interaction partners:
- AP-1 complex subunit mu-1
- AP-1 complex subunit beta-1
- AP-1 complex subunit gamma-1
- AP-1 complex subunit mu-2
- AP-1 complex subunit gamma-like 2
- AP-2 complex subunit beta
- AP-4 complex subunit mu-1
- AP-2 complex subunit mu
- AP-4 complex subunit beta-1
- AP-4 complex subunit epsilon-1
Sequence:
MMRFMLLFSRQGKLRLQKWYLATSDKERKKMVRELMQVVLARKPKMCSFLEWRDLKVVYKRYASLYFCCAIEGQDNELITLELIHRYVELLDKYFGSVCELDIIFNFEKAYFILDEFLMGGDVQDTSKKSVLKAIEQADLLQEEDESPRSVLEEMGLA
Protein: Solute carrier family 25 member 44 (Q8BGF9)
Organism: Mus musculus (Mouse)
Function: Mitochondrial solute transporter which transports branched-chain amino acid (BCAA; valine, leucine and isoleucine) into mitochondria in brown adipose tissue (BAT). BAT is involved in BCAA catabolism and actively utilizes BCAA in the mitochondria for thermogenesis.
Subcellular location: Mitochondrion membrane {ECO:0000305|PubMed:31435015}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEDKRNIQIIEWEHLDKKKFYVFGVAMTMMIRVSVYPFTLIRTRLQVQKGKSLYHGTFDAFVKILRADGVAGLYRGFLVNTFTLISGQCYVTTYELTRKFVADYSQSNTVKSLVAGGSASLVAQSITVPIDVVSQHLMMQRKGEKMGRFQVHGNLEGQGVIAFGQTKDIIRQILRADGLRGFYRGYVASLLTYIPNSAVWWPFYHFYAEQLSRLCPQECPHIVFQAISGPLAAATASILTNPMDVIRTRVQVEGKSSIVLTFRQLMAEEGPWGLMKGLSARIISATPSTIVIVVGYESLKKLSLRPELVDSRHW
Protein: Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) (G3MU82)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQCSPDPEDLLIVPTHDIPSYDESLDPFGPEGHLSLDIDCFSKFMSRSDNRIMSKPIIVRGIPWRILAICRNQQGSRHSMNSRVNRSNFNFGFFLQCNNDELLQKRGMWRCYGTAVLEVLNADGPSIQKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDGYVVNDTIKLRCRFTADVPTGANYMWDSKRHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGTEPNESNIVLAMQRVFYELQMASEAVETNSLTRAFGWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYCGVEQKINERFSFPEKMNLASCCELGPMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHESAVDPTSSAKWCKFDDDVVSRTTTDDAIVSNFGGEKTMNSSAYMLVYVRDNAIDQFLAPIPDSQIPQSVSRTFEMERLHRNREKKKLEEEQLCMGIVLVTPDIVASNHSFDLVDQSIVHDSIPHETVWKHMFTAELYQFVHDRLFEKSAMQKIDMFDSDDEARQARRDNLRRIKSKKFNFRLWRMTDSYSLERTTQKLTSRLRPSEFIDCKTDTRLDTLLSQDFETIYVEFSNNIERPLCEYDTARDLLFFVKYYDTMTDKFTIIGHTMFDCHKRFNLYRSMLCEMIGLPADTELKYYMEHAASYLELVDLTQNYSIGRLVEEQDGGILVVEKVETSTSTQNAKQKMNELFLDVEVEFVQSFYNKKPEEEPFEQFVKRICLDDKLFTVAEEIGARLNVDPKKVLIWTRVSGSRFEPFFDDYMLNTCKGLMTRPVHDPRAYKRYRVQYAIMPFDIDEISKHRIQTKLFWQLPNGHVEELTLFPLKEGTVIDIINEAKRYYPFVEGGSGKFRLLQIGAPPLSNQRVYQIYGENTLISDLDQRTMYKLQALHCRLEEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRLRRKLNDVSDADFAKYKFALLSRDKLQLCRTIEFNNGEKVNLADMANQTTGVPQVYIGLDHKSPIQHSSEAAIRILN
Protein: Uncharacterized protein (Q57YJ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein kinase, putative
- Chromatin assembly factor 1 subunit B, putative
- Protein kinase, putative
- Aurora kinase
- Histone H3 variant
- Histone H3, putative
- Protein kinase, putative
- cyclin-dependent kinase
- Histone H4
- Histone H4
Sequence:
MTTAGQSDAFTRVSLHSVTALGKCPAPFSDPIAVKVVLEVFGCPPKHSIDVKFTWKPIWDFPVDQVLDEFEVGPLATVGKHELVLHSDPPDVAKIPDPTGPTALTIAFTYRGKQFLHIGYNAVVLCEGEMPDVFEDAAMLSRQLTQCFKKETTIAWDEDHEDVEEKTVINGKDNDISDVKEKDHNGHAAYDDEAKVPEGVSPTKKKARCEGSLSQEGEKEKHHR
Protein: Transcriptional activator protein LysR (P03030)
Organism: Escherichia coli (strain K12)
Function: This protein activates the transcription of the lysA gene encoding diaminopimelate decarboxylase. LysR is also a negative regulator of its own expression.
Subcellular location: Cytoplasm.
Interaction partners:
- Probable HTH-type transcriptional regulator LrhA
- Diaminopimelate decarboxylase
- DNA-binding transcriptional dual regulator OxyR
- HTH-type transcriptional regulator HdfR
- HTH-type transcriptional activator AaeR
- HTH-type transcriptional regulator TdcA
- HTH-type transcriptional regulator XapR
Sequence:
MAAVNLRHIEIFHAVMTAGSLTEAAHLLHTSQPTVSRELARFEKVIGLKLFERVRGRLHPTVQGLRLFEEVQRSWYGLDRIVSAAESLREFRQGELSIACLPVFSQSFLPQLLQPFLARYPDVSLNIVPQESPLLEEWLSAQRHDLGLTETLHTPAGTERTELLSLDEVCVLPPGHPLAVKKVLTPDDFQGENYISLSRTDSYRQLLDQLFTEHQVKRRMIVETHSAASVCAMVRAGVGISVVNPLTALDYAASGLVVRRFSIAVPFTVSLIRPLHRPSSALVQAFSGHLQAGLPKLVTSLDAILSSATTA
Protein: Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13) (P45452)
Organism: Homo sapiens (Human)
Function: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:8576151}. Secreted {ECO:0000269|PubMed:8576151}.
Interaction partners:
- Metalloproteinase inhibitor 2
- Runt-related transcription factor 2
- Aggrecan core protein
- Collagen alpha-1
- Plasminogen
- A disintegrin and metalloproteinase with thrombospondin motifs 3
- A disintegrin and metalloproteinase with thrombospondin motifs 4
- A disintegrin and metalloproteinase with thrombospondin motifs 5
- Metalloproteinase inhibitor 1
- Collagen alpha-1
Sequence:
MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC
Protein: Probable alpha-1,6-mannosyltransferase MNN10 (EC 2.4.1.-) (Bud emergence delay protein 1) (Mannan polymerase II complex MNN10 subunit) (M-Pol II subunit MNN10) (P50108)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for polarized growth and efficient budding.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type II membrane protein.
Interaction partners:
- Putative glycosyltransferase HOC1
- Mannan polymerase complexes subunit MNN9
- Mannan polymerase II complex ANP1 subunit
- Probable alpha-1,6-mannosyltransferase MNN11
- Mannan polymerase I complex VAN1 subunit
- Alpha-1,2-mannosyltransferase MNN2
- Dolichyl-phosphate-mannose--protein mannosyltransferase 2
- Initiation-specific alpha-1,6-mannosyltransferase
- Dolichyl-phosphate-mannose--protein mannosyltransferase 5
- Dolichyl-phosphate-mannose--protein mannosyltransferase 3
Sequence:
MSSVPYNSQLPISNHLEYDEDEKKSRGSKLGLKYKMIYWRKTLCSSLARWRKLILLISLALFLFIWISDSTISRNPSTTSFQGQNSNDNKLSNTGSSINSKRYVPPYSKRSRWSFWNQDPRIVIILAANEGGGVLRWKNEQEWAIEGISIENKKAYAKRHGYALTIKDLTTSKRYSHEYREGWQKVDILRQTFREFPNAEWFWWLDLDTMIMEPSKSLEEHIFDRLETLADRELKSFNPLNLRDDIPYVDYSEEMEFLITQDCGGFNLGSFLIKNSEWSKLLLDMWWDPVLYEQKHMVWEHREQDALEALYENEPWIRSRIGFLPLRTINAFPPGACSEYSGDSRYFYSEKDHDFVVNMAGCNFGRDCWGEMQYYTTLMEKLNRKWYTRFFFP
Protein: Centrosomal protein CEP104 N-terminal domain-containing protein (Q57Z38)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVGLIPYDIVYRSSEDNEFPITGLGNGLATSSENVECFSTTNPSNHAVAEQHCSGKGWQSARFASMPQELVLRFPGNAELVNLRILSHESKIMSKMEVRLYALDDGDEVNGVGGHYGLEAPSFREVRFLKLGSVNFSSNEHTNYRSKERKTVHLHAKAYFLKLLFHAPHQNAFNRFKQIGVYSIECSGQISKRIPRHVDHAVVSSCIVSQTPVERDHTRESSNYNGSGVKLPPLQLEQQQYQLQHLLQEQDRQGEGERSPVETPVRNIITQDEGMPAFRSVRILEFEDFFVRRSAELLMLKNQAISMDDFDTAKACQDRIKLMNRRSKRIYQAEQDKVQAIIDEDFDAAKEAKQQMDTMIEKVYNDVQVPQLRQVPDPLEYSSDTFSEDAPQDGRRSGAEAIGLSIGCSGDRYGMCGERNEKMCWSAERQKLAPEGEYQDLPSGPTGDSGMSPFDGAGSDLGPSIFDDFDKDTGQKLDAQNIWHQKGQEIADAKCNNDDWNAQERPPGANQDVSVSDGTDEYAIGGRLQPWEEGVVREIMEASGETDMPKLPDVGGRKFSEMQNLNNVVGLFTTACLYSSNFKLRESALSVLASKMTTLYESSPVSIEEGVLRYLDLSGYGLQDHIPAVANAACAFVRSVLEDEANVFEEVMCPVVNLLPRLLCCAADYNPRLREEAMSTLALFVRKPEIGKGVILSAVLADPVDKDRRRLSHTHARTQLARLSVLKDLAANGGLQVRGSAGSMGKHNENAWSRLLQPCLNHQSSEVRDLAVSTASYLISEEKLVLTKRRAGEIDNVSIRDQLKAAAELLRAQRDGEAPSSPNSAAAFTPFSMRQRTPNVKPEKALGKKCRKAPKAQERQV
Protein: Vesicle transport through interaction with t-SNAREs homolog 1A (Vesicle transport v-SNARE protein Vti1-like 2) (Vti1-rp2) (Q9JI51)
Organism: Rattus norvegicus (Rat)
Function: V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. Involved in vesicular transport from the late endosomes to the trans-Golgi network. Along with VAMP7, involved in an non-conventional RAB1-dependent traffic route to the cell surface used by KCNIP1 and KCND2 (By similarity). May be concerned with increased secretion of cytokines associated with cellular senescence.
Subcellular location: Membrane {ECO:0000269|PubMed:9705316}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9705316}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:9705316}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9705316}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:9705316}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9705316}. Golgi apparatus membrane {ECO:0000269|PubMed:9705316}; Single-pass type IV membrane protein {ECO:0000269|PubMed:9705316}. Note=Mainly associated with the Golgi apparatus. Enriched in small synaptic vesicles and clathrin-coated vesicles from nerve terminals. Isoform 1/VTI1A localizes to the cell bodies of hippocampal neurons as well as to nerve terminals.
Interaction partners:
- Syntaxin-5
- Syntaxin-6
- Syntaxin-16
- Vesicle-associated membrane protein 4
- Synaptobrevin homolog YKT6
- Vesicle-associated membrane protein 8
- Syntaxin-12
- Vesicle-associated membrane protein 7
- Vesicle-associated membrane protein 3
- BET1 homolog
Sequence:
MSADFEGYEQDFAVLTAEITSKISRVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGMLRRIIQNRILLVILGIIVVITILTAITFFVRGH
Protein: Beta-defensin 8 (BD-8) (mBD-8) (Defensin, beta 8) (Defensin-related peptide) (Defr1) (Q91V82)
Organism: Mus musculus (Mouse)
Function: A synthetic peptide displays antimicrobial activities against S.aureus, P.aeruginosa, E.coli and B.cepacia. The antimicrobial activity against S.aureus, E.coli and B.cepacia is reduced in raised concentration of NaCl, but its action against P.aeruginosa is independent of NaCl concentration.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MRIHYLLFTFLLVLLSPLAAFSQKINEPVSCIRNGGICQYRCIGLRHKIGTCGSPFKCCK
Protein: D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (O08651)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
Interaction partners:
- Phosphoserine aminotransferase
- Phosphoserine phosphatase
- Phosphoglycerate mutase 1
- Serine hydroxymethyltransferase
- Phosphoglycerate mutase 2
- Serine hydroxymethyltransferase
- Asparagine synthetase
- Methylenetetrahydrofolate dehydrogenase
- Glycine cleavage system P protein
- Alanine--glyoxylate aminotransferase
Sequence:
MAFANLRKILISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGVLVMNTPNGNSLSAAELTCGMLMCLARQIPQATASMKDGKWDRKKFMGTELNGKTLGILGLGRIGREVAARMQAFGMKTVGYDPIISPEVAASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMHAWAGSPKGTIQVVTQGTSLKNAGTCLSPAVIVGLLREASKQADVNLVNAKLLVKEAGLNVTTSHSPGVPGEQGIGECLLTVALAGAPYQAVGLVQGTTPMLQMLNGAVFRPEVPLRRGQPLLLFRAQPSDPVMLPTMIGLLAEAGVQLLSYQTSKVSDGDTWHVMGLSSLLPSLDAWKQHVSEAFQFCF