wanglab/gogpt-training-data huggingface dataset:
Protein: Major sperm protein (O76615)
Organism: Caenorhabditis elegans
Subcellular location: Cell projection, pseudopodium {ECO:0000256|ARBA:ARBA00037818}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Integral membrane protein
- Spermatocyte protein spe-27
- Spermatocyte protein spe-8
- Serine/threonine-protein kinase spe-6
Sequence:
MALESIGQRSKQFYYDHAAGDTATQKHISHEKSQINLEMTGEPGGGERRYFEGLVGTKELVILSALTMCLYLINGEYAQTICTALTSVPPALFSYRVLTNQMTDKQGYHSILFYWTLYGLTALIDQFAGTAQGYNLCKCGLLGVFFFHAVRSNLSAVPATWKFAEKLEVLTSLVSQLETDGFLRNYDAMTPTITQFSEDDSLQYIFPVEENLEMSTACSFVPSLDMQSTQNPSPSTLKTMKIEESRNFQTMSAMTLACGGAAADIVTVPADRITFAAGKLEEVIRVTNVSQSHIMFALKTNADAYLIAAPTSGVLLSGQSMTIRVGVTGNYFDDFSDPGVSIDKLAIDYALIPSRSYSKFSSEFFYSQNRRRLAIRVFYQ
Protein: Neuritin-like protein (Q496H8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MMRCCRRRCCCRQPPHALRPLLLLPLVLLPPLAAAAAGPNRCDTIYQGFAECLIRLGDSMGRGGELETICRSWNDFHACASQVLSGCPEEAAAVWESLQQEARQAPRPNNLHTLCGAPVHVRERGTGSETNQETLRATAPALPMAPAPPLLAAALALAYLLRPLA
Protein: Cyclin-G-associated kinase (EC 2.7.11.1) (DnaJ homolog subfamily C member 26) (P97874)
Organism: Rattus norvegicus (Rat)
Function: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14976}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14976}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O14976}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O14976}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles. {ECO:0000250|UniProtKB:O14976}.
Interaction partners:
- Clathrin heavy chain 1
- Clathrin heavy chain linker domain-containing protein 1
- Huntingtin-interacting protein 1-related protein
- Clathrin light chain A
- Ras-related protein Rab-7L1
- Dynamin-2
- Clathrin light chain B
- Phosphatidylinositol-binding clathrin assembly protein
- BAG family molecular chaperone regulator 5
- Heat shock cognate 71 kDa protein
Sequence:
MSLLQSALDFLAGPGSLGGAAGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDLGSGREYALKRLLSNEEEKNRAIIQEVCFLKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLRRVECKGPLSCDSILKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQKRAMVEEEITRNTTPMYRTPEIVDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPVNDTRYTVFHDLIRGMLKVNPEERLSIAEVVRQLQEIAAARNVNPKAPITELLEQNGGYGNSGPSRAQPPSGGPVNSSGVLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESAIKNNIEDVRLFLDAKHPGHYAVYNLSPRIYRASKFHNRVTECGWAVRRAPHLHSLYTLCRSMHAWLREDHRNVCVVHCMDGRAASAVAVCAFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYVCDMVAEEPITPHSKPMLVKSVVMTPVPLFSKQRNGCRPFCEVYVGEERVTTTSQEYDRMKEFKIEDGKAVIPLGITVQGDVLTIIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSRDVPPWENTSLRGLNPKILFSNREEQQDILSKFGKPELPRQPGSTAQYDAEAGSPEAEITESDSPQSSSTDTNHFLHTLDWQEEKDPETGVDNTSPKESQSNLIADGDGSEVSDEEEASCPSEERKPGAGEDTPRLAAGTRQQDLIFDVGMLAAPQEPVQPEEGVDLLGLHSEGDLRPAAPLQASGVQSSNTDLLSSLLEPSDASQVGPPGDLLGGETPLLLASPVSLLGVQSNLQGKVPDTVDPFDQFLLPSSSDTQPCSKPDLFGEFLNSDSVASSTAFPSTHSAPPPSCSTAFLHLGDLPAEPNKVIASSSHPDLLGGWDTWAETALPGPASMPVPEGTLFSSAGHPAPPGPNPSQTKSQNPDPFADLSDLSSSLQGLPAGLPAGSFVGTSATTHKSNSSWQTTRPTAPGTSWPPQAKPAPRASEQLRSHFSVIGAREERGVRAPSFAQKPKVSENDFEDLLPNQGFSKSDKKGPKTMAEMRKQELARDTDPFKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVSMADLVTPEQVKKQYRRAVLVVHPDKATGQPYEQSAKMIFMELNDAWSEFENQGSRPLF
Protein: Zinc finger and BTB domain-containing protein 46 (BTB-ZF protein expressed in effector lymphocytes) (BZEL) (BTB/POZ domain-containing protein 4) (Q8BID6)
Organism: Mus musculus (Mouse)
Function: Functions as a transcriptional repressor for PRDM1.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Chemokine XC receptor 1
- Basic leucine zipper transcriptional factor ATF-like 3
Sequence:
MNNRKEDMEITSHYRHLLRELNEQRQHGVLCDACVVVEGKVFKAHKNVLLGSSRYFKTLYCQVQKTSDQATVTHLDIVTAQGFKAIIDFMYSAHLALTSRNVIEVMSAASFLQMTDIVQACHDFIKAALDISIKSDASDELSEFEIGTPASNSTEALISAVMAGRSISPWLARRTSPANSSGDSAIASCHEGGSSYGKEDQEPKADGPDDVSSQSLWPGDVGYGSLRIKEEQISPSHYGGSELPSSKDTAIQNSLSEQGSGDGWQPTGRRKNRKNKETVRHITQQVEEDSQAGSPVPSFLPTSGWPFSSRDSNVDLTVTEASSLDSRGERAELYAHIDEGLLGGETSYLGPPLTPEKEEALHQATAVANLRAALMSKNSLLSLKADVLGDDGSLLFEYLPKGAHSLSLNEFTVIRKKFKCPYCSFSAMHQCILKRHMRSHTGERPYPCEICGKKFTRREHMKRHTLVHSKDKKYVCKVCSRVFMSAASVGIKHGSRRHGVCADCAGRGVGTPLDHGGGGEGSPEALFAGEGPYLEDPDDPRGEAEEELVEDEDEDVAKWKDDVGLAHEDALLGDDKDDEDSPQGPHSPSGEPDKDFAWIS
Protein: B-box type zinc finger protein with CCT domain-containing protein (F4I1N0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00357}.
Interaction partners:
Sequence:
MTSHQNIKISEKIMISKYQEDVKQPRACELCLNKHAVWYCASDDAFLCHVCDESVHSANHVATKHERVCLRTNEISNDVRGGTTLTSVWHSGFRRKARTPRSRYEKKPQQKIDDERRREDPRVPEIGGEVMFFIPEANDDDMTSLVPEFEGFTEMGFFLSNHNGTEETTKQFNFEEEADTMEDLYYNGEEEDKTDGAEACPGQYLMSCKKDYDNVITVSEKTEEIEDCYENNARHRLNYENVIAAWDKQESPRDVKNNTSSFQLVPPGIEEKRVRSEREARVWRYRDKRKNRLFEKKIRYEVRKVNADKRPRMKGRFVRRSLAIDS
Protein: Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (P13384)
Organism: Bos taurus (Bovine)
Function: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P18065}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin
- Cation-independent mannose-6-phosphate receptor
Sequence:
MQPRLGGPALLLLPPLLLLLLLGAGGGDCGARAEVLFRCPPCTPESLAACKPPPGAAAGPAGDARVPCELVREPGCGCCSVCARLEGERCGVYTPRCGQGLRCYPNPGSELPLRALVHGEGTCEKHGDAEYSASPEQVADNGEEHSEGGLVENHVDGNVNLMGGGGGAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQGARGVHTQRMQ
Protein: Alcohol dehydrogenase 5 (EC 1.1.1.1) (Alcohol dehydrogenase V) (P38113)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Alcohol dehydrogenase 4
- S-
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase 2
- Alcohol dehydrogenase 3, mitochondrial
- Fatty aldehyde dehydrogenase HFD1
- Pyruvate decarboxylase isozyme 2
- Aldehyde dehydrogenase [NAD
- Pyruvate decarboxylase isozyme 3
- Pyruvate decarboxylase isozyme 1
Sequence:
MPSQVIPEKQKAIVFYETDGKLEYKDVTVPEPKPNEILVHVKYSGVCHSDLHAWHGDWPFQLKFPLIGGHEGAGVVVKLGSNVKGWKVGDFAGIKWLNGTCMSCEYCEVGNESQCPYLDGTGFTHDGTFQEYATADAVQAAHIPPNVNLAEVAPILCAGITVYKALKRANVIPGQWVTISGACGGLGSLAIQYALAMGYRVIGIDGGNAKRKLFEQLGGEIFIDFTEEKDIVGAIIKATNGGSHGVINVSVSEAAIEASTRYCRPNGTVVLVGMPAHAYCNSDVFNQVVKSISIVGSCVGNRADTREALDFFARGLIKSPIHLAGLSDVPEIFAKMEKGEIVGRYVVETSK
Protein: Tyramine/octopamine receptor (Tyr/Oct-Dro) (P22270)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for both octopamine and tyramine, invertebrate neurotransmitters, and neuromodulators. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. The rank order of potency for agonists is tyramine > octopamine > dopamine > epinephrine > norepinephrine > serotonin > histamine. For antagonists, the rank order is yohimbine > chlorpromazine > phentolamine > mianserine > cyproheptadine > dihydroergotamine > clonidine > synephrine. Tyramine has a functional role in the olfactory system as a neurotransmitter or a neuromodulator.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Alpha2-adrenergic-like octopamine receptor, isoform B
Sequence:
MPSADQILFVNVTTTVAAAALTAAAAVSTTKSGSGNAARGYTDSDDDAGMGTEAVANISGSLVEGLTTVTAALSTAQADKDSAGECEGAVEELHASILGLQLAVPEWEALLTALVLSVIIVLTIIGNILVILSVFTYKPLRIVQNFFIVSLAVADLTVALLVLPFNVAYSILGRWEFGIHLCKLWLTCDVLCCTSSILNLCAIALDRYWAITDPINYAQKRTVGRVLLLISGVWLLSLLISSPPLIGWNDWPDEFTSATPCELTSQRGYVIYSSLGSFFIPLAIMTIVYIEIFVATRRRLRERARANKLNTIALKSTELEPMANSSPVAASNSGSKSRLLASWLCCGRDRAQFATPMIQNDQESISSETHQPQDSSKAGPHGNSDPQQQHVVVLVKKSRRAKTKDSIKHGKTRGGRKSQSSSTCEPHGEQQLLPAGGDGGSCQPGGGHSGGGKSDAEISTESGSDPKGCIQVCVTQADEQTSLKLTPPQSSTGVAAVSVTPLQKKTSGVNQFIEEKQKISLSKERRAARTLGIIMGVFVICWLPFFLMYVILPFCQTCCPTNKFKNFITWLGYINSGLNPVIYTIFNLDYRRAFKRLLGLN
Protein: Oncomodulin-1 (OM) (Parvalbumin beta) (P0CE72)
Organism: Homo sapiens (Human)
Function: Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
Interaction partners:
- Prestin
- Membrane-associated phosphatidylinositol transfer protein 1
- Zinc finger protein Gfi-1
Sequence:
MSITDVLSADDIAAALQECRDPDTFEPQKFFQTSGLSKMSANQVKDVFRFIDNDQSGYLDEEELKFFLQKFESGARELTESETKSLMAAADNDGDGKIGAEEFQEMVHS
Protein: AT26658p (Q8T3X6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTAAGPAAVRVADPVAAPAADPAAAPAAVLAAPPVAPLAARRAASVAHPAACRVAHPAAPPAALPVAPLAAVRAAVRAAAPAALLAEGQSASDPRQRIRIRFRRQELGANATTSSSSSLESRWSPPAITS
Protein: Transcription initiation factor TFIID subunit 5 (Transcription initiation factor TFIID 100 kDa subunit) (TAF(II)100) (TAFII-100) (TAFII100) (Q15542)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TAF5 is involved in two modules of TFIID, in TFIID-A together with TAF3 and TBP, and in TFIID-B with TAF8. Involved in contacts between TFIID and TFIIF in the PIC.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 11
- TATA-box-binding protein
Sequence:
MAALAEEQTEVAVKLEPEGPPTLLPPQAGDGAGEGSGGTTNNGPNGGGGNVAASSSTGGDGGTPKPTVAVSAAAPAGAAPVPAAAPDAGAPHDRQTLLAVLQFLRQSKLREAEEALRREAGLLEEAVAGSGAPGEVDSAGAEVTSALLSRVTASAPGPAAPDPPGTGASGATVVSGSASGPAAPGKVGSVAVEDQPDVSAVLSAYNQQGDPTMYEEYYSGLKHFIECSLDCHRAELSQLFYPLFVHMYLELVYNQHENEAKSFFEKFHGDQECYYQDDLRVLSSLTKKEHMKGNETMLDFRTSKFVLRISRDSYQLLKRHLQEKQNNQIWNIVQEHLYIDIFDGMPRSKQQIDAMVGSLAGEAKREANKSKVFFGLLKEPEIEVPLDDEDEEGENEEGKPKKKKPKKDSIGSKSKKQDPNAPPQNRIPLPELKDSDKLDKIMNMKETTKRVRLGPDCLPSICFYTFLNAYQGLTAVDVTDDSSLIAGGFADSTVRVWSVTPKKLRSVKQASDLSLIDKESDDVLERIMDEKTASELKILYGHSGPVYGASFSPDRNYLLSSSEDGTVRLWSLQTFTCLVGYKGHNYPVWDTQFSPYGYYFVSGGHDRVARLWATDHYQPLRIFAGHLADVNCTRFHPNSNYVATGSADRTVRLWDVLNGNCVRIFTGHKGPIHSLTFSPNGRFLATGATDGRVLLWDIGHGLMVGELKGHTDTVCSLRFSRDGEILASGSMDNTVRLWDAIKAFEDLETDDFTTATGHINLPENSQELLLGTYMTKSTPVVHLHFTRRNLVLAAGAYSPQ
Protein: Glycosylating toxin TcdB (Toxin B) (M4NKV9)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004501}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004501}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004501}. Host cytoplasm, host cytosol {ECO:0000256|ARBA:ARBA00023586}. Host endosome membrane {ECO:0000256|ARBA:ARBA00023585}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSLVNRKQLEKMANVRFRVQEDEYVAILDALEEYHNMSENTVVEKYLKLKDINSLTDTYIDTYKKSGRNKALKKFKEYLVIEILELKNSNLTPVEKNLHFIWIGGQINDTAINYINQWKDVNSDYNVNVFYDSNAFLINTLKKTIIESASNDTLESFRENLNDPEFNHTAFFRKRMQIIYDKQQNFINYYKAQKEENPDLIIDDIVKTYLSNEYSKDIDELNAYIEESLNKVTENSGNDVRNFEEFKTGEVFNLYEQELVERWNLAGASDILRVAILKNIGGVYLDVDMLPGIHPDLFKDINKPDSVKTAVDWEEMQLEAIMKHKEYIPEYTSKHFDTLDEEVQSSFESVLASKSDKSEIFLPLGDIEVSPLEVKIAFAKGSIINQALISAKDSYCSDLLIKQIQNRYKILNDTLGPIISQGNDFNTTMNNFGESLGAIANEENISFIAKIGSYLRVGFYPEANTTITLSGPTIYAGAYKDLLTFKEMSIDTSILSSELRNFEFPKVNISQATEQEKNSLWQFNEERAKIQFEEYKKNYFEGALGEDDNLDFSQNTVTDKEYLLEKISSSTKSSERGYVHYIVQLQGDKISYEAACNLFAKNPYDSILFQKNIEDSEVAYYYNPTDSEIQEIDKYRIPDRISDRPKIKLTFIGHGKAEFNTDIFAGLDVDSLSSEIETAIGLAKEDISPKSIEINLLGCNMFSYSVNVEETYPGKLLLRVKDKVSELMPSMSQDSIIVSANQYEVRINSEGRRELLDHSGEWINKEESIIKDISSKEYISFNPKENKIIVKSKNLPELSTLLQEIRNNSNSSDIELEEKVMLAECEINVISNIETQVVEERIEEAKSLTSDSINYIKNEFKLIESISDALCDLKQQNELEDSHFISFEDISETDEGFSIRFINKETGESIFVETEKTIFSEYANHITEEISKIKGTIFDTVNGKLVKKVNLDTTHEVNTLNAAFFIQSLIEYNSSKESLSNLSVAMKVQVYAQLFSTGLNTITDAAKVVELVSTALDETIDLLPTLSEGLPIIATIIDGVSLGAAIKELSETSDPLLRQEIEAKIGIMAVNLTTATTAIITSSLGIASGFSILLVPLAGISAGIPSLVNNELVLRDKATKVVDYFKHVSLVETEGVFTLLDDKVMMPQDDLVISEIDFNNNSIVLGKCEIWRMEGGSGHTVTDDIDHFFSAPSITYREPHLSIYDVLEVQKEELDLSKDLMVLPNAPNRVFAWETGWTPGLRSLENDGTKLLDRIRDNYEGEFYWRYFAFIADALITTLKPRYEDTNIRINLDSNTRSFIVPIITTEYIREKLSYSFYGSGGTYALSLSQYNMGINIELSESDVWIIDVDNVVRDVTIESDKIKKGDLIEGILSTLSIEENKIILNSHEINFSGEVNGSNGFVSLTFSILEGINAIIEVDLLSKSYKLLISGELKILMLNSNHIQQKIDYIGFNSELQKNIPYSFVDSEGKENGFINGSTKEGLFVSELPDVVLISKVYMDDSKPSFGYYSNNLKDVKVITKDNVNILTGYYLKDDIKISLSLTLQDEKTIKLNSVHLDESGVAEILKFMNRKGSTNTSDSLMSFLESMNIKSIFVNFLQSNIKFILDANFIISGTTSIGQFEFICDENNNIQPYFIKFNTLETNYTLYVGNRQNMIVEPNYDLDDSGDISSTVINFSQKYLYGIDSCVNKVVISPNIYTDEINITPVYETNNTYPEVIVLDANYINEKINVNINDLSIRYVWSNDGNDFILMSTSEENKVSQVKIRFVNVFKDKTLANKLSFNFSDKQDVPVSEIILSFTPSYYEDGLIGYDLGLVSLYNEKFYINNFGMMVSGLIYINDSLYYFKPPVNNLITGFVTVGDDKYYFNPINGGAASIGETIIDDKNYYFNQSGVLQTGVFSTEDGFKYFAPANTLDENLEGEAIDFTGKLIIDENIYYFEDNYRGAVEWKELDGEMHYFSPETGKAFKGLNQIGDDKYYFNSDGVMQKGFVSINDNKHYFDDSGVMKVGYTEIDGKHFYFAENGEMQIGVFNTEDGFKYFAHHNEDLGNEEGEEISYSGILNFNNKIYYFDDSFTAVVGWKDLEDGSKYYFDEDTAEAYIGLSLINDGQYYFNDDGIMQVGFVTINDKVFYFSDSGIIESGVQNIDDNYFYIDDNGIVQIGVFDTSDGYKYFAPANTVNDNIYGQAVEYSGLVRVGEDVYYFGETYTIETGWIYDMENESDKYYFDPETKKACKGINLIDDIKYYFDEKGIMRTGLISFENNNYYFNENGEMQFGYINIEDKMFYFGEDGVMQIGVFNTPDGFKYFAHQNTLDENFEGESINYTGWLDLDEKRYYFTDEYIAATGSVIIDGEEYYFDPDTAQLVISE
Protein: S-M checkpoint control protein rad4 (P74) (Protein cut5) (P32372)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential component for DNA replication and also the checkpoint control system which couples S and M phases. May directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Interacts simultaneously with both 'Thr-187' phosphorylation sites in a crb2 dimer for establishing the DNA checkpoint.
Subcellular location: Nucleus.
Interaction partners:
- Cell division control protein 45 homolog
- DNA replication regulator sld3
- DNA repair protein crb2
- DNA repair protein rad9
- DNA replication licensing factor mcm5
- Protein kinase rad3
- DNA replication licensing factor mcm3
- DNA damage response protein Mdb1
- DNA replication complex GINS protein psf2
- DNA replication regulator sld2
Sequence:
MGSSKPLKGFVICCTSIDLKQRTEISTKATKLGAAYRSDFTKDVTHLIAGDFDTPKYKFAAKSRPDIKIMSSEWIPVLYESWVQGEDLDDGLLVDKHFLPTLFKCRVCLTNIGQPERSRIENYVLKHGGTFCPDLTRDVTHLIAGTSSGRKYEYALKWKINVVCVEWLWQSIQRNAVLEPQYFQLDMPAEKIGLGAYVRLDPNTTEAKSYSENQKISKNKEKSGQSLAALAEEADLEPVIMKRGKKRDRSILWEELNNGKFEFSSRSEENSVLLDDFTPETVQPLEENELDTELNIENEAKLFKNLTFYLYEFPNTKVSRLHKCLSDNGGQISEFLSSTIDFVVIPHYFPVDELPIFSFPTVNEWWIERCLYYKKIFGIDEHALAKPFFRPSLVPYFNGLSIHLTGFKGEELSHLKKALTILGAVVHEFLGVQRSILLVNTNEPFSMKTRFKIQHATEWNVRVVGVAWLWNIIQSGKFIDQVSPWAIDKKENQEIKKFTNQNNMVFPTSDRDTRLQNSLAQQPIGHSTPHNSPSLLSVKKRQNNHIRSNTLIQLNSNSKDSTIFPRRSVTVPGDKIDTVWKSSVTKPETPTSPQEHVSYIDPDAQREKHKLYAQLTSNVDAIPPANDLQNQENGLLLITESHRKLRRR
Protein: Glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) (NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase) (NAD(P)H-dependent dihydroxyacetone-phosphate reductase) (P46919)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the biosynthesis of the sn-glycerol 3-phosphate required for phospholipid synthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394, ECO:0000269|PubMed:15743965}.
Interaction partners:
- GTPase Der
- Glycerol-3-phosphate cytidylyltransferase
- Glycerol-3-phosphate acyltransferase
- Aerobic glycerol-3-phosphate dehydrogenase
- Glycerol-1-phosphate dehydrogenase [NAD
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Diacylglycerol kinase
- Phosphatidate cytidylyltransferase
- Serine acetyltransferase
- 3'-5' exonuclease DinG
Sequence:
MKKVTMLGAGSWGTALALVLTDNGNEVCVWAHRADLIHQINELHENKDYLPNVKLSTSIKGTTDMKEAVSDADVIIVAVPTKAIREVLRQAVPFITKKAVFVHVSKGIEPDSLLRISEIMEIELPSDVRKDIVVLSGPSHAEEVGLRHPTTVTASSKSMRAAEEVQDLFINHNFRVYTNPDIIGVEIGGALKNIIALAAGITDGLGYGDNAKAALITRGLAEIARLGTKMGGNPLTFSGLTGVGDLIVTCTSVHSRNWRAGNLLGKGYKLEDVLEEMGMVVEGVRTTKAAYQLSKKYDVKMPITEALHQVLFNGQKVETAVESLMARGKTHEMEDLVNTFENQVK
Protein: Nrg2p (A0A1D8PP98)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
AWLLKKKSDVFCHLFFAIFFFSSAFFSPSFFVDVSXAHRSPTGLPPAPRFSQLHNQSPPKQSNNLPTKLHNRVATLIVXSTCLAVSKFNFCHLKLKNRLPLLLSVNSILSLLL
Protein: Pre-mRNA-splicing factor SYF1 (P91175)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein T27F2.1
- TPR_REGION domain-containing protein
- Pre-mRNA-splicing factor syf-2
- Protein BUD31 homolog
- Protein isy-1
- Intron-binding protein aquarius
- Peptidyl-prolyl cis-trans isomerase E
- PSP proline-rich domain-containing protein
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor RBM22
Sequence:
MADKENATKIEKMPNSETMKGISSEDVPFEEDIIRNPTSVNCWQRYIDHKLQNKSPAKQMFLIYERALAVFERSYKLWYHYLKYRESTIVNKCPTDNSWRALCDTYERCLMRLHKMPRIWICYCEVMIKRGLITETRRVFDRALRSLPVTQHMRIWTLYIGFLTSHDLPETTIRVYRRYLKMNPKAREDYVEYLIERDQIDEAAKELTTLVNQDQNVSEKGRTAHQLWTQLCDLISKNPVKIFSLNVDAIIRQGIYRYTDQVGFLWCSLADYYIRSAEFERARDVYEEAIAKVSTVRDFAQVYDAYAAFEEREVSIMMQEVEQSGDPEEEVDLEWMFQRYQHLMERKNELMNSVLLRQNPHNVGEWLNRVNIYEGNYNKQIETFKEAVKSVNPKIQVGKVRDLWIGLAKLYEDNGDLDAARKTFETAVISQFGGVSELANVWCAYAEMEMKHKRAKAALTVMQRACVVPKPGDYENMQSVQARVHRSPILWAMYADYEECCGTVESCRKVYDKMIELRVASPQMIMNYAMFLEENEYFELAFQAYEKGIALFKWPGVFDIWNTYLVKFIKRYGGKKLERARDLFEQCLENCPPTHAKYIFLLYAKLEEEHGLARHALSIYNRACSGVDRADMHSMYNIYIKKVQEMYGIAQCRPIFERAISELPEDKSRAMSLRYAQLETTVGEIDRARAIYAHAAEISDPKVHVKFWDTWKNFEVAHGNEATVRDMLRVRRSVEASYNVNVTLTSVQMRVDAERKAQETTTSSNPMDSLDQQQQQPSDGAGSITQVSMNKGNISFVRGAGKTVQQNTTENPDEIDLDEDDDDEEDDGGDADISVKVVPAQIFGNLKLAEEEEEA
Protein: Probable sigma-70 factor, ECF subfamily (Q9I222)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transmembrane sensor
- Sigma factor regulator, FemR
- Ferric-mycobactin receptor, FemA
- Luciferase-like domain-containing protein
- Secretin/TonB short N-terminal domain-containing protein
- Major facilitator superfamily
- Probable major facilitator superfamily
- Probable sigma-70 factor, ECF subfamily
- Probable transmembrane sensor
- Probable transmembrane sensor
Sequence:
MDSQGSIKNTLIAQLFQQNYDWLCKKLSYQTGCSHSAEDLAAEAFLQVWMLPDPASIRSPRAFLATIAQRLMYESWRRKDLERAYLQILAEAPEAVQPSPHEQWMLIESLQAIDRLLDGLSGQARAVFLMSQLEGLTYVQIGERLGLSLGRIHQLMKDALHCCYRGFQE
Protein: Deubiquitinase and deneddylase Dub1 (ChlaDub1) (EC 3.4.22.-) (O84876)
Organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease possesses deubiquitinating and deneddylating activities.
Subcellular location: Secreted {ECO:0000250}. Host cell {ECO:0000250}. Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Secreted, and delivered into the host cell. {ECO:0000250}.
Interaction partners:
- Tail-Specific Protease
Sequence:
MLSPTNSTSKKAPVPPQDSSKPVLISEEPQNQLLQKVARTALAVLLVVVTLGLILLFYSFSDLQSFPWCCQTRPSTKEQPTISIPVPLPSPPLAVPRPSTPPPPVISRPSTPPAPTPAISPPSTPSAPKPSTPPPLPPKAPKPVKTQEDLLPFVPEQVFVEMYEDMARRWIIEALVPAWDSDIIFKCLCYFHTLYQGLIPLETFPPATIFNFKQKIISILEDKKAVLRGEPIKGSLPICCSEENYRRHLHGTTLLPVFMWYHPTPKTLSDTMQTMKQLAIKGSVGASHWLLVIVDIQARRLVYFDSLYNYVMSPEDMEKDLQSFAQQLDQVYPAYDSQKFSVKIAAKEVIQKGSGSSCGAWCCQFLHWYLRDPFTDALNDLPVDSVERHENLASFVQACEAAVQDLPELFWPEAKALF
Protein: Aquaporin PIP2-7 (Plasma membrane intrinsic protein 2-7) (ZmPIP2-7) (ZmPIP2;7) (Q9ATM4)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAKDVEQVTEQGEYSAKDYHDPPPAPLIDPDELTKWSLYRAAIAEFIATLLFLYITVLTIIGYKRQSDTKIPGNTECDGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLGRKVSLVRALLYMIAQCAGAICGAGLAKGFQKSFYNRYGGGVNTVSDGYNKGTALGAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPVTGTGINPARSFGPAVIFNNDKAWDDQWIYWVGPFVGAAVAAIYHQYILRGSAIKALGSFRSNA
Protein: Protein MNE1 (P24720)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Intron-encoded DNA endonuclease aI5 beta
- Protein PET54
Sequence:
MKLLFKRYSSSHIGKLIKDSLITPEILPQLGRQPSSHKRLPNNKRTNSITDKWLKDALTRKDKLNEDKLQNVNLRLNVVLTTLQKLRTSDNPALYFALLNRIGTGHIKWLNKSGRQIDAFPPDRLPLEFYHELSNMLYKLSLRSANDKIALAKFSLQLLDRYYFLKTKSLTIEGKFRANIKFLRNCTLLIVKSQSNYYLRAIQRLFAENSEGQLLANLSQLAFYVETSQWTSMLDILSSCVPDSGLRGSKERERAIQLLELFSPCLVKSLKVMIAQNMENEACQILRSLSEWNFHFDQHDSSNLIQLSQNHSCLKVIETMNGLSSTTAVTRQFGLEKLPTDVSLKQSIHILSKDNFEPLKQDSFLQFLSFKLSDLPLNLEVWKKHIKEVDDQMQAESNLHSLRAFFIDMLLCHLSVRKDFDFMLSLVEHIVYEKNLWQPLLLTDNIVGNKENSTFHCLFHGASQDISTKLTLLALYNQLNEIGYQFTSHDFLSMLKVCKNYSDSDFFYFAFYNLLVTQSHKFFLFDKFSDKFSWRLPIQIGDAISEWLSSLEIDIQENTDRVLQITDDVGEWYVENKPFKSEKGTIQPINIMELRKIFGERKTLFHMDSEIFQKSKAKRDKEMRNEALFTANDAEYNFAADVSYAKRVENLFSYIRSKQMQQK
Protein: Large ribosomal subunit protein eL27y (60S ribosomal protein L27-2) (Q8LCL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL22y
Sequence:
MVKFLKQNKAVILLQGRYAGKKAVIIKSFDDGTSDRRYGHCLVAGLKKYPSKVIRKDSAKKTAKKSRVKCFIKLVNYQHLMPTRYTLDVDLKEVATLDALKSKDKKVTALKEAKAKLEERFKTGKNRWFFTKLRF
Protein: Small forked protein (Q24340)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMLGSVKMHKNSRRNYFTLSFHRFDIFRSNKKAKLLNAGSTNGSSIAASSDDSQSRYGGSVHAANGSAANGHFYGYSEGNKNQGSNGNGNGNGNGGGGNYHSHPNQPHYATGQPHQYTPSLYGGGSSAEDHYELTQQQQQIYGETHLPSGQRTGGPNLVNKQLVLPFVPPSFPNKSQDGVTHLIKPSEYLKSISIDKVRAHPPPAPRIRRTTCRYRSPSSRHPHQHQHHPHPHPHPHHPHQLHGMGEQPPLPPPPPPLPHGMLPPQPPMGPPMGVAGGQDATMSGKSHKPKKPHGSAPNSQDTATRKQHQPLSAISIQDLNSQLRRTDTQKVPKPYQMPARSLSMQCLTSSTETYLKSDLIAELKISKDIPGIKKMKVEQQMASRMDSEHYMEITKQFSGNNYVDQIYLQIPERDQAGNAIPDWKRQMMAKKAAERAKKDFEERMAQEAESRRLSQIPQWKRDLLARREETENKLKAAIYTPKVEENNRVADTWRLKNRAMSIDNININLAGMEQHYQQIQFQQKQQQLQLGNKENHVDPKGADQDQEHGVGIGSALVTLTLASLEVRSSSTHRRAARAAPRRRRITSSPGAPSCARPTAVSA
Protein: Adenosine transporter, putative (Q38EK0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Heat shock 70 kDa protein, putative
Sequence:
MLGFESFSEFVVYVTFIFFGMSVMMVTNAIYSIPAFFTEYYKYAQGSSDAQTENENFWNNILTYYNAAVFSAQVLLETFMLTNVGRRIPIRIRLIFGLTIPLVELIALILITVCHTSEAGAKATIIIIALVGGVSKTLCDSSNAALVGPFPTRFYGAIVWGLGVSGLITSLMSIIIKASMDDSFESMLTQSRIYFGIVIFIQVIACVLLALLTKNPYAIKYAAEFRHAAAKESAVESNEPVQETITDQEANAGEEGERVEKSTSKMNVLNVSEDPDKMKDTDQVDGTTNAQQMLDANLWFVVKRIWPMLVSCFFVFFATLLVFPGVFFAVEVKDGWYITLTAAMFNFGDFLSRLVLQFKQLRPSPIVVLIGTFARLLIIPLLVLCVRGIIPGSALPYILCLLWGLTNGYFGGMSMIYAPRTGSLTTAGQRSLAAICGNLALLLGLFAGSMLALAVMTALPES