wanglab/gogpt-training-data huggingface dataset:
Protein: Histone deacetylase family protein (Q72A58)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Chaperone protein HtpG
- Hydantoinase/oxoprolinase family protein
- Snf2 family protein
- Lipoprotein, putative
- DUF3298 domain-containing protein
Sequence:
MLEAKNRLGVIFFPAFDWAISPTHPEREERLLYTQDQLREEGLFDIAGITEHKPDVATREDVERVHFCLPDVSSVCTKSHLVSAGGAIKAARLVMEKRADKAFALIRPPGHHAMRVVHGNRGFCNINIEAVMLEHIREQYGRLRVAIVDTDCHHGDGTQDIYWHDRDTLFISLHQDGRTLYPGTGFPQELGGPNAMGRTINIPLPPGTSDRGFLHVIEHVVRPILDDFKPDLIINSAGQDNHFSDPITNMNFTARGYAMLNRMLDPDIAVLEGGYAIQGALPYVNLGICLAMAGLDFDDVREPGLDLAAIEQPRNVTDYIERLCDELPRLYFEPPARPKQGDVVGDTFVRTRDVYYDTDGISESQVETVTLCEHCSGAMKVETWSTVNPLSVGIHIPQDACDACHAAGLRMEDEAKTRGNYRYIQCIDRRGKRYTQHGF
Protein: Large ribosomal subunit protein eL32 (60S ribosomal protein L32) (P62910)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL36
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL8
- Small ribosomal subunit protein eS10
Sequence:
MAALRPLVKPKIVKKRTKKFIRHQSDRYVKIKRNWRKPRGIDNRVRRRFKGQILMPNIGYGSNKKTKHMLPSGFRKFLVHNVKELEVLLMCNKSYCAEIAHNVSSKNRKAIVERAAQLAIRVTNPNARLRSEENE
Protein: Fe(3+) dicitrate transport system permease protein FecD (Iron(III) dicitrate transport system permease protein FecD) (P15029)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2651410}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fe
- Fe
- Fe
- Fe
- Ferric enterobactin transport ATP-binding protein FepC
- Iron
- Vitamin B12-binding protein
- Iron
- Ferric citrate uptake sigma factor regulator FecR
- Ferric citrate uptake sigma factor FecI
Sequence:
MKIALVIFITLALAGCALLSLHMGVIPVPWRALLTDWQAGHEHYYVLMEYRLPRLLLALFVGAALAVAGVLIQGIVRNPLASPDILGVNHAASLASVGALLLMPSLPVMVLPLLAFAGGMAGLILLKMLAKTHQPMKLALTGVALSACWASLTDYLMLSRPQDVNNALLWLTGSLWGRDWSFVKIAIPLMILFLPLSLSFCRDLDLLALGDARATTLGVSVPHTRFWALLLAVAMTSTGVAACGPISFIGLVVPHMMRSITGGRHRRLLPVSALTGALLLVVADLLARIIHPPLELPVGVLTAIIGAPWFVWLLVRMR
Protein: TFIIA-alpha and beta-like factor (General transcription factor II A, 1-like factor) (Q8R4I4)
Organism: Mus musculus (Mouse)
Function: May function as a testis specific transcription factor. Binds DNA in conjunction with GTF2A2 and TBP (the TATA-binding protein) and together with GTF2A2, allows mRNA transcription.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor IIA subunit 2
- TATA box-binding protein-like 1
- Transcription initiation factor IIA subunit 1
- TATA-box-binding protein
- Stonin-1
- Transcription initiation factor IIB
- TATA box-binding protein-like 2
- General transcription factor IIE subunit 1
- General transcription factor IIF subunit 2
Sequence:
MAFINLVPKLYQSVIEDVIEGVRDLFAEEGIEEQVLKDLKKLWETKVLQSKATEDFFRNSTQVPLLTLQLPHALPPALQPEASLLIPAGRTLPSFTPEDLNTANCGANFAFAGYPIHVPAGMAFQTASGHLYKVNVPVMVTQTSGRTEILQHPFQQVLQQLGQPLVIQTTVPTLHPCSLQAATEKSLRMEAVLQPPPILHPPPVDRTHVENAASDRRLLPGNELRPQESSPYLSLPGVGFPPQAALTESSLEPVLGVSASLTQNLHSDPFSQGPPGPLHHHLLESQLQSLKDSIYGCDSTKQLRKAEEPSSLRVSEKNCTSERDLNIRVTDDDINEIIQIDGTGDNSSTEEMGSIRDADENEFPGIIDAGDLNVLEEVDSVSNEDSTANSSDNEDHQINAPEEDPLNSGDDVSEQDVPDLFDTENVIVCQYDKIHRSKNRWKFYLKDGVMCFGGRDYVFAKAIGEAEW
Protein: Sodium/potassium-transporting ATPase subunit beta-3 (Sodium/potassium-dependent ATPase subunit beta-3) (ATPB-3) (CD antigen CD298) (P97370)
Organism: Mus musculus (Mouse)
Function: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q63377}; Single-pass type II membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:P54709}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:P54709}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-2
- Phospholemman
- Protein ATP1B4
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MTKTEKKSFHQSLAEWKLFIYNPSSGEFLGRTSKSWGLILLFYLVFYGFLAALFTFTMWAMLQTLNDEVPKYRDQIPSPGLMVFPKPQTALEYTFSMSEPQTYKKLVEDLESFLKPYSVEEQKNLTSCPDGAPFIQHGPDYRACQFPVSLLEECSGVTDANFGYSKGQPCILVKMNRIIDLIPDGYPQISCLPKEENATIATYPEFGVLDLKYFPYYGKKRHVGYRQPLVAVQVKFDSGLNKKEVTVECHIAGTRNLKNKNERDKFLGRVSFKVTARA
Protein: Nexilin (Q9Z2J4)
Organism: Rattus norvegicus (Rat)
Function: Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9832551}. Cell junction, adherens junction {ECO:0000269|PubMed:9832551}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:19881492}. Note=Localizes to the cell-matrix AJ (PubMed:9832551). Not found at the cell-cell AJ (PubMed:9832551).
Interaction partners:
- Protein MAK16 homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- GTP-binding protein 4
- Ribosome production factor 1
- RRP15-like protein
- Ribosome biogenesis protein BRX1 homolog
- EBNA1 binding protein 2
- Probable ribosome biogenesis protein RLP24
- P2Y purinoceptor 1
- Peter pan homolog
Sequence:
MNDVSQKAEILLSSSKPVPKSYVPKLGKGDVKDKFEAMQRAREERNQRRSRDEKQRRKEQYIREREWNRRKQEIKDMLASDEEEEPSKVEKAYVPKLTGTVKGKFDEMEKHRQEEQRKRTEEERKRRIEQDLLEKRKMQRELAKRAEQEGDDSLLITVVPAKSYRAAANRKDPEDLDREHRNGRVSQEEEKTRHEEECRALKEAKCLSLVMDDETEAKKESRFPGKLKSTFEELERQRQENRKKQAEEEARRRLEEERRAFEEARRNMVNEEDESQDTETVFKEYRPGKLRLSFEEIERQRREEEKRKAEEEARRRMEEEKKAFAEARRSMVLDDDSPEIYKAVSQESLTPGKLEINFEQLLRQKMEEERRRTEEERRQKLEMEKQEFEQLRQEMGKEEEENESFGLSREYEELIKLKRSGSIQAKNLKSKFEKIGQLSEKEVQKKIEEERAKRRAIDLEIKEREAENFHEDDDVDVKPAKKSESPFTHKVNMKARFEQMAKARQEEEQRRIEEQKLLRMQFEQKEIDAALQKKREDDEEEEGSIVNGSTTEDEEQTRSGAPWFKKPLRNTSVVDSEPVRFTVKVTGEPKPEVTWWFEGELLQDGEDYQYIERGETYCLYLPETFPEDGGEYMCKAVNSKGSAASTCILTIEMDDY
Protein: Mediator of RNA polymerase II transcription subunit 20 (Mediator complex subunit 20) (Q10317)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 27
Sequence:
MPVHGVIYYSSPSMATFLSPAQDNLVRTYFAQHLKKWVVQYKLYRNAVTPKTLEFLKQNINPSMLACVDEATMIDAEPELEDIIVRTKLWNFRQSFTIEGSIYEVGSFKVAIANVLQKSVWKGILFHVTYDGTESVDLARPIIQEFFLKCFLQNNKSVTPVYESFFNQPRHSLDSKLLLQLFKQRIDTVSQRT
Protein: Transcription termination factor 5, mitochondrial (Mitochondrial transcription termination factor 5) (mTerf5) (Q9VEB4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds promoter DNA and regulates initiation of transcription. Regulates mitochondrial replication and transcription. Required for normal topology and maintenance of mitochondrial DNA (mtDNA) levels. Regulates mtDNA replication by re-activating replication after replication pausing. Likely to regulate replication pausing by coordinating with the mitochondrial termination factor mTTF which promotes replication pausing. Their function in replication pausing prevents unregulated replication that may occur for example by collisions between the machineries of DNA replication and transcription during mtDNA synthesis. This ensures the incorporation of RNA transcripts into replication intermediates at the replication fork and allows for proper fork progression. Possibly functions downstream of Dref which activates genes involved in mtDNA replication and maintenance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22784680}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory complex subunit p50
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 2
Sequence:
MLRNGQNQAQLLARSLGQLARGMASSKRVSSKKEDLKPKLPKPPTVEIPMEEPLNASYLSKTLGSSYRSWAAALEKHPELKTLKRKDLLSSYDTLKSLDYSVDDIIAKPMIIYYGATTLANRHSVLQECGFHNVTVQTLAKYVTVVNKPIEVLKAHNYIPFDVKVAERLAGYFKDIKLPVDLRELESETLTLKSLRQSLINAYLRERLQMDDNDLQKLWRVYTRIRHKSFRAVQDTIELLTKEFNFSAERLRKNSFLLYSEADNVRRILREVPTIDSQDIREIGFRRPKILMSTCDSLKQTLQHVHAFGISEDAVLRCLEVLTLGPDTVLERLRDLQEIEEFQVLGTNPRILRLVHYQNKARLRLDYLNQLRVRCASLHILSCGSEAFAKFARDGSDRTKGRDIVVYLSNVLGKDVQVLRNLLSRHPNWCHIPLLHVKQCLEYLRSKKFKLNEIFANIHLLLYPIKRIEEKMLLLQSPDAQEDLQLPVANFDSLSNNEILTLILYLIESEFHFTGDGIWTEQHTHHVENFNNLLPDFPESLNKVYKYGVKPAEKMIMERL
Protein: At5g57345 (Transmembrane protein) (Q8LAD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g21865
Sequence:
MYFAAIASSRQSFLSNNFSFQHSFKPKSNVNLTRPNSICCKSSHHDDETDSSRKNENQLAKLAIATLAVGVLALGSVGDAFAAKSGGRIGGQAFRSSAPRPPPRINNRSRTNIYVNPQVAPPLIGGYGYGYGGYGWSPFSFFAPGPAVAVGVGGGFDLLLLFMFFGAASAVARNFFRSRNDEDDEDDY
Protein: Polymerase basic protein 2 (RNA-directed RNA polymerase subunit P3) (P03427)
Organism: Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))
Function: Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062}. Host mitochondrion {ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:16242167, ECO:0000269|PubMed:1985200}.
Interaction partners:
Sequence:
MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPVTSTVHYPKIYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTTTKEKKEELQGCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEARNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVNILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKREEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKALFQNWGIESIDNVMGMIGILPDMTPSTEMSMRGVRISKMGVDEYSSAEKIVVSIDRFLRVRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAVRGQYSGFVRTLFQQMRDVLGTFDTAQIIKLLPFAAAPPKQSGMQFSSLTINVRGSGMRILVRGNSPIFNYNKTTKRLTVLGKDAGPLTEDPDEGTAGVESAVLRGFLILGKEDRRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRNSSILTDSQTATKRIRMAIN
Protein: 3-hydroxyisobutyryl-CoA hydrolase (HIB-CoA hydrolase) (HIBYL-CoA-H) (EC 3.1.2.4) (3-hydroxyisobutyryl-coenzyme A hydrolase) (A0A140VJL0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU369070}.
Interaction partners:
Sequence:
MGQREMWRLMSRFNAFKRTNTILHHLRMSKHTDAAEEVLLEKKGCTGVITLNRPKFLNALTLNMIRQIYPQLKKWEQDPETFLIIIKGAGGKAFCAGGDIRVISEAEKAKQKIAPVFFREEYMLNNAVGSCQKPYVALIHGITMGGGVGLSVHGQFRVATEKCLFAMPETAIGLFPDVGGGYFLPRLQGKLGYFLALTGFRLKGRDVYRAGIATHFVDSEKLAMLEEDLLALKSPSKENIASVLENYHTESKIDRDKSFILEEHMDKINSCFSANTVEEIIENLQQDGSSFALEQLKVINKMSPTSLKITLRQLMEGSSKTLQEVLTMEYRLSQACMRGHDFHEGVRAVLIDKDQSPKWKPADLKEVTEEDLNNHFKSLGSSDLKF
Protein: TNFAIP3-interacting protein 3 (A20-binding inhibitor of NF-kappa-B activation 3) (ABIN-3) (Listeria-induced gene protein) (Q96KP6)
Organism: Homo sapiens (Human)
Function: Binds to zinc finger protein TNFAIP3 and inhibits NF-kappa-B activation induced by tumor necrosis factor, Toll-like receptor 4 (TLR4), interleukin-1 and 12-O-tetradecanoylphorbol-13-acetate. Overexpression inhibits NF-kappa-B-dependent gene expression in response to lipopolysaccharide at a level downstream of TRAF6 and upstream of IKBKB. NF-kappa-B inhibition is independent of TNFAIP3 binding.
Interaction partners:
- Tumor necrosis factor alpha-induced protein 3
- TNFAIP3-interacting protein 2
Sequence:
MAHFVQGTSRMIAAESSTEHKECAEPSTRKNLMNSLEQKIRCLEKQRKELLEVNQQWDQQFRSMKELYERKVAELKTKLDAAERFLSTREKDPHQRQRKDDRQREDDRQRDLTRDRLQREEKEKERLNEELHELKEENKLLKGKNTLANKEKEHYECEIKRLNKALQDALNIKCSFSEDCLRKSRVEFCHEEMRTEMEVLKQQVQIYEEDFKKERSDRERLNQEKEELQQINETSQSQLNRLNSQIKACQMEKEKLEKQLKQMYCPPCNCGLVFHLQDPWVPTGPGAVQKQREHPPDYQWYALDQLPPDVQHKANGLSSVKKVHP
Protein: NLE domain-containing protein (Q583H9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- Pescadillo homolog
- RNA-binding protein, putative
- Ribosome biogenesis protein, putative
- Nucleolar protein, putative
- Nucleolar GTP-binding protein 1
- Ribosome assembly factor mrt4
- rRNA processing protein, putative
- CCAAT-binding factor domain-containing protein
- 60S ribosome subunit biogenesis protein NIP7 homolog
Sequence:
MQEEAISSAATGVGHVMVTFFTDSYAKAMPEESYAVPLNVLPEGLNVLVQSVLSVNDQVFDFLYNGEYITTTLQKFLSRRGVSTEELVNVEYTPALQAKESSHLPHDDWVSSVRVPFVGHSELLLTGSYDRCIRLWDADDCVAIGAHHDECVKEVVVHPMKPRSTATNTTRDSVKKRARSSLLEDFYCVSCSKDGRAAAWVFNATASKFQLLSSVKAHTDAIESIDISPGAGKYVATASWDCTVKVFEWSQVVDGATEPSAKEPLVSFTDHTRPALSCRFSAAKGAALLYSSGLDGTLKCMDVETAVLQKQYIGDHPVQGLAVRTVGGGGGGDLIIAACTDNRARLYDTRVGESTGSVKVFSGHKQWLYAASWLWRPDEGEVNGGNFFATASEDSTVRLWDLRCGTNALLTLDTSHTDGVLDVTYSGNGEIVSCGKDNSTKSFQCFKGDSLLN
Protein: No long nerve cord, isoform C (EC 3.4.24.-) (No long nerve cord, isoform E) (Q0E8N3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSVNMNWTSPKIWAALFVTTLCLLDTQAAWAKKLNASQAFDDTWNTASDLENELEQQKRSKVQSAGGGGGAGGGPGQWSSWSDWSTCSRTCDGGIMHQMRRCGSPGSCRGESTRYRICNMQPCPEQQDFRSSQCSAYNDVPYDGTLYKWTPHYDYVEPCALTCRGHPAHLVEDISRETGDGNAEEAEHYDEQSVIVQLSARVQDGTRCRSGSLDMCIQGKCQRVGCDLKIGSTKKIDGCGVCGGDGNSCSQPLFNWEMAPMSQCSVTCGSGYKMSRPICRNRLTNADVDDTLCSVTNRPEASVEQCNTHSCPPRWIADDWSTCSRLCGHGYRERMVVCAEESNGIKTRVADIMCRTPKPPTQETCIIEECPHWEVEDWTGCSVSCGQGIQMRGVECKSTDGSLSAKCDPLTKPGSMQQCSTGIHCGGSLNKVGGTIIVGSSRSLNERSERQLDSSDADEDNEDENDEGDDVDDLESGQDTDDGEGLSYADQPLLYAHRTQSRLNQEAPDEPRTMHLMNGNSNNNFNRGEDESEGPSLDPTYIKDNEWSPCSVTCGEGIRRRTYNCKIFLEYSRTVATVNDSLCEGKKPHDEVERCVEDPCMLPSHGFDDQFPRDSIKVGVSEPGKTYVWREQGYTSCSASCLGGVEELIINCVREDNGRVVSPFLCSPETKPEARVRTCNDRPCPPRWNYSDYTPCSKSCGIGIKTREVQCIHEVTRGGDNTMVVPNSMCPQPPPADRQYCNVLDCPVRWEVGEWSKCSHTCGYGFKDRKVECKQIMAQEHKIERPESMCPSAKPADKKPCNVKPCPPEDPKPVIQINNSTHIQHDPKKTKITLKVGGAGLVFFGTQVKIKCPVKRYNRTKIKWSKDHKPLQRSRKYKVSKKGALRILDITFRDAGVYSCHAGLSSAEISIEVKAKPGQQIEELEQQETERLVREKSGTEALTSADMKSADGTGTSTAVGPNSHVNGSAQQHGSRRRQQQSERLQNGRERSRRPKSDGVQHADSSIMEDDLSQLVQSEDRIPQPASASSGGSRTRTLLAMPYFQALLSNLQLLWPLQRFKDSRGQHLLQGEALKFGIDLSGKDFDQDESERVPAEQLPPEVLHSPSDPEYHEPSKSGPEADVPHVPPHMPHARWETGAAASTTAVPSLPNDGFVYRWMLGEWSQCSQECGAAGSGLQRRTVSCQRAAKATSSGSTSDTENNVVDNSECFAHGLELPEFFQSCGNEACPQWSKGDWTPCQRSHCHGRNTAMQRREVTCRYPNGTEGSICDEYERPAMRQECYNERCEGVWRVEPWSECNAPCGRKGIKYRILQCVWYGSRRPAGNVCKHQPRPAVMKVCKSPACQAQLSSSPAQLCRDSSRYCRNARAMGLCRLHRYKLKCCGSCEQQPNQHLIL
Protein: Early transcribed membrane protein 14.2 (Q8IK77)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Antigen 332, DBL-like protein
Sequence:
MKLIKVYVFLFIMLMIGLLGCGNVCNELKEKKNMLLKENPDKLLNKKRRKKLVYSVIGTLSAILGIAIFGMGINSHFKEKKKTIWDEVGKDIDSILNRTIAVGIWKTRKNYKNEIEDIEKIIPSQEEIQKILIYQIENKNIKITDGYMKEIQSLSKYVLYNIRNSMRNYTKTLSYYS
Protein: Eukaryotic translation initiation factor 4B1 (AtTif4B1) (eIF4B1) (Q9LIN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes the eIF4F and eIF4A RNA-dependent ATP-hydrolysis activity with different efficiency depending on mRNAs, thus providing mRNA discrimination during initiation of translation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Oxidoreductase/transition metal ion-binding protein
- Large ribosomal subunit protein uL5m
- Probable mediator of RNA polymerase II transcription subunit 19b
- Pseudouridine-5'-phosphate glycosidase
- Formin-like protein
- Large ribosomal subunit protein P3y
- Protein BTR1
- Large ribosomal subunit protein P3z
- Large ribosomal subunit protein eL13x
- Small ribosomal subunit protein uS11z
Sequence:
MSKAWGGIGIGAWADEAERADEEQAAEATAATADTQSFPSLREAAAATATSGKSRKMKKMSLSEFTTGAYTAPGGRNSVGLTQQEILQLPTGPRQRSEEEMQPGRLGGGFSSYGGRSGGRIGRDRDDSDGSWSGGGGGGGRRPYGGGFDDDRRGNQSRVSDFPQPSRADEVDDWGKEKKPLPSFDQGRQGRYSGDGGGFGGGGSGFGGGGGGGGGGLSRADDVDNWGAGKRQAPVRSSTFGSSFGDSGQEERRRLVLEPRKVESGGSETPPVVEKTSKPNPFGAARPREDVLAEKGLDWKKIDSEIEAKKGSSQTSRPTSAHSSRPSSAQSNRSESSGLNNVVKPRPKVNPFGDAKPREVLLEEQGKDWRKMDLELEHRRVDRPETEEEKMLKEEIEELRKKLEKESVAPEIKESDQEPGSNNNHNDLPEIIRGKEKDLEILTRELDDKVRFRQKPVERPGSGAGRTGTYSERTHSRAGSIDETRSFESTERPRSRGAVDAWVRPANEQRRNFQGTKERGFFSNRSSSREGW
Protein: Adenylate kinase isoenzyme 6 homolog (AK6) (EC 2.7.4.3) (Dual activity adenylate kinase/ATPase) (AK/ATPase) (Q9UU88)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity. May be involved in rRNA maturation and transcription regulation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03173, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03173, ECO:0000269|PubMed:16823372}.
Interaction partners:
- 20S-pre-rRNA D-site endonuclease nob1
- Ribonucleoside-diphosphate reductase large chain
- Adenylosuccinate lyase
- Adenylate kinase
- Nucleoside diphosphate kinase
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Inosine triphosphate pyrophosphatase
- Pyruvate kinase
- Ribonucleoside-diphosphate reductase small chain
Sequence:
MGNEERELPNIIICGTPGTGKTTLAEQVAETTELENICIGDVVKENHLHFGFDEKWKTYDVDEDKVLDYLEPKLLKGGCIIDWHTCGLFSEELIDLVVVLRTDHSKLWERLESRGYSLEKIQENNEAEIMQICLEEARESFDPKIVVELPSESIEEMESNLSRITQWVTNWKKNH
Protein: Tubulin beta chain (B1PBW0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain-like
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain-like
- Tubulin alpha chain-like
- Tubulin alpha chain
Sequence:
MREILHVQGGQCGNQIGSKFWEVICDEHGVDPTGSYTRDESSSSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSIRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQHYISLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSSTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQYQDATVEEEGEYEGEEGVEEN
Protein: Rho GTPase-activating protein SYDE1 (Synapse defective protein 1 homolog 1) (Protein syd-1 homolog 1) (Q6ZW31)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases. As a GCM1 downstream effector, it is involved in placental development and positively regulates trophoblast cells migration. It regulates cytoskeletal remodeling by controlling the activity of Rho GTPases including RHOA, CDC42 and RAC1.
Interaction partners:
Sequence:
MAEPLLRKTFSRLRGREKLPRKKSDAKERGHPAQRPEPSPPEPEPQAPEGSQAGAEGPSSPEASRSPARGAYLQSLEPSSRRWVLGGAKPAEDTSLGPGVPGTGEPAGEIWYNPIPEEDPRPPAPEPPGPQPGSAESEGLAPQGAAPASPPTKASRTKSPGPARRLSIKMKKLPELRRRLSLRGPRAGRERERAAPAGSVISRYHLDSSVGGPGPAAGPGGTRSPRAGYLSDGDSPERPAGPPSPTSFRPYEVGPAARAPPAALWGRLSLHLYGLGGLRPAPGATPRDLCCLLQVDGEARARTGPLRGGPDFLRLDHTFHLELEAARLLRALVLAWDPGVRRHRPCAQGTVLLPTVFRGCQAQQLAVRLEPQGLLYAKLTLSEQQEAPATAEPRVFGLPLPLLVERERPPGQVPLIIQKCVGQIERRGLRVVGLYRLCGSAAVKKELRDAFERDSAAVCLSEDLYPDINVITGILKDYLRELPTPLITQPLYKVVLEAMARDPPNRVPPTTEGTRGLLSCLPDVERATLTLLLDHLRLVSSFHAYNRMTPQNLAVCFGPVLLPARQAPTRPRARSSGPGLASAVDFKHHIEVLHYLLQSWPDPRLPRQSPDVAPYLRPKRQPPLHLPLADPEVVTRPRGRGGPESPPSNRYAGDWSVCGRDFLPCGRDFLSGPDYDHVTGSDSEDEDEEVGEPRVTGDFEDDFDAPFNPHLNLKDFDALILDLERELSKQINVCL
Protein: Antiholin-like protein LrgB (P60643)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. Increases tolerance to penicillin possibly by inhibiting the formation of the CidAB holin-like complexes within the membrane, thus reducing penicillin-induced lethality. Possibly plays a role in programmed cell death (PCD), triggering PCD in response to penicillin, and possibly other antibiotics, and environmental stresses.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Antiholin-like protein LrgA
- Transcriptional regulatory protein LytR
- Sensor histidine kinase/phosphatase LytS
- Holin-like protein CidA
Sequence:
MINHLALNTPYFGILLSVIPFFLATILFEKTNRFFLFAPLFVSMVFGVAFLYLTGIPYKTYKIGGDIIYFFLEPATICFAIPLYKKREVLVKHWHRIIGGIGIGTVVALLIILTFAKLAQFANDVILSMLPQAATTAIALPVSAGIGGIKELTSLAVILNGVIIYALGNKFLKLFRITNPIARGLALGTSGHTLGVAPAKELGPVEESMASIALVLVGVVVVAVVPVFVAIFF