wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock protein family H (Hsp110) member 1 (A0A0A0MSM0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATAAVLRGPAAHWVESFQKAREEGSGSGTWRGRWRRRSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFIQKEKENLSYDLVPLKNGGVGIKVMYMGEEHLFSVEQITAMLLTKLKETAENSLKKPVTDCVISVLGTAFDPFLGGKNFDEKLVEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCAELLQKIEVPLYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILSPAFKVREFSVTDAVPFPISLIWNHDSEDTEGVHEVFSRNHAAPFSKVLTFLRRGPFELEAFYSDPQGVPYPEAKIGRFVVQNVSAQKDGEKSRVKVKVRVNTHGIFTISTASMVEKVPTEENEMSSEADMECLNQRPPENPDTDKNVQQDNSEAGTQPQVQTDAQQTSQSPPSPELTSEENKIPDADKANEKKVDQPPEAKKPKIKVVNVELPIEANLVWQLGKDLLNMYIETEGKMIMQDKLEKERNDAKNAVEEYVYEFRDKLCGPYEKFICEQDHQNFLRLLTETEDWLYEEGEDQAKQAYVDKLEELMKIGTPVKVRFQEAEERPKMFEELGQRLQHYAKIAADFRNKDEKYNHIDESEMKKVEKSVNEVMEWMNNVMNAQAKKSLDQDPVVRAQEIKTKIKELNNTCEPVVTQPKPKIESPKLERTPNGPNIDKKEEDLEDKNNFGAEPPHQNGECYPNEKNSVNMDLD
Protein: Oxamate carbamoyltransferase subunit AllF (OXTCase subunit AllF) (EC 2.1.3.5) (Oxamic transcarbamylase subunit AllF) (Q47208)
Organism: Escherichia coli (strain K12)
Function: Not known; multicopy suppressor of dominant negative ftsH mutations.
Interaction partners:
- Oxamate carbamoyltransferase subunit AllG
- Oxamate carbamoyltransferase subunit AllH
- Succinate--CoA ligase subunit beta
- Carbamate kinase
- Ureidoglycolate dehydrogenase
- NADH-quinone oxidoreductase subunit C/D
- Uncharacterized protein YahG
- Putative purine permease YbbY
- Allantoate amidohydrolase
- (S)-ureidoglycine aminohydrolase (UGHY) (UGlyAH)
Sequence:
MIHAFIKKGCFQDSVSLMIISRKLSESENVDDVSVMMGTPANKALLDTTGFWHDDFNNATPNDICVAIRSEAADAGIAQAIMQQLEEALKQLAQGSGSSQALTQVRRWDSACQKLPDANLALISVAGEYAAELANQALDRNLNVMMFSDNVTLEDEIQLKTRAREKGLLVMGPDCGTSMIAGTPLAFANVMPEGNIGVIGASGTGIQELCSQIALAGEGITHAIGLGGRDLSREVGGISALTALEMLSADEKSEVLAFVSKPPAEAVRLKIVNAMKATGKPTVALFLGYTPAVARDENVWFASSLDEAARLACLLSRVTARRNAIAPVSSGFICGLYTGGTLAAEAAGLLAGHLGVEADDTHQHGMMLDADSHQIIDLGDDFYTVGRPHPMIDPTLRNQLIADLGAKPQVRVLLLDVVIGFGATADPAASLVSAWQKACAARLDNQPLYAIATVTGTERDPQCRSQQIATLEDAGIAVVSSLPEATLLAAALIHPLSPAAQQHTPSLLENVAVINIGLRSFALELQSASKPVVHYQWSPVAGGNKKLARLLERLQ
Protein: Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) (G3MU83)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQCSPDPEDLLIVPTHDIPSYDESLDPFGPEGHLSLDIDCFSKFMSRSDNRIMSKPIIVRGIPWRILAICRNQQGSRHSMNSRVNRSNFNFGFFLQCNNDELLQKRGMWRCYGTAVLEVLNADGPSIQKKIHHSFHNTEVDWGFSNYDQYDTLCNPKDGYVVNDTIKLRCRFTADVPTGANYMWDSKRHTGCIGLRNQGATCYMNSILQSFYFTTGFRRAVYNMDVGTEPNESNIVLAMQRVFYELQMASEAVETNSLTRAFGWDKLDAFNQHDVQEFCRVLLDNLETKMKGTSEEKSIPNLFRGNMKSYIKCLDVDYESSRTESFYDVQLNVLGMDSLERAFEAYTTSEILDDENKYDAGDHGLQRAEKGVKFVELPPILHVQLMRFQYCGVEQKINERFSFPEKMNLASCCELGPMLTEEDCVYSLHAVLVHSGEFHGGHYVTYINVNLHESAVDPTSSAKWCKFDDDVVSRTTTDDAIVSNFGGEKTMNSSAYMLVYVRDNAIDQFLAPIPDSQIPQSVSRTFEMERLHRNREKKKLEEEQLCMGIVLVTPDIVASNHSFDLVDQSIVHDSIPHETVWKHMFTAELYQFVHDRLFEKSAMQKIDMFDSDDEARQARRDNLRRIKSKKFNFRLWRMTDSYSLERTTQKLTSRLRPSEFIDCKTDTRLDTLLSQDFETIYVEFSNNIERPLCEYDTARDLLFFVKYYDTMTDKFTIIGHTMFDCHKRFNLYRSMLCEMIGLPADTELKYYMEHAASYLELVDLTQNYSIGRLVEEQDGGILVVEKVETSTSTQNAKQKMNELFLDVEVEFVQSFYNKKPEEEPFEQFVKRICLDDKLFTVAEEIGARLNVDPKKVLIWTRVSGSRFEPFFDDYMLNTCKGLMTRPVHDPRAYKRYRVQYAIMPFDIDEISKHRIQTKLFWQLPNGHVEELTLFPLKEGTVIDIINEAKRYYPFVEGGSGKFRLLQIGAPPLSNQRVYQIYGENTLISDLDQRTMYKLVSSALHCRLEEVPIDELDMSPGEFLCPVVHFDREPTKLFGLSFVIKIRNNELMTEVRDRLRRKLNDVSDADFAKYKFALLSRDKLQLCRTIEFNNGEKVNLADMANQTTGVPQVYIGLDHKSPIQHSSEAAIRILN
Protein: Galectin-7 (Gal-7) (HKL-14) (PI7) (p53-induced gene 1 protein) (P47929)
Organism: Homo sapiens (Human)
Function: Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11706006}. Nucleus {ECO:0000269|PubMed:11706006}. Secreted {ECO:0000305}. Note=May be secreted by a non-classical secretory pathway.
Interaction partners:
- Galectin-3-binding protein
- Apoptosis regulator Bcl-2
- Mothers against decapentaplegic homolog 3
Sequence:
MSNVPHKSSLPEGIRPGTVLRIRGLVPPNASRFHVNLLCGEEQGSDAALHFNPRLDTSEVVFNSKEQGSWGREERGPGVPFQRGQPFEVLIIASDDGFKAVVGDAQYHHFRHRLPLARVRLVEVGGDVQLDSVRIF
Protein: Nuclear pore complex protein NUP98A (Nucleoporin 98A) (Nucleoporin autopeptidase) (Q8RY25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Protein SEH1
- Protein RAE1
- Protein transport protein SEC13 homolog B
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP205
- F7H2.18 protein
- Protein transport protein SEC13 homolog A
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP160
Sequence:
MFGSSNPFGQSSGTSPFGSQSLFGQTSNTSSNNPFAPATPFGTSAPFAAQSGSSIFGSTSTGVFGAPQTSSPFASTPTFGASSSPAFGNSTPAFGASPASSPFGGSSGFGQKPLGFSTPQSNPFGNSTQQSQPAFGNTSFGSSTPFGATNTPAFGAPSTPSFGATSTPSFGASSTPAFGATNTPAFGASNSPSFGATNTPAFGASPTPAFGSTGTTFGNTGFGSGGAFGASNTPAFGASGTPAFGASGTPAFGASSTPAFGASSTPAFGASSTPAFGGSSTPSFGASNTSSFSFGSSPAFGQSTSAFGSSAFGSTPSPFGGAQASTPTFGGSGFGQSTFGGQQGGSRAVPYAPTVEADTGTGTQPAGKLESISAMPAYKEKNYEELRWEDYQRGDKGGPLPAGQSPGNAGFGISPSQPNPFSPSPAFGQTSANPTNPFSSSTSTNPFAPQTPTIASSSFGTATSNFGSSPFGVTSSSNLFGSGSSTTTSVFGSSSAFGTTTPSPLFGSSSTPGFGSSSSIFGSAPGQGATPAFGNSQPSTLFNSTPSTGQTGSAFGQTGSAFGQFGQSSAPAFGQNSIFNKPSTGFGNMFSSSSTLTTSSSSPFGQTMPAGVTPFQSAQPGQASNGFGFNNFGQNQAANTTGNAGGLGIFGQGNFGQSPAPLNSVVLQPVAVTNPFGTLPAMPQISINQGGNSPSIQYGISSMPVVDKPAPVRISSLLTSRHLLHRRVRLPARKYRPGENGPKVPFFTDDEESSSTPKADALFIPRENPRALVIRPVQQWSSRDKSILPKEQRPTAPLHDNGKSPDMATDAANHDRNGNGELGATGERIHTSVNANQKPNGTTRSDQASEKERPYKTLSGHRAGEAAIVYEHGADIEALMPKLRQSDYFTEPRIQELAAKERADPGYCRRVRDFVVGRHGYGSIKFMGETDVRRLDLESLVQFNTREVIVYMDESKKPAVGQGLNKPAEVTLLNIKCIDKKTGKQFTEGERVEKYKMMLKKKAEAQGAEFVSFDPVKGEWKFRVEHFSSYKLGDEDEEDGV
Protein: Sex-determining transformer protein 2 (Ce-Tra-2) (P34709)
Organism: Caenorhabditis elegans
Function: Plays a major role in controlling sexual cell fates. Promotes female development in XX animals where it sequesters one or more of the FEM proteins to the membrane thereby freeing the tra-1 protein (a putative transcription factor) to enter the nucleus and promote female development. In XO animals it acts as a receptor for her-1 which prevents it from binding to FEM proteins thereby repressing the activity of tra-1. Negatively regulates male development when bound to fem-3 and is required together with tra-1 for promoting spermatogenesis. Also required for feminizing tra-3 activity.
Subcellular location: Membrane {ECO:0000269|PubMed:1498366}; Multi-pass membrane protein {ECO:0000269|PubMed:1498366}.
Interaction partners:
- Sex-determination protein fem-3
- Protein her-1
- Sex-determining transformer protein 1
- Female germline-specific tumor suppressor gld-1
- Protein phosphatase fem-2
- Calpain-5
- F-box domain-containing protein
- XO lethal protein 1
- Anti-proliferative protein domain-containing protein
- FOG-1 protein
Sequence:
MKLKYNKLLVSVVIVTFVTFGLLLAECFGKSIDYQEKSIFPSFVSQGFFETRTNNEEYIIEKIAQTQENGVDMRSTLHFTQHGYLLNNISNLKIKFRQKTYTLNDVCFKPHITIFQQSSSSDQNEYPHYIQRLLLEMQRLSPCLIVTPLNCFYDIYRIHGEISNWNKNTDFLNRRLRNSYIEAIGENDERPYVKSNYGPSLIKSWADHMFDLPSKSFTNSTKDALFQKIKLWLLSIEPRQKTCAASIHSCDTPLDSEHYFNICTDMQSVDNFAEKKTKFKLEDVDEEFAMNLDCVDDQEQFIEWMQELEIRKMYSHVTEKPDYPNVVNQTCDKIFHDLNSTGIEFFDGSRSFSSTKSQFDTMQTEIVLLTPEMLLSAMQHSDFVNGFESIWTIEKAEELIHEFRLALKEETEKFKENRMSKMIRVTSRVLDNTVTTKLQSFSEKQTIHFVVNVHSLIVILFTIFVWSGAPLRSAFMFFVRDALTCLLFCFVCSTDGVIVLDTELIKYIIVLTLANLYFTTRSSFCTERLSRCIQREKRFPINSNFASLITVDTMTDSRQIQYFLSTVTKYQAAQDSYSNELFERFPKNWGCTSILIFPIVFVYWYFIDSNFDKICVSVLPSFCLAAGEELFAKNMFWKEREAMQAKQRLENEEQAESITGSSLEKLFAGNKPVSNTDKANIVKKSSIIRNQKPCLQDLSPGTYDVSNFMKYPHQASRIFREKIIGLYLRILKLRTLGVILCIPAILLIVISIGLLFIPVKRETLHTDSKQDDIFIEFEIFNFSTNWKIVNQNLKQFSEDIESIGTLYTISNWQKSFERFEQETNKNASAEWNILFKWINDEPINSAVTLFSEKSSGNQTIANPFKFRLRYGFDAKNETTVIEIVQKIDELLSKCSKNLSPKAVGVLYEHYHRIAVVWNLFAFNQLTTAGIFIILLSIITFIFAITPTIKATFLFSLLVVGTQIEVAALVHLFSLDHHQIYTNLALFAGFLAAWDPFCALLRYRRRILYKSETRRTPELASKRRVLLPIVATADIAQFFVLLITAFSILAIICSIVPELNIFFVPTVILIVIQIVAVFNSIIVSIATKQMFESEVRHYLHRDLRGSTTAVRVYNLVQKQRLASSLDEPQVELDEFSIKRSSPPCRYYAPPPKYSCKKRSRSSDEDEDSDPNQPGPSNRRSPKTGNKRVRGNGDNTELYIPNRYELIVSGKSVGGNTSAAWNGPGSTLEQNMNALEECFELGVDEYDFDEHDGDEGCELVQDMLDRERNLMNKRSTAQRRESRNIEKMKKSQENLDKEKSEEKISESKKNQDDSIESPNLPGTPANLPVDEPLPPVGRLYIVEHVLPEEYRRDPLTEPPSMEDCIRAHSDPNLPPHPRADQYPASFTRPMVEYCEDIYWTHRTGQLPPGLQVPRRPYDYYHITERTPPPEDLNWVPPAESPPIPIPQQAFDLLEERRRNHREQQDEAREGDLSDPEV
Protein: Autoinducer 2 sensor kinase/phosphatase LuxQ (EC 2.7.13.3) (EC 3.1.3.-) (P54302)
Organism: Vibrio harveyi (Beneckea harveyi)
Function: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-2, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Autoinducer 2-binding periplasmic protein LuxP
- Phosphorelay protein LuxU
- Aerobic respiration control sensor protein
- diguanylate cyclase
- S-ribosylhomocysteine lyase
- histidine kinase
- histidine kinase
- Diguanylate cyclase domain protein
- histidine kinase
- histidine kinase
Sequence:
MTTTRSNIKKRRSLATLITKIIILVLAPIILGIFIQSYYFSKQIIWQEVDRTKQQTSALIHNIFDSHFAAIQIHHDSNSKSEVIRDFYTDRDTDVLNFFFLSIDQSDPSHTPEFRFLTDHKGIIWDDGNAHFYGVNDLILDSLANRVSFSNNWYYINVMTSIGSRHMLVRRVPILDPSTGEVLGFSFNAVVLDNNFALMEKLKSESNVDNVVLVANSVPLANSLIGDEPYNVADVLQRKSSDKRLDKLLVIETPIVVNAVTTELCLLTVQDNQSVVTLQIQHILAMLASIIGMIMIALMSREWIESKVSAQLESLMSYTRSAREEKGFERFGGSDIEEFDHIGSTLESTFEELEAQKKSFRDLFNFALSPIMVWSEESVLIQMNPAARKELVIEDDHEIMHPVFQGFKEKLTPHLKMAAQGATLTGVNVPIGNKIYRWNLSPIRVDGDISGIIVQGQDITTLIEAEKQSNIARREAEKSAQARADFLAKMSHEIRTPINGILGVAQLLKDSVDTQEQKNQIDVLCHSGEHLLAVLNDILDFSKIEQGKFNIQKHPFSFTDTMRTLENIYRPICTNKGVELVIENELDPNVEIFTDQVRLNQILFNLVSNAVKFTPIGSIRLHAELEQFYGAENSVLVVELTDTGIGIESDKLDQMFEPFVQEESTTTREYGGSGLGLTIVKNLVDMLEGDVQVRSSKGGGTTFVITLPVKDRERVLRPLEVSQRIKPEALFDESLKVLLVEDNHTNAFILQAFCKKYKMQVDWAKDGLDAMELLSDTTYDLILMDNQLPHLGGIETTHEIRQNLRLGTPIYACTADTAKETSDAFMAAGANYVMLKPIKENALHEAFVDFKQRFLVERT
Protein: stearoyl-CoA 9-desaturase (EC 1.14.19.1) (W5PZ56)
Organism: Ovis aries (Sheep)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
SQCPRAQMPAHLLQEEISSSYTTTTTITAPPSRVLQNGGGKLEKTPLYLEEDIRPEMRDDIYDPTYQDKEGPKPKLEYVWRNIILMGLLHLGALYGITLIPTCKIYTFLWVLFYYVISALGITAGVHRLWSHRTYKARLPLRVFLIIANTMAFQNDVFEWSRDHRAHHKFSETDADPHNSRRGFFFSHVGWLLVRKHPAVREKGATLDLSDLRAEKLVMFQRRYYKPGVLLLCFILPTLVPWYLWGETFQNSLFFATFLRYAVVLNATWLVNSAAHMYGYRPYDKTINPRENILVSLGAVGEGFHNYHHTFPYDYSASEYRWHINFTTFFIDCMAAIGLAYDRKKVSKAAVLARMKRTGEESYKSG
Protein: Tetrahydromethanopterin S-methyltransferase subunit A 1 (EC 7.2.1.4) (N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A 1) (P80184)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Part of a complex that catalyzes the formation of methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and methyl-tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01093, ECO:0000269|PubMed:8223548}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01093, ECO:0000269|PubMed:8223548}.
Interaction partners:
- Tetrahydromethanopterin S-methyltransferase subunit F
- Tetrahydromethanopterin S-methyltransferase subunit C
- Tetrahydromethanopterin S-methyltransferase subunit G
- Tetrahydromethanopterin S-methyltransferase subunit H
- Tetrahydromethanopterin S-methyltransferase subunit D
- Methyl-coenzyme M reductase I operon protein D
- Tetrahydromethanopterin S-methyltransferase subunit E
- Tetrahydromethanopterin S-methyltransferase subunit B
- Tungsten formylmethanofuran dehydrogenase, subunit A
- Methyl-coenzyme M reductase I subunit alpha
Sequence:
MVEKKSPAEGWPVVNGDYIVGDPESPVAATTLASHIEDIPVEAGAAIAGPCKTENLGIEKMIANLISNPNIRFLILCGSEVQGHITGQSIEALHQNGVDPDKRNIIGATGAIPYIENIPDEGIERFQKQLEIVNLIDVEDADAIKAKVKECIEKDPGAFEEEAMIIKVEEGGEEEEGEEVKPVAPETALIEARMRNIQTQVKMIGSTNRMFAGMYSGKVQGIMIGLAFTLTLGILLLV
Protein: Probable mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Processing A-glucosidase I) (O14255)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glucosidase 2 subunit alpha
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
- Calnexin homolog
- Putative oxidoreductase C1F5.03c
- RNA exonuclease 4
- Putative holocytochrome-c1 synthase
Sequence:
MVSDMLGGNKRWILFGLLSFLLNCVLVSCSVEDIEKAANDSFLWGPYRPNLYVGIRPKIPDSLMTGLMWSNVDDYARFSKMRHSAEHGDDIGAFGWKHYDVRRGGQQVIDDFLMGIKLETDFVKLPEGNWALRVHGIPLPGAPTDLTTSLFFYAYVEGEGKVGTKVNHANHVYMEGKTPDLGKFRIQTFNRLGEHPVSPASVDLESMVMDKDFFAGFNVKKEGAWRTSELILYLLDTKMKVISDKEGYESLKDLPPAYSTLTLPNLPSEEGLQFIQKVFKGEFMFDIVFNYASSKKISEEMISQAIDKNLQEFEEKFQATFPLKAPYDTEKAHQIFAHTAFSNLFGNVGFFTGDSIVSKNPIELDDEDYEFMQGFESAAGKLAEGTAFHDIERSLFTIVPSRPHFPRGFYWDEGFHLLPVGLWDNDFSLEILKSWFSLVNEDGWVGREQILGEEARSKVPDEFQTQYPDIANPPTLILALKGYIERLQEQQGKLNNRFSGEGEDYSLDDLEYLRSVSISNPEKSVQFLRDLFPLLLRHYEWFRETQKGDFETWERECFSQVEGYRWRGRTYQHCLASGLDDYPRAQPPSTAELHVDLLSWMTSFTRSLHFVAEFLGETEEAEKLAGYENAMLRNLEDNHWDEEVQAYCDSSVDEYDDPINVCHKGYVTLLPMMLGLLPADSGRLTSLLKLIRDENELWSPYGIRSLSMNDVYFGTGENYWRGPIWINMNYLILSSLYQNYINTPGPNQNLARSIYEELRTNVVNNVFENWRQTGIFWEQYDPTTGKGQRTKDFTGWTSLVVNIMSENY
Protein: Polyadenylation and cleavage factor homolog 4 (Q0WPF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes flowering by suppressing FLC-mediated inhibition of flowering through the regulation of FCA pre-mRNA alternative processing. Regulates mRNA maturation including alternative polyadenylation, splicing or transcription initiation of stress-associated genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:18298670}. Cytoplasm {ECO:0000269|PubMed:18298670}.
Interaction partners:
- Protein CLP1 homolog
- 30-kDa cleavage and polyadenylation specificity factor 30
- Polyadenylation and cleavage factor homolog 1
- Polyadenylation and cleavage factor homolog 5
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulating factor 64
- Cleavage stimulation factor subunit 77
- Cleavage and polyadenylation specificity factor subunit 3-I
- Protein CLP1 homolog 5
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Sequence:
MDSEKILNPRLVSINSTSRKGMSVELPQKPPPPPSLLDRFKALLNQREDEFGGGEEVLPPSMDEIVQLYEVVLGELTFNSKPIITDLTIIAGEQREHGEGIANAICTRILEAPVEQKLPSLYLLDSIVKNIGRDYGRYFSSRLPEVFCLAYRQAHPSLHPSMRHLFGTWSSVFPPPVLRKIDMQLQLSSAANQSSVGASEPSQPTRGIHVNPKYLRRLEPSAAENNLRGINSSARVYGQNSLGGYNDFEDQLESPSSLSSTPDGFTRRSNDGANPSNQAFNYGMGRATSRDDEHMEWRRKENLGQGNDHERPRALIDAYGVDTSKHVTINKPIRDMNGMHSKMVTPWQNTEEEEFDWEDMSPTLDRSRAGEFLRSSVPALGSVRARPRVGNTSDFHLDSDIKNGVSHQLRENWSLSQNYPHTSNRVDTRAGKDLKVLASSVGLVSSNSEFGAPPFDSIQDVNSRFGRALPDGTWPHLSARGPNSLPVPSAHLHHLANPGNAMSNRLQGKPLYRPENQVSQSHLNDMTQQNQMLVNYLPSSSAMAPRPMQSLLTHVSHGYPPHGSTIRPSLSIQGGEAMHPLSSGVLSQIGASNQPPGGAFSGLIGSLMAQGLISLNNQPAGQGPLGLEFDADMLKIRNESAISALYGDLPRQCTTCGLRFKCQEEHSKHMDWHVTKNRMSKNHKQNPSRKWFVSASMWLSGAEALGAEAVPGFLPTEPTTEKKDDEDMAVPADEDQTSCALCGEPFEDFYSDETEEWMYKGAVYMNAPEESTTDMDKSQLGPIVHAKCRPESNGGDMEEGSQRKKMRS
Protein: MAU2 chromatid cohesion factor homolog (Sister chromatid cohesion protein ssl3) (O94459)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in sister chromatid cohesion. Forms a complex with mis4, which is required for the association of the cohesin complex with chromosomes.
Subcellular location: Nucleus. Note=Associates with chromatin. {ECO:0000305}.
Interaction partners:
- Sister chromatid cohesion protein mis4
- Structural maintenance of chromosomes protein 1
- Sister chromatid cohesion protein pds5
- Wings apart-like protein homolog 1
- Structural maintenance of chromosomes protein 3
- Cohesin subunit psc3
- Cohesin subunit rad21
Sequence:
MTGLNETDARILVTSRHLFLWPLAETYFKNAEKVLQDCGVCDSFGRLLSTGLQCLYSVLMDTKMEPRVELLTRKRICEVLLSHTVEYADVEAILNRALIIAEQHNLTEYKFSLQLLLSRVFCRTSPKAAKVLLTRCVREAEEYAKVAEIYHSNNQSNPHRWVYEFLLATLEFQNVSQVANSIHNYANHHKHQHLQLLAMILNQSLPMDEISTDSDQISILCLVTQIAQCLRKGEILLAREILPKIHSKLESETFVWPSSYIDFFIDDTSKISIKWMSINQLYLLIYLISGFCYISDSTSGRASRFLQEGLRITGDFKHQERCVLEYLESQKWINNITKDMKYYLIATYLSRSRLSKAERILQSTEDDQTGFLGILKGMYLQKRGDLKKAEVHYRETAKNFSFRTDTFIISTLNLINILEDSAAASRCLESIEPLCNKHEKKIFKLWLLVLKVIREGPQVHQSNVLPRVIQQSSEYANTQLQYISLTELSERFGKLEHAEKMAISALELAKKSKDELWCLISGRILEDFYRSVQKYDKMRQQALENSAYSKLIEDIYSFV
Protein: Histone H2A (F4KCF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU003767}.
Interaction partners:
Sequence:
MDSGTKVKKGAAGRRSGGGPKKKPVSRSVKSGLQFPVGRIGRYLKKGRYSKRVGTGAPVYLAAVLEYLAAENSCGFCSVASLTIYRCRMSSSDFRVLELAGNAARDNKKNRIIPRHVLLAVRNDEELGTLLKGVTIAHGGVLPNINPILLPKKSEKAASTTKTPKSPSKATKSPKKS
Protein: Probable ubiquitin carboxyl-terminal hydrolase 12 (EC 3.4.19.12) (Deubiquitinating enzyme 12) (Ubiquitin thioesterase 12) (Ubiquitin-specific-processing protease 12) (O60079)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Putative zinc protease mug138
- COP9 signalosome complex subunit 5
- Probable ubiquitin carboxyl-terminal hydrolase 2
- Ubiquitin carboxyl-terminal hydrolase 11
- Cullin-3
- Ubiquitin carboxyl-terminal hydrolase mug105
- Probable ubiquitin carboxyl-terminal hydrolase 3
- BTB/POZ domain-containing protein 3
- RING-box protein pip1
- Small ribosomal subunit protein uS9m
Sequence:
MDSLSESSTSSYHGKRPRSLSEESQSSSNMDDISQKSISLGDASEISKNLPSIAEQKQLIGELVNNQPELELGQVDNYILSYSWYERLCSYLAEDGPFPGPVDQEDIADLETGTLKPDLQEEIDFTIISRDVWDLLVRWYGLKGPEFPRETVNLGSESHPHLVVEVYPPIFSLTLLSTNAVDANESHKPKKISLSSKSTLEDLLEGVKYTLSLPSDQFRLWRVDTDQPLHRTIDPSSFIKINSKEIIDFLEKSKTLVELGMDSSCSLVAECMINETWPVDRALRLQFLIQQRNNQSSNEEQKQEKRVPGTCGLSNLGNTCYMNSALQCLTHTRELRDFFTSDEWKNQVNESNPLGMGGQVASIFASLIKSLYSPEHSSFAPRQFKATIGKFNHSFLGYGQQDSQEFLAFLLDGLHEDLNRIYQKPYTSKPDLYEVDEEKIKNTAEECWRLHKLRNDSLIVDLFQGMYRSTLVCPVCNTVSITFDPFMDLTLPLPVKQVWSHTVTFIPADTNLTPLAIEVVLESKAATIEDLVKYVAEKSGCSDYRKILVTETYKGRFYRFLTQLSKSLLMEISEEDEIYLYELERPYEDGSDDILVPVYHISDDSTNSANSYMSSRDFGHPFVLQLSDNEVTDASFISEKLKLKYQQFTTLKNLKNIDSLESLELGHEDEQVQKGPLDVDMDHSQTPLFEMRVFHDRFEKIPTGWNMSVSNLPLLTERDKKDLESTVDPLDAHSIEEEDDSEFKDVAPGSYPEPSKSNENTKLTAKENDRLLIQGDLLVCEWPEKSYQFVFSVAPSSPQMGRSLWLESKTILSDKKDDSEDSRTITLNDCLDEFEKTEQLGEEDPWYCPTCKEFRQASKQMEIWRCPEILIFHLKRFSSERRFRDKIDDLVEFPIDNLDMSMRTGSYKLSEKENPKLIYELYAVDNHYGGLGGGHYTAFAKNPDNGQFYCFDDSRVTPVCPEETVTSAAYLLFYRRKTS
Protein: Melanocyte-stimulating hormone receptor (MSH-R) (Melanocortin receptor 1) (MC1-R) (Q01726)
Organism: Homo sapiens (Human)
Function: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31097585}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-opiomelanocortin
- Agouti-signaling protein
- Tyrosinase
- P protein
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Membrane-associated transporter protein
- E3 ubiquitin-protein ligase MGRN1
- Sodium/potassium/calcium exchanger 5
Sequence:
MAVQGSQRRLLGSLNSTPTAIPQLGLAANQTGARCLEVSISDGLFLSLGLVSLVENALVVATIAKNRNLHSPMYCFICCLALSDLLVSGSNVLETAVILLLEAGALVARAAVLQQLDNVIDVITCSSMLSSLCFLGAIAVDRYISIFYALRYHSIVTLPRARRAVAAIWVASVVFSTLFIAYYDHVAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIARLHKRQRPVHQGFGLKGAVTLTILLGIFFLCWGPFFLHLTLIVLCPEHPTCGCIFKNFNLFLALIICNAIIDPLIYAFHSQELRRTLKEVLTCSW
Protein: Alkaline protease secretion protein AprE (Q03025)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the secretion of alkaline protease.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Alkaline protease secretion protein AprF
- Alkaline protease secretion ATP-binding protein AprD
- Serralysin
- Uncharacterized protein
- Proteinase inhibitor
- Probable ATP-binding/permease fusion ABC transporter
- Transport protein HasD
- Probable outer membrane protein
Sequence:
MTRTVKRDENAYARLGWLLVLFGFGGALLWAAFAPLDQGVAVPATVIISGQRKSVQHPLGGVVKHILVRDGQHVEAGEPLIRMEPTQARANVDSLLNRYANARLNQARLQAEYDGRRTLEMPAGLAEQAPLPTLGERLELQRQLLHSRQTALANELSALRANIEGLRAQLEGLRQTEGNQRLQQRLLNSQLSGARDLAEEGYMPRNQLLEQERQLAEVNARLSESSGRFGQIRQSIAEAQMRIAQREEEYRKEVNGQLAETQVNARTLWEELSSARYELRHAEIRAPVSGYVAGLKVFTDGGVIGPGELLMYIVPNSDSLEVEGQLAVNLVDRIHSGLPVEMLFTAFNQSKTPRVTGEVTMVSADRLLDEQNKQPYYALRAQVDAAAMGKLKGLQIRPGMAVQVFVRTGERSLLNYLFKPLFDRAHVALAEN
Protein: Cathepsin B (EC 3.4.22.1) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain] (P43233)
Organism: Gallus gallus (Chicken)
Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.
Subcellular location: Lysosome.
Interaction partners:
- Apoptosis regulator Bcl-2
- Uncharacterized protein.
- Cathepsin D
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Cystatin
- Legumain.
- Lysosome-associated membrane glycoprotein 1
- Annexin A2
- Cystatin B
Sequence:
MSWSRSILCLLGAFANARSIPYYPPLSSDLVNHINKLNTTGRAGHNFHNTDMSYVKKLCGTFLGGPKAPERVDFAEDMDLPDTFDTRKQWPNCPTISEIRDQGSCGSCWAFGAVEAISDRICVHTNAKVSVEVSAEDLLSCCGFECGMGCNGGYPSGAWRYWTERGLVSGGLYDSHVGCRAYTIPPCEHHVNGSRPPCTGEGGETPRCSRHCEPGYSPSYKEDKHYGITSYGVPRSEKEIMAEIYKNGPVEGAFIVYEDFLMYKSGVYQHVSGEQVGGHAIRILGWGVENGTPYWLAANSWNTDWGITGFFKILRGEDHCGIESEIVAGVPRMEQYWTRV
Protein: DNA damage checkpoint protein 1 (Q08949)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Checkpoint protein RAD24
- DNA damage checkpoint control protein MEC3
- DNA replication regulator DPB11
- Serine/threonine-protein kinase MEC1
- DNA damage checkpoint control protein RAD17
- Replication factor C subunit 2
- Replication factor C subunit 4
- Replication factor C subunit 5
- Replication factor C subunit 3
- DNA repair protein RAD9
Sequence:
MSFKATITESGKQNIWFRAIYVLSTIQDDIKITVTTNELIAWSMNETDTTLCQVRFQKSFFEEYEFKPHEIVFGENGVQVIEDTYGNSHKLYSFRVNGRHLTTISRKPDGDGIKSFTIAVNNTSTCPESLANRLIVVIEMDSLIVKEYCPQFQPIKYDPIIINLKYKRRFLDVFGTAASDRNPQEPLDPKLLDVFTNTERELTSALFNEEVESDIRKRNQLTAADEINYICCNSTLLKNFLDNCNVNVTDEVKLEINVHRLSITAFTKAVYGKNNDLLRNALSMSNTISTLDLEHYCLFTTIEDEKQDKRSHSKRREHMKSIIFKLKDFKNFITIGPSWKTTQDGNDNISLWFCHPGDPILMQMQKPGVKLELVEVTDSNINDDILEGKFIKTAISGSKEEAGLKDNKESCESPLKSKTALKRENLPHSVAGTRNSPLKVSYLTPDNGSTVAKTYRNNTARKLFVEEQSQSTNYEQDKRFRQASSVHMNMNREQSFDIGTTHEVACPRNESNSLKRSIADICNETEDPTQQSTFAKRADTTVTWGKALPAADDEVSCSNIDRKGMLKKEKLKHMQGLLNSQNDTSNHKKQDNKEMEDGLGLTQVEKPRGIFD