wanglab/gogpt-training-data huggingface dataset:
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q4GY50)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MLLPVFLFLALFLSAKQATSDVGPADNGAVFRQLCKLVALAEKSPALGPHATLNTAAVTEMEELNISLSPATWQAKFAKAEVTDTLEEMKTKANVTDDNIAKDWHNKWRQWVLAYKATRPDTAAATRIKEAGFNNLTPGRRWAAQMRVQAHLARAQALLTEGKQYSAAAAKPTAADYPKKLKDAVLGDDVGNKASVTIAKTFSGGANSGRSNACGGNIANHPATTAAATLMCVCAEAAANQPGGACISGQTVTTTWTTAAPPALGVWTQLAGECPDDDGAVISADALLTPIRELNSMVVKLNNAGFLGKTVTKSNCDGSSDAGVCVKYSDFTGKGDKKFTDIPWVVKLVNLAQDLQLREAAAAAIKNINHQLKAEREAAYACATALTEPPTTVETKSLSSKTKEDKEGCKQQKSNKTACTEANCKWQGKTETDGPCKPKDGEGQTNAAAGTGTGTAGDQKKERAASAWCAKHGTDETACENDKTGDKQNCAFRKGKESEDEPEKEKHSLCSFIVNNKLALIAAAFFSLEAFQNCKDF
Protein: SD02526p (Q8T9G1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLAPIVRNSLGQEQRSQLDGLFRHRDEEADDEVEEEEQNIVRRKPPNRANLYLSELSSGRRKPLKMQRDVKLQRRTKDEEDDDDVQVIDYLSPAGLPIEVEQPKQLTRMKAKYLHFADNRRPPYYGTWRKKSSSISARRPLAQDKVLFDYEVDSDCEWEEEEPGESLSASEDEKEKESEEESEEEYNEWYVPHGHLSDEELQNDGDGMEDGHTREAQKAKLQVLQQEFAQEMKKQTKKIKARLLGPVWLDENGNKSELFPAIFAHTIDMYACWQVEPLSLEPPPEPERQDQTPEQPVPLQLDDRLMQQLVRLTHGNRNSKTFLINEYLEYLKTQATAEANQTTLPSKAVLREKFDELASWKTVELSTPEAAAASANSAKKGRKPKKRLCWVVASDMLEKFQLPDLQLQNQWNYTLTPKVSDGPDAAQQEQSPPADAVPAASPASNQTTNSAPTTPISGQTQAGQGVKKRATLIMSVPRDQPIPSATKNKLISQFLQRQSDASKPKEKMQEKPPPIVFDDVVMLSD
Protein: Acrosin (EC 3.4.21.10) (P79343)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MRIIGGQDAAHGSWPWMVSLQIFTYHNNRRYHVCWGLLLNAHWLLTAAHCFRIKKKVTDWRLIFGAKEVEWGSNKPVKPPLQERYVEKIIIHEKYSASSEANDIALIKITPPVICGHFIGPGCLPQFRAGPPRVPQTCWVAGWGFLRENARRTSPVLQEAHVDLIDLDLCNSTRWYNGRIRSTNVCAGYPEGKIDTCQGDSGGPLMCKDSVENSYVVVGITSWGVGCSRAKRPGVYTSTWSYLNWIASKIGSNTVHMIQLPTAPPASTPAAQASPGSVQPSIRPPWFFQHVPQPPPSQQAIAVAQPSRPSSPRPSVPPAPRPPRPPPPQPSTRPPQALSFAKRLQQLIEVLKGKTFLNEKSNYEMETTGLPGQHASS
Protein: E3 ubiquitin-protein ligase TRIM9 (Q9UAQ3)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Netrin receptor unc-40
- Netrin unc-6
- Slit homolog 1 protein
- Abnormal cell migration protein 10
- UNC-34
- CRAL-TRIO domain-containing protein
- Protein sax-3
- Netrin receptor unc-5
- Protein eva-1
- Protein madd-4
Sequence:
MEEELKCTICIRFFEDPIILTCGHSLCRMCALKAHQPSTSSGSSSTSSPRPSTPGILSQILSSASSPISPQSAGSSSGASDTMSLCVSDNGDHESDKLSVVSETDSGVVGCGRTSRPSSIIGPPLSRLHNILTPSTSGVQLVCNSCQKPSYFCDENSIVSAPTNLAMQNVIRRYLLAHPDKAFLTPSCSGSSGSSGSSQSSDEASSQCQLCEGSENRMANVFCEQCDIYYCTPCQTALHPARGPLAKHNLLQANDGERKKSSAITTATTVRDLLRCATHPGEGLTMYCLACKVPVCSRCLQDLRHANHDVQSLPIACKGHKTELSTTLQQLSEKAKTATEEIGRLKGLHDVVKNNCNDFKSSLCIQIDQLIEQLQMRKEKLMQHVDEQADNKRRILKSQIVKCTGKLTKTSALIQFCIEALKEPDPTVYMQISNALLHRSTSLEFLWHKEMRTKPETDSEFVLNLDTKHLQYTIQTLDFAQLKAGPRGTRFKGDASRVPSAPIIETSECSAENNSVTVVWRPRNDGSAVDGFALEIDTGRDDGNFKEVYSGPDTICTIDGLHFNTVYAARVKSYNSAGESEYSESICLQTAHVAWFQLTKSPSQRDMILSNECATLSGSSLEYRTILGSIAFSKGVHYWEVTIDRHDGNSDIVIGVAQPAVNRNVMLGKDLHGWSMYVDGERSWYLHNETHHNRVLGGVTRGTVIGVRLDCDRGTMEYTVNDRKRIYQDDSMAFTNMPRGLYYPAFSVNANSSITVHTGLSSPSS
Protein: RNA polymerase II-associated protein 1 C-terminal domain-containing protein (Q583E1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVEEPSGIVLYGDVVERTGIVEGGTSKNSSSGNGNIEKGRSILRPIQAVVGRAFPHIDPNRFYGNNATEMQCEGDPNDGRMPMKTTKSATFSSITTSGFTAHVQPGLSGNIEAASISADRGFGAIDCMSRQRQWDPKDFENLECGYYTVPLNTCNAAPAGTCVSHPEVPSGELYVELLLQFLRSTVRKHRECAMEALRARLLVDRPLRELFTTGTECAQLLHLIINELASAGHALPCRVAAECLVLLLFDPTMEVEEAIGEIGCPPTDLAEISTNECNDMTFAELSECMRSGEDKGNALERLGMTKAVLDSLNLIPCTLASRLLLGSGVLLLPNVAIRVASDPRFVRFVRERLRSVLLGSETVSGVVEELLVLRHVLRLQQTCATLLPALHETLMLFIRFVCSIPVEQARSPHDVVGCLAAFLVVRAAVRQGFVGLFNDTAEGLLSATVLGSGIPAEMWLLLASSSEGDGVGRVFPTMEVFAAELARAAVRTIQAHITVAETGAANGEETGHLVSLLAALSSMHYLATYFTLYAGSDDLLFLLGTEHETQSRLKEFMAANVLTSKGLQHAFLRLSSKRHTPLPLDLLNTRNVKTTVGGGEDGKICLNKIELVGACWASLTHARVRLAAAFTGLVHMTEWEVPVGYATALATSFEEKCLGLKDVMGRLLPDELCTMVEVVQLMRRGVHGTSAVGGGSTVSQQQQRDSCAQNSSSRACTQKLHIAETFLLHSIFLTKHGQDVAPGLIDAILGLQDVTIADEAAVIDPFVEPTVTLAESLRRAVAQTRWPWFLFPLYDEDLREKGVWCGWVHRTLGMHQRMKDVLQWDLILCHTLRWAISSCHSFDKWEEADVRTDEEVKRLLHELCTGVLPRAGRLIATSASDVLKALASTIPLHEEVSMEYCLFVALAITCTACEPTAAVSIARLLSNTLLEGSTYCLTSSSDFEVTEAPIPHHSGSNSTAARSNPAVSSAHGYDNKLLNQWAASGSLLCDNTQVSATAQWDLGNFTEVLHSVEFYGPGGPAHGSNAIKKGILQNLVEGIARLYLRQRPLTAFECQALRQDLQQLQWCPPCLREELDKCNN
Protein: Acyl-coenzyme A oxidase (G8BAZ8)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- acetyl-CoA C-acyltransferase
- Oleate-induced peroxisomal protein POX18
- Probable electron transfer flavoprotein subunit alpha
- Probable electron transfer flavoprotein subunit beta
- Acyl-coenzyme A oxidase
- Acyl-CoA dehydrogenase NM domain-like protein
- Peroxisomal hydratase-dehydrogenase-epimerase
- acetyl-CoA C-acyltransferase
- acetyl-CoA C-acetyltransferase
- Acetyl-CoA C-acyltransferase
Sequence:
MSVPFTAKNVNLSKGPDPQTSIQTERAAQKFNPQAMQYFLEGSRERAEVIKALTQQMERDPILFTDGSFYDMNKNQLREMTAVKINRIARYMEVDSPDVYAQRLSLIGVFDPSVCTRIAVNLGLFANCIKGNGTADQIKYWTLDKHTNYLRGIYGCFGMTELAHGSNVMGLETTATFDKENDEFIINTPHVGATKWWIGGAAHSATHCTVYARLKVDGEDYGVKTFVVPLRDSNHDLMPGVTVGDIGAKMGRDGIDNGWIQFSSVRIPRFFMLQKFCKVSRDGEVVLPPLEQLSYSALLGGRVMMVLESYRMLARVSTIALRYAIGRRQFKGDNVDPNDENALETQLLDYPLHQKRLFPYLAAAYVISAGALKVEKTIEDTLAFLDKAVANNDQKAIMQSIGAMKSLFVDSGSLKPTCTWLAAEGIDQCRQACGGHGYSAYNGFGRAYNDWVVQCTWEGDNNVLCMNTGKPFVKNVIGLEDNGKAVKGGSEFLNQLKDYTGSGASKVILENANDITDLKKFIKSLEVAIIRLSSETAKTVRKENFDFVGAELVNISKLNAHRYVLSTYVDRVDAHDDASLKPYLYDLGRVYAATVVLDKFSGIFLTFNVASTNAITDLAKIVIPKLCKQIRPNVVGLTDSFQMSDMMINAAIGRYDGDIYENYFDLVKTLNPPRNDKAPYSAALEGMLNRPSLEERERFEKSAETAEILSK
Protein: 23S rRNA-specific endonuclease VapC20 (EC 3.1.-.-) (Ribonuclease VapC20) (RNase VapC20) (Toxin VapC20) (P95004)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An endoribonuclease that cleaves both E.coli and M.smegmatis 23S rRNA between G2661 and A2662 in the sarcin-ricin loop (SRL, E.coli 23S rRNA numbering). The SRL sequence is highly conserved and is implicated in GTP hydrolysis by EF-Tu and EF-G. Acts on purified ribosomes but not on isolated RNA in E.coli, nor on a shortened artificial substrate. Upon expression in E.coli inhibits cell growth, colony formation and translation. Its toxic effect is neutralized by coexpression, or subsequent expression (tested over 2 hours) with cognate antitoxin VapB20.
Interaction partners:
- Antitoxin VapB20
- Ribonuclease VapC26
- Ribonuclease VapC4
- Ribonuclease VapC15
- Ribonuclease VapC11
- Ribonuclease VapC25
- Ribonuclease VapC19
- Ribonuclease VapC32
Sequence:
MIFVDTSFWAALGNAGDARHGTAKRLWASKPPVVMTSNHVLGETWTLLNRRCGHRAAVAAAAIRLSTVVRVEHVTADLEEQAWEWLVRHDEREYSFVDATSFAVMRKKGIQNAYAFDGDFSAAGFVEVRPE
Protein: Desmoglein-1-alpha (Desmoglein-1) (Dsg1-alpha) (DG1) (DGI) (Desmosomal glycoprotein I) (Q61495)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q7TSF1}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q7TSF1}. Cell junction, desmosome. Cytoplasm {ECO:0000250|UniProtKB:Q02413}. Nucleus {ECO:0000250|UniProtKB:Q02413}.
Interaction partners:
- Desmocollin-1
- Junction plakoglobin
- Corneodesmosin
- Desmoglein-1-beta
- Plakophilin-1
- Desmoplakin
- Desmoglein-1-gamma
- Plakophilin-3
- Plakophilin-2
- Keratin, type II cytoskeletal 1
Sequence:
MDWHSFRIAALLLTSLVVLEVNSEFQIQVRDHNAKNGTIKWHSIRRQKREWIKFAAACREGEDNSKRNPIAKIHSDCAANQPVTYRISGVGIDQPPYGIFIINQKTGEINITSIVDREVTPFFIIYCRALNAQGQDLENPLELRVRVMDINDNPPVFSMTTFLGQIEENSNANTLVMKLNATDADEPNNLNSMIAFKIIRQEPSDSPMFIINRKTGEIRTMNNFLDREQYSQYSLVVRGSDRDGGADGMSAESECSITILDVNDNIPYLEQSSYDITIEENALHSQLVQIRVIDLDEEFSDNWKAIIFFISGNEGNWFEIEMNERTNVGTLKVVKPLDYEAMKNLQLSIGVRNVAEFHQSIISQYRLTATMVTVTVLNVIEGSVFRPGSKTFVVDSRMEANHRVGEFVATDLDTGRASTNVRYEMGNNPENLLVVDSRTGIITLRNRVTMEQYQRLNGEYKGTVLSIDDSLQRTCTGTIVIELSGTGWVTGSESGGSSSGSGDDRDRVTNGYQGTSSTENPQRVTGSWGGSGIDGTRPNTNPFQGDPDETLETPLYGDNVHFGPAGIGLLIMGFLVLGLVPFLLICCDCGGAPGGGAGFEPVPECSDGAIHTWAVEGPQPEPHEGITTICVPQMPPGNANVIEYIDNSGVYTNEYCGREMQDLGGGERTTGFELMDGVKTSAAPEICQEYSGTLRRNSMRECRDGGLNMNFMESYFCQKAYAYADEDEGRPSNDCLLIYDIEGVGSPAGSVGCCSFIGEDLDESFLDTLGPKFKKLADISLGKEIDSYPDSDPSWPPQSTEPMCPQHTEPLGSGHPPISPHFGTTTVISENAYHSGPGVQHPVPIPDPLGYGNVTVRESYTTSGTLKPSVHFHDNQQASNVVVTERVVGPISGADLHGMLEIPDLRGGANVIVTERVIAPGSSLPTSLTIPNPQETSNVVVTERVIQPTSGMIGNLSMTPELSSAHNVIVTERVVSGAGMSEIAGTAGLGGVGGIGSSGLVSTTMGASGTGLNMGGTATIGHMRSSSDHHFSQTVGSASPSMARSRITKYNTVQYSK
Protein: NSFL1 cofactor p47 (XY body-associated protein XY40) (p97 cofactor p47) (O35987)
Organism: Rattus norvegicus (Rat)
Function: Reduces the ATPase activity of VCP. Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis. May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). Inhibits the activity of CTSL (in vitro) (By similarity). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (By similarity). Also, regulates spindle orientation during mitosis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12810701}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:12810701, ECO:0000269|PubMed:9214505}. Chromosome {ECO:0000269|PubMed:1495983}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23649807}. Note=Predominantly nuclear in interphase cells (PubMed:12810701). Bound to the axial elements of sex chromosomes in pachytene spermatocytes (PubMed:1495983). A small proportion of the protein is cytoplasmic, associated with Golgi stacks (PubMed:12810701). Localizes to centrosome during mitotic prophase and metaphase (PubMed:23649807). {ECO:0000269|PubMed:12810701, ECO:0000269|PubMed:1495983, ECO:0000269|PubMed:23649807}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- UBX domain-containing protein 2A
- Nuclear protein localization protein 4 homolog
- Ubiquitin recognition factor in ER-associated degradation protein 1
- UBX domain-containing protein 6
- Deubiquitinating protein VCPIP1
- ASPSCR1 tether for SLC2A4, UBX domain containing
- FAS-associated factor 1
- UBX domain-containing protein 10
- UBX domain protein 8
Sequence:
MAEERQDALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEEEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGERRRHSGQDVHVVLKLWKTGFSLDNGDLRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLNTSSPAQQAENEAKASSSILINEAEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFVLMTTFPNKELADENQTLKEANLLNAVIVQRLT
Protein: L-tyrosine decarboxylase (TDC) (TyrDC) (EC 4.1.1.25) (Levodopa decarboxylase) (L-dopa decarboxylase) (EC 4.1.1.-) (P0DTQ4)
Organism: Enterococcus faecalis (strain EnGen0310 / MMH594)
Function: Catalyzes the decarboxylation of L-tyrosine to produce tyramine. Plays a role in acid resistance since tyramine production via tyrosine decarboxylation appears to provide a cytosolic pH maintenance mechanism that helps the bacterium cope with acid stress such as that encountered in gastrointestinal tract (GIT) environments. Therefore, may contribute to the colonization of the human GIT by E.faecalis (By similarity).
Interaction partners:
Sequence:
MKNEKLAKGEMNLNALFIGDKAENGQLYKDLLIDLVDEHLGWRQNYMPQDMPVISSQERTSESYEKTVNHMKDVLNEISSRMRTHSVPWHTAGRYWGHMNSETLMPSLLAYNFAMLWNGNNVAYESSPATSQMEEEVGHEFAHLMSYKNGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVKPELVAGKSDWELLNMPTKEIMDLLESAEDEIDEIKAHSARSGKHLQAIGKWLVPQTKHYSWLKAADIIGIGLDQVIPVPVDHNYRMDINELEKIVRGLAEEQIPVLGVVGVVGSTEEGAVDSIDKIIALRDELMKDGIYYYVHVDAAYGGYGRAIFLDEDNNFIPYEDLQDVHEEYGVFKEKKEHISREVYDAYKAIELAESVTIDPHKMGYIPYSAGGIVIQDIRMRDVISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHVLPLNVAGYGKLIGASIEGSHHFYNFLNDLTFKVGDKEIEVHTLTHPDFNMVDYVFKEKGNDDLVAMNKLNHDVYDYASYVKGNIYNNEFITSHTDFAIPDYGNSPLKFVNSLGFSDEEWNRAGKVTVLRAAVMTPYMNDKEEFDVYAPKIQAALQEKLEQIYDVK
Protein: Regulator of G-protein signaling 5 (B1APM2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MCARNISQDILILQMHSAHWHINGKYEEKSNLMFWAKEIKIKLGILLQKPDSVGDLVIPYNEKPEKPAKTQKTSLDEALQWRDSLDKLLQNNYGLASFKSFLKSEFSEENLEFWIACEDYKKIKSPAKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSLSSFDMAQKRIHALMEKDSLPRFVRSEFYQELIK
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (Q57U53)
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:
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
- Phosphodiesterase
- Phosphodiesterase
Sequence:
MASFMRLVTPLGAAVACSHLLMVVLPLLLLIPGLCADKDCNSSSVTVRVYNLLYGSDVSKAIYEPVIAGFNASLHAHNDDLPANVCIEVEHVHARSDEDYVSYLKNKIDGDAAVQNKSELPIVLGPFGDWETRNISSELEELKVVAFSPFTGSSDVRVWKKNLYFLTASPIAQVLALIRYAVSQLRLQRLGFMYLKGVFYGDKEYKLTLKVMSIMGRKLCGVFELDSSTDGRASDDDFEAAWKRFAPTMPQGVIVFGSPIEDTKRFLLKFLGSNELRGAYILIPSMLQYVIKNSWMKKLAVKNFVPERVILTGLTPLANDNEYIAVRKFQTDMEKYLETNGKLNGHNYEKGHFYQHSTDGELMVHGWITGEVLWRTLGSRELLCNRTAYMNSLYNQRRYVIDDLVIGDFGGECEGKAGQRGAACKCNQGGNVVYMKRMGTDRNLHPVKEGVVTLASSRCYTNLLQLYAPLNGIMFRLEDNPLAQRITEEYRDGASLVVGKGQLGQGDRFFLHELNSTSSATKHNMLEEVKERVVTAVFGVVDDALLSMTDMTFIDPIPLSPRLKHPGRNVLHLSPTIEQQIFVMVERVVVPNSWGSVHAIVRSSDARGIKSVLRKTFWALGGSLGAFDEVTDGESVKSLLPHSGFVLVIGLTEADITAIAEHLDNHREVRVFVLFFDVALLYSEFVKVFKKHPQAAERLLFATSLPHWADNNTTSETVQEFHRDVGNESKWTPLALLGYATARAMESVVLQMGRVNSEELINTIFSQSVIVADDMWYGPFEDSCSNSRWSSAKDCIVNYGATHISVWSMARVLNPSVPPVSGVATPSIRYYKDGLNMTEEEFIGTIVGTILCLIALVLIVMLMRKCMRGDTRDNENAPKELTDPVTLIFTDIESSTAQWAAHPELMPDAVATHHRLIRTLISKYGCYEVKTVGDSFMIACKSPFAATQLACDLQRCFLEHDWKTDVFDTSYREFERQRAEDDGDYVPPTGHLDPDVYSRLWNGLRVRVGIHTGLCDIRHDEVTKGYDFYGRTSNMAARAESIANGGQVLLTRSTYLSLSTSEREQLNVTALGDVPLRGVPKPVEMYQLNAVPGRTFTTLRLDRRIIDEDTSVSCSDGSSIGAVLSDAAYQVVACVEALLGAFPTAQRKKLLMPFCNRWGVSAPRNVSDTWDATTCRNVTRLLAAKVGRVVDFGTKNTHDSVQSFDRRSSTSRPLLNAVSEECSLASTSSCIQSSCSVVYMMNGSDDDTSKCSPKHCNMCPLLPE
Protein: small monomeric GTPase (EC 3.6.5.2) (Q6PBX2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00037843}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037843}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004656}.
Interaction partners:
- Protein SEC13 homolog
- Protein transport protein Sec31A
- Prolactin regulatory element-binding
- Protein transport protein Sec23A
- Protein transport protein Sec31A
- Protein transport protein SEC23
- Protein transport protein Sec24A isoform X2
- Protein transport protein Sec24D
- Protein transport protein Sec24C
- SEC16 homolog B, endoplasmic reticulum export factor.
Sequence:
MSFIFDWIYSGFSSVLQFLGLYKKSGKLVFLGLDNAGKTTLLHMLKDDRLGQHVPTLHPTSEELTIAGMTFTTFDLGGHAQARRVWKNYLPAINGIVFLVDCIDHGRLAESKTELDALMTDETIGNVPILILGNKIDKPEAISEEKLREIFGLYGQTTGKGNIPLKELNTRPLEVFMCSVLKRQGYGEGFRWLSQYID
Protein: YEATS domain-containing protein 4 (Glioma-amplified sequence 41 homolog) (Gas41) (Q9CR11)
Organism: Mus musculus (Mouse)
Function: Chromatin reader component of the NuA4 histone acetyltransferase (HAT) complex, a complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (By similarity). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac) (By similarity). Also able to recognize and bind crotonylated histone H3 (By similarity). May also recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ); additional evidences are however required to confirm this result in vivo (By similarity). Plays a key role in histone variant H2AZ1/H2A.Z deposition into specific chromatin regions: recognizes and binds H3K14ac and H3K27ac on the promoters of actively transcribed genes and recruits NuA4-related complex to deposit H2AZ1/H2A.Z (By similarity). H2AZ1/H2A.Z deposition is required for maintenance of embryonic stem cell.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376}.
Interaction partners:
- DNA methyltransferase 1-associated protein 1
- RuvB-like 1
- Vacuolar protein sorting-associated protein 72 homolog
- RuvB-like 2
- Inhibitor of growth protein 3
- MRG/MORF4L-binding protein
- Transformation/transcription domain-associated protein
- Mortality factor 4-like protein 1
- Chromatin modification-related protein MEAF6
- E1A-binding protein p400
Sequence:
MFKRMAEFGPDSGGRVKGVTIVKPIVYGNVARYFGKKREEDGHTHQWTVYVKPYRNEDMSAYVKKIQFKLHESYGNPLRVVTKPPYEITETGWGEFEIIIKIFFIDPNERPVTLYHLLKLFQSDTNAMLGKKTVVSEFYDEMIFQDPTAMMQQLLTTSRQLTLGAYKHETEFAELEVKTREKLEAAKKKTSFEIAELKERLKASRETINCLKNEIRKLEEDDQTKDI
Protein: KH-type splicing regulatory protein (M0R0I5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPESKKLASQGDSISSQLGPIHPPPRTSMTEEYRVPDGMVGLNSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQ
Protein: POU domain protein (B5ME60)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MVHSSMGAPEIRMSKPLEAEKQGLDSPSEHTDTERNGPDTNHQNPQNKTSPFSVSPTGPSTKIKAEDPSGDSAPAAPLPPQPAQPHLPQAQLMLTGSQLAGDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQPPKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPASYSPHMVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLSGLNPSTGSTMVGLSSGLSPALMSNNPLATIQALASGGTLPLTSLDGSGNLVLGAAGAAPGSPGLVTSPLFLNHAGLPLLSTPPGVGLVSAAAAAVAASISSKSPGLSSSSSSSSSSSSSTCSETAAQTPGGPGGPEAGSKPE
Protein: Rho GTPase activating protein 45 (K7ES92)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGVGRKGGAGETESHPRIGLELASWLPHPQQEAESNLRKAKQGYVQRCEDHDKARFLVAKAEEEQAGSAPGAGSTATKTLDKRRRLEEEAKNKAEEAMATYRTCVADAKTQKQELEDTKVTALRQIQEVIRQSDQTIKSATISYYQMMHMQTAPLPVHFQMLCESSKLYDPGQQYASHVRQLQRDQEPDVHYDFEPHVSANAWSPVMRARKSSFNVSDVARPEAAGSPPEEGGCTEGTPAKDHRAGRGHQVHKSWPLSISDSDSGLDPGPGAGDFKKFERTSSSGTMSSTEELVDPDGGAGASAFEQADLNGMTPELPVAVPSGPFRHEGLSKAARTHRLRKLRTPAKCRECNSYVYFQGAECEECCLACHKKCLETLAIQCGHKKLQGRLQLFGQDFSHAARSAPDGVPFIVKKCVCEIERRALRTKGIYRVNGVKTRVEKLCQAFENGKELVELSQASPHDISNVLKLYLRQLPEPLISFRLYHELVGLAKDSLKAEAEAKAASRGRQDGSESEAVAVALAGRLRELLRDLPPENRASLQYLLRHLRRIVEVEQDNKMTPGNLGIVFGPTLLRPRPTEATVSLSSLVDYPHQARVIETLIVHYGLVFEEEPEETPGGQDESSNQRAEVVVQVPYLEAGEAVVYPLQEAAADGCRESRVVSNDSDSDLEEASELLSSSEASALGHLSFLEQQQSEASLEVASGSHSGSEEQLEATAREDGDGDEDGPAQQLSGFNTNQSNNVLQAPLPPMRLRGGRMTLGSCRERQPEFV
Protein: GH06241p (Q95U55)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMRNLMLRLGYNKFFIQGGDWGSIIGSNIATLYPENVLGYHSNMCNNLSPKSLAKGLVAEFWPSLFVPSGFEDFFFPKSNEMRYLMEESGYFHIQATKPDTIGAALTDNPVGLAAYILEKFSTWTNPSYRSLPDGRLTKRYKMDALLDNLMIYYLTNSITTSQRLYAEQYAQAQRDLHLDRVPTRVPTGCARFKSDIMQFLDVQLKDKYTNLVHSTYHKKGGHFAALEVPKVLYKDFIDFVETVERKFKIKTL
Protein: BAR/IMD domain containing adaptor protein 2 (cDNA FLJ55181, highly similar to Brain-specific angiogenesis inhibitor1-associated protein 2) (B4DWA1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLPEGQRQRALGFGTVTSTYSPVGQYIDAISNKQGELENYVSDGYKTALTEERRRFCFLVEKQCAVAKNSAAYHSKGKELLAQKLPLWQQACADPSKIPERAVQLMQQVASNGATLPSALSASKSNLVISDPIPGAKPLPVPPELAPFVGRMSAQESTPIMNGVTGPDGEDYSPWADRKAAQPKSLSPPQSQSKLSDSYSNTLPVRKSVTPKNSYATTENKTLPRSSSMAAGLERNGRMRVKAIFSHAAGDNSTLLSFKEGDLITLLVPEARDGWHYGESEKTKMRGWFPFSYTRVLDSDGSDRLHMSLQQGKSSSTGNLLDKDDLAIPPPDYGAASRAFPAQTASGFKQRPYSVAVPAFSQGLDDYGARSMSR
Protein: Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain] (Q8K3U6)
Organism: Rattus norvegicus (Rat)
Function: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Tissue factor
- Tissue factor pathway inhibitor
- GDP-fucose protein O-fucosyltransferase 1
- Coagulation factor X
- Prothrombin
- Coagulation factor IX
- Thrombomodulin
- Vitamin K-dependent gamma-carboxylase
- Antithrombin-III
- Coagulation factor XI
Sequence:
MVPQTHGLLLLYFLLQLQGPLGAVVFITQEEAHGVLHRQRRANSLLEELWSSSLERECNEERCSFEEAREIFKSPERTKQFWTIYSDGDQCASNPCQNGGTCQDHLKSYVCFCPLDFEGRNCEKNKNEQLICANENGDCDQYCRDHVGTKRTCSCHEDYVLQPDEVSCKPKVEYPCGRIPVVEKRNFSRPQGRIVGGYVCPKGECPWQAVLKFNEALLCGAVLLDTRWIVTAAHCFDKFGKLVNITVVLGEHDFSEKEGTEQVRLVEQVIMPNKYTRGRTDHDIALVRLHRPVTFTDYVVPLCLPERAFSENTLASIRFSRVSGWGQLLDRGATALELMVIEVPRLMTQDCLEHAKHSANTPRITENMFCAGYMDGTKDACKGDSGGPHATHYHGTWYLTGVVSWGEGCAAIGHIGVYTRVSQYIDWLVKYMDSKLRVGISRVSLL
Protein: Putative glutamine-dependent NAD(+) synthetase (EC 6.3.5.1) (NAD(+) synthase [glutamine-hydrolyzing]) (O74940)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- NAD-capped RNA hydrolase
- Nicotinamide riboside kinase
- NAD-dependent histone deacetylase sir2
- NAD-dependent protein deacetylase hst4
- NAD-dependent protein deacetylase hst2
- IMP-specific 5'-nucleotidase 1
- Uncharacterized kinase C24B10.02c
- Uncharacterized kinase C3H5.11
- Putative nicotinamide mononucleotide adenylyltransferase
Sequence:
MERYVTIASCQLNQWAMDFEGNRLRIIDSIKEAKRQNASLRVGPELEVTGYGCEDHFLESDTYYHSWEMLCSIIHDPDCQDILLDIGMPVMHKAMRHNCRILALNGKILLIRPKIWLCDDGNFRESRWFTPWLRPRVVETHYLPTFVAKSLNQTTVPIGDAILQCNETVVGVETCEELFTPNSPHIDMALDGVEIFINASGSHHELRKLTTRVNLIQNATEKCGGIYLYSNQRGCDGGRLYYDGSSMIFANGKMLAQGHQFSLKDVEVISATVDVDTVRSYRFQPSHGIQGVTRPSYERIHVNFSLSSYQQDYDIYRKPTDPIEVTIPLPEEEITFGPACWLWDYLRRSHAAGFFLPLSGGLDSCSTAVLVYSMCRIVCKAMEEDDAQVLSDVRRIVGDPSYSSTDPKKLLNHLFYTAFMGSEHSSKETRSRAKELSSLIGSYHTDVNIDTMTSAVVKLFALVTGKTPQFRSNGGTNAENLALQNIQARSRMLLGYLFAQLLPWVRGYSGSLLVLGSSNVDECLRGYLTKYDCSSADINPIGGISKTDLKSFLRYAKEALDLPILQEFLDATPTAELEPTTESYVQSDEADMGMTYAELSVFGRLRKISKCGPYSMFTQLMHQWGDRLSPSQVAEKVKRFFHYYGINRHKMTTLTPSYHAETYGVDDNRYDLRQFLYPSWTWQNKKIDALASKFEQHQRK