wanglab/gogpt-training-data huggingface dataset:
Protein: Dynein light intermediate chain (Q1LUM9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU366047}.
Interaction partners:
- Dynein, cytoplasmic 1, heavy chain 1.
- Cytoplasmic dynein 1 intermediate chain 1
- Dynein, cytoplasmic 1, intermediate chain 2a-like isoform X2
- Dynein cytoplasmic 2 heavy chain 1.
- WD_REPEATS_REGION domain-containing protein.
- Dynein, cytoplasmic 1, intermediate chain 2a
- Dynein light chain roadblock
- Dynein light intermediate chain
- Dynactin subunit 2
- Dynein light chain Tctex-type 1
Sequence:
MATTGRNTLLSVSTNVNNSTSESQNPEEEDGQNLWSSILSEVSTRSRSKLPSGKNVVVMGEVGSGKTTLVAKLQGVEEYMKGRGLEYLYFNVHDDDIDDQSRCNAWVLDGDLYHKGLQKFAISLENLEDSLILFVVDLSRPWLALDSLQKWGSVVRDFVDKLRVPPETMRELEHRLTKQFQEYVEPGSDLDAVPQRRNPESDEESVLLPLGENTLTHNLGLPIVVVCTKCDAISTLEKEHDYKDEHLDFIQSHIRRFCLQYGAALLYTSMKENKNLDLLYKYLVHRLYGFPFNSPAQVVEKDSVFIPSGWDNEKKIAILHENFQMVKAEDSFEDVIVKPPVRKFVHEKEVQAEDDQVFLVKLQSLLSKQPPVTAGRPVDPTNRAPTGSPRTTNRSAAANVANVMPMQSGTKKIDPNMKGGQTSEGVLANFFNSLLTKKAGSPGPGGQPAGGGSNTPGTVRKSGSKLGLTDVQAELDRISNKSDLDSSAPNATTPPAENDKS
Protein: Pleckstrin homology domain-containing family G member 3 (PH domain-containing family G member 3) (A1L390)
Organism: Homo sapiens (Human)
Function: Plays a role in controlling cell polarity and cell motility by selectively binding newly polymerized actin and activating RAC1 and CDC42 to enhance local actin polymerization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27555588}. Note=Colocalizes with actin at the leading edge of polarized cells. {ECO:0000269|PubMed:27555588}.
Interaction partners:
- Cell division control protein 42 homolog
Sequence:
MPVSTSLHQDGSQERPVSLTSTTSSSGSSCDSRSAMEEPSSSEAPAKNGAGSLRSRHLPNSNNNSSSWLNVKGPLSPFNSRAAAGPAHHKLSYLGRVVREIVETERMYVQDLRSIVEDYLLKIIDTPGLLKPEQVSALFGNIENIYALNSQLLRDLDSCNSDPVAVASCFVERSQEFDIYTQYCNNYPNSVAALTECMRDKQQAKFFRDRQELLQHSLPLGSYLLKPVQRILKYHLLLQEIAKHFDEEEDGFEVVEDAIDTMTCVAWYINDMKRRHEHAVRLQEIQSLLINWKGPDLTTYGELVLEGTFRVHRVRNERTFFLFDKTLLITKKRGDHFVYKGNIPCSSLMLIESTRDSLCFTVTHYKHSKQQYSIQAKTVEEKRNWTHHIKRLILENHHATIPQKAKEAILEMDSYYPNRYRCSPERLKKAWSSQDEVSTNVRQGRRQSEPTKHLLRQLNEKARAAGMKGKGRRESESSRSSRRPSGRSPTSTEKRMSFESISSLPEVEPDPEAGSEQEVFSAVEGPSAEETPSDTESPEVLETQLDAHQGLLGMDPPGDMVDFVAAESTEDLKALSSEEEEEMGGAAQEPESLLPPSVLDQASVIAERFVSSFSRRSSVAQEDSKSSGFGSPRLVSRSSSVLSLEGSEKGLARHGSATDSLSCQLSPEVDISVGVATEDSPSVNGMEPPSPGCPVEPDRSSCKKKESALSTRDRLLLDKIKSYYENAEHHDAGFSVRRRESLSYIPKGLVRNSISRFNSLPRPDPEPVPPVGSKRQVGSRPTSWALFELPGPSQAVKGDPPPISDAEFRPSSEIVKIWEGMESSGGSPGKGPGQGQANGFDLHEPLFILEEHELGAITEESATASPESSSPTEGRSPAHLARELKELVKELSSSTQGELVAPLHPRIVQLSHVMDSHVSERVKNKVYQLARQYSLRIKSNKPVMARPPLQWEKVAPERDGKSPTVPCLQEEAGEPLGGKGKRKPVLSLFDYEQLMAQEHSPPKPSSAGEMSPQRFFFNPSAVSQRTTSPGGRPSARSPLSPTETFSWPDVRELCSKYASRDEARRAGGGRPRGPPVNRSHSVPENMVEPPLSGRVGRCRSLSTKRGRGGGEAAQSPGPLPQSKPDGGETLYVTADLTLEDNRRVIVMEKGPLPSPTAGLEESSGQGPSSPVALLGQVQDFQQSAECQPKEEGSRDPADPSQQGRVRNLREKFQALNSVG
Protein: Pheromone-processing carboxypeptidase KEX1 (EC 3.4.16.6) (Carboxypeptidase D) (Q5AFP8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Kexin
- Ste13p
- Pro-apoptotic serine protease NMA111
Sequence:
MKLILSTLIVFIHTLLVSALPTKEGSDPNSAKKYLVSDLPGLHENITPDNSIPLMFAGQLEIYPETDTHYFFWKFSDSNPETVTNRTIFWLNGGPGCSSMDGALLETGPFRINSQQQVISNNGSWHKMGDIIYVDQPAGTGFSYSDTYITDLDQVAEYFLKFMEKYYELFPEEIGYEIYFAGESYAGQYIPYIADAILQRNKKLVDGEHKYDLRGVLIGNGWVSPNEQSLSYLPFFKDHGLIDVHHPKWATLLAKHEQCQKIVNKIDSTFDDGVVHYYEVSSSTCEAILTDLLEYTQDTASEKDQRCVNMYDYTLRDSYPSCGMNWPYELVNVGPFLRQEKVMHQLNLINLKKWNECNGRVGRTFQARHSIPAVHLLPELAKEIPVMLFNGANDIICNSQGVLSYLQKLQWNGETGFTNKDNQISWIYDNKEVGYIIWERNISFINIYNSSHMVPYDLPDVSRALIDLITGKYDEKDVDGKKSFVTYPLGSRKESDASADGEENAGSDKVPGDSPSQTIDPMISSSTASSSSVESSLSSSTASADSDSTSSKFTRLIQLAVILVIFWGVYVLYASYKSRPSSIIKKPTNNTSNVTRSSAGKKKNVQWADQLNQFEDDERTQEPNQGIIAKAIGKITGSKDTRGRYAPVQRGNGNEYIDDIELGEGLSDPNVDEFIIGSDDDEEQGQAHSGAATHNQKQKPMN
Protein: Cytosolic carboxypeptidase-like protein 5 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein-like 5) (Protein deglutamylase CCP5) (Q8NDL9)
Organism: Homo sapiens (Human)
Function: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000269|PubMed:23085998}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:23085998}. Midbody {ECO:0000269|PubMed:23085998}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed (By similarity). Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis. {ECO:0000250|UniProtKB:Q09M02, ECO:0000269|PubMed:23085998}.
Interaction partners:
- Tubulin polyglutamylase TTLL6
Sequence:
MELRCGGLLFSSRFDSGNLAHVEKVESLSSDGEGVGGGASALTSGIASSPDYEFNVWTRPDCAETEFENGNRSWFYFSVRGGMPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPTRPRWERIRDRPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQELLNQLDQRFPENHPTHSSPLDTIYYHRELLCYSLDGLRVDLLTITSCHGLREDREPRLEQLFPDTSTPRPFRFAGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAVLHPAIYGAKAVLLYHHVHSRLNSQSSSEHQPSSCLPPDAPVSDLEKANNLQNEAQCGHSADRHNAEAWKQTEPAEQKLNSVWIMPQQSAGLEESAPDTIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPAFPSRYTVELFEQVGRAMAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRNSRGLSSTLNVGVNKKRGLRTPPKSHNGLPVSCSENTLSRARSFSTGTSAGGSSSSQQNSPQMKNSPSFPFHGSRPAGLPGLGSSTQKVTHRVLGPVREPRSQDRRRQQQPLNHRPAGSLAPSPAPTSSGPASSHKLGSCLLPDSFNIPGSSCSLLSSGDKPEAVMVIGKGLLGTGARMPCIKTRLQARPRLGRGSPPTRRGMKGSSGPTSPTPRTRESSELELGSCSATPGLPQARPPRPRSAPAFSPISCSLSDSPSWNCYSRGPLGQPEVCFVPKSPPLTVSPRV
Protein: ATPase SWSAP1 (SWIM-type zinc finger 7-associated protein 1) (SWS1-associated protein 1) (ZSWIM7-associated protein 1) (ZSWIM7AP1) (Q6NVH7)
Organism: Homo sapiens (Human)
Function: ATPase which is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). Has a DNA-binding activity which is independent of its ATPase activity.
Subcellular location: Nucleus {ECO:0000305|PubMed:21965664}.
Interaction partners:
- Zinc finger SWIM domain-containing protein 7
- DNA mismatch repair protein Msh2
- DNA mismatch repair protein Msh6
- Serine-protein kinase ATM
- DNA repair endonuclease XPF
- X-ray repair cross-complementing protein 6
- Protein PAXX
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- REST corepressor 1
- DNA-dependent protein kinase catalytic subunit
Sequence:
MPAAGPPLLLLGTPGSGKTALLFAAALEAAGEGQGPVLFLTRRPLQSMPRGTGTTLDPMRLQKIRFQYPPSTRELFRLLCSAHEAPGPAPSLLLLDGLEEYLAEDPEPQEAAYLIALLLDTAAHFSHRLGPGRDCGLMVALQTQEEAGSGDVLHLALLQRYFPAQCWLQPDAPGPGEHGLRACLEPGGLGPRTEWWVTFRSDGEMMIAPWPTQAGDPSSGKGSSSGGQP
Protein: Proteasome subunit beta type-4 (Q556Q0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-5
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-2
- Proteasome subunit beta type-6
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-7
- Proteasome subunit beta type-1
Sequence:
MSHEHVNFPVYGQVDYFKQQQPQQPQYNPHLGGKQKTLDPIVTGTSVIAIKYDKGVVMGSDMLLSYGSLARFNSTERMKKFGGYTIVGASGEYSDFQSITNTLNDLVTDDHCMDDGSKLSSEEIWNYLARVLYNQRNRGNPLWNTLVVMGYQGGKSFLGKVDLVGTCYKDDIITTGYGSHIALPLLRKARDENPNMNLEQAKQLIQDCLRVLFYRDARSSKKIQISVAGEEGIEISGPIELDTFHWNSGEAAVKNFSQV
Protein: Translocation and assembly module subunit TamB (Autotransporter assembly factor TamB) (P39321)
Organism: Escherichia coli (strain K12)
Function: Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. In reconstituted TAM this subunit (Ag43, AC P39180) is not necessary for substrate penetration in the outer membrane. Substrate binding to TamA moves its POTRA domains about 30 Angstroms into the periplasm, which would deform either the outer membrane or TamB and may provide force to reset TAM.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:22466966}; Single-pass membrane protein {ECO:0000305|PubMed:22466966}.
Interaction partners:
- Translocation and assembly module subunit TamA
- Gamma-glutamylcyclotransferase family protein YtfP
- Outer membrane protein assembly factor BamA
- AsmA family protein YicH
- Outer membrane protein assembly factor BamB
- AsmA family protein YhjG
- Probable phospholipid transport protein YdbH
- Chromosome partition protein MukB
- LPS-assembly protein LptD
- Outer membrane protein assembly factor BamC
Sequence:
MSLWKKISLGVVIVILLLLGSVAFLVGTTSGLHLVFKAADRWVPGLDIGKVTGGWRDLTLSDVRYEQPGVAVKAGNLHLAVGLECLWNSSVCINDLALKDIQVNIDSKKMPPSEQVEEEEDSGPLDLSTPYPITLTRVALDNVNIKIDDTTVSVMDFTSGLNWQEKTLTLKPTSLKGLLIALPKVAEVAQEEVVEPKIENPQPDEKPLGETLKDLFSRPVLPEMTDVHLPLNLNIEEFKGEQLRVTGDTDITVSTMLLKVSSIDGNTKLDALDIDSSQGIVNASGTAQLSDNWPVDITLNSTLNVEPLKGEKVKLKMGGALREQLEIGVNLSGPVDMDLRAQTRLAEAGLPLNVEVNSKQLYWPFTGEKQYQADDLKLKLTGKMTDYTLSMRTAVKGQEIPPATITLDAKGNEQQVNLDKLTVAALEGKTELKALLDWQQAISWRGELTLNGINTAKEFPDWPSKLNGLIKTRGSLYGGTWQMDVPELKLTGNVKQNKVNVDGTLKGNSYMQWMIPGLHLELGPNSAEVKGELGVKDLNLDATINAPGLDNALPGLGGTAKGLVKVRGTVEAPQLLADITARGLRWQELSVAQVRVEGDIKSTDQIAGKLDVRVEQISQPDVNINLVTLNAKGSEKQHELQLRIQGEPVSGQLNLAGSFDRKEERWKGTLSNTRFQTPVGPWSLTRDIALDYRNKEQKISIGPHCWLNPNAELCVPQTIDAGAEGRAVVNLNRFDLAMLKPFMPETTQASGIFTGKADVAWDTTKEGLPQGSITLSGRNVQVTQTVNDAALPVAFQTLNLTAELRNNRAELGWTIRLTNNGQFDGQVQVTDPQGRRNLGGNVNIRNFNLAMINPIFTRGEKAAGMVSANLRLGGDVQSPQLFGQLQVTGVDIDGNFMPFDMQPSQLAVNFNGMRSTLAGTVRTQQGEIYLNGDADWSQIENWRARVTAKGSKVRITVPPMVRMDVSPDVVFEATPNLFTLDGRVDVPWARIVVHDLPESAVGVSSDVVMLNDNLQPEEPKTASIPINSNLIVHVGNNVRIDAFGLKARLTGDLNVVQDKQGLGLNGQINIPEGRFHAYGQDLIVRKGELLFSGPPDQPYLNIEAIRNPDATEDDVIAGVRVTGLADEPKAEIFSDPAMSQQAALSYLLRGQGLESDQSDSAAMTSMLIGLGVAQSGQIVGKIGETFGVSNLALDTQGVGDSSQVVVSGYVLPGLQVKYGVGIFDSIATLTLRYRLMPKLYLEAVSGVDQALDLLYQFEF
Protein: holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) (Q54MI2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Malonyl-CoA:ACP transacylase
- Malonyl-CoA:ACP transacylase
- Malonyl-CoA:ACP transacylase
- 4'-phosphopantetheinyl transferase domain-containing protein
- Dephospho-CoA kinase
- Probable polyketide synthase 16
- Probable polyketide synthase 2
- [acyl-carrier-protein] S-malonyltransferase
- Acyl carrier protein, mitochondrial
- beta-ketoacyl-[acyl-carrier-protein] synthase I
Sequence:
MNQNEKELVNILLLGFDISKWKPNDIEWKEINDFINDPIESNRISNFKRPNKDGSWLIGKDNDSAKSSIIGRRLMIELVNKMLSLDYNSIKFKRTQSNKPYLSTTTTISNKFSFNISHDSNWVIGIGSLISDSIGIDIMDCKIPRNQKMSEFFDTMSSCFTDNEWKIINQGKDDQSKIDLFFIHWCLKESYIKADGKGLNIELKSFEFIIDQTNQTAQIFILNDKKNKSILNNYQFTYFKPFKNDKDNNNNSFVIAICLDLTNHNHNNNNNNALTNNIITKDNLSIQILESDFKIK
Protein: Importin subunit alpha-7 (Karyopherin subunit alpha-6) (O60684)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Interaction partners:
- Importin subunit beta-1
- Importin subunit alpha-5
- Regulator of chromosome condensation
- Nuclear pore complex protein Nup50
- GTP-binding nuclear protein Ran
- mRNA cap guanine-N
- Nuclear cap-binding protein subunit 2
- Importin subunit alpha-4
- Nuclear pore complex protein Nup153
- Interleukin-1 family member 10
Sequence:
METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPRVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSVCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGNIVTGDDIQTQVILNCSALPCLLHLLSSPKESIRKEACWTISNITAGNRAQIQAVIDANIFPVLIEILQKAEFRTRKEAAWAITNATSGGTPEQIRYLVSLGCIKPLCDLLTVMDSKIVQVALNGLENILRLGEQEGKRSGSGVNPYCGLIEEAYGLDKIEFLQSHENQEIYQKAFDLIEHYFGVEDDDSSLAPQVDETQQQFIFQQPEAPMEGFQL
Protein: Glycoprotein hormone receptor II (Q9NDI1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAARCRWSWRLALCPLLLQLLLQLLLLPPSAMGHDETKENPAPDMQNSQEQEPYVHLQHLQQQQQQNPQTVQQLSQITVNRTSKSASVTPTGIRENVMLPSADPEKEAQILYEKSLQEYHGSQLSTASTATDVIAGKRTLHSICERWLQKHCHCTGSLEVLRLSCRGIGILAVPVNLPNEVVVLDLGNNNLTKLEANSFFMAPNLEDLTLSDNSIINMDPNAFYGLAKLKRLSLQNCGLKSLPPQSFQGLAQLTSLQLNGNALVSLDGDCLGHLQKLRTLRLEGNLFYRIPTNALAGLRTLEALNLGSNLLTIINDEDFPRMPNLIVLLLKRNQIMKISAGALKNLTALKVLELDDNLISSLPEGLSKLSQLQELSITSNRLRWINDTELPRSMQMLDMRANPLSTISAGAFRGMSKLRKLILSDVRTLRSFPELEACHALEILKLDRAGIQEVPANLCRQTPRLKSLELKTNSLKRIPNLSSCRDLRLLDLSSNQIEKIQGKPFNGLKQLNDLLLSYNRIKALPQDAFQGIPKLQLLDLEGNEISYIHKEAFSGFTALEDLNLGNNIFPELPESGLRALLHLKTFNNPKLREFPPPDTFPRIQTLILSYAYHCCAFLPLVAMSSQKKTSQVQEAVLFPSDAEFDMTLWNNSMMNIWPQMHNLSKQLGASMHDPWETAINFNEEQLQTQTGGQIATSYMEEYFEEHDVSGPATGYGFGTGLFSGMSTEDFQPGSVQCLPMPGPFLPCADLFDWWTLRCGVWVVFLLSLLGNGTVVFVLLCSRSKMDVPRFLVCNLAAADFFMGIYLGILAIVDAATLGEFRMFAIPWQMSVLCQLSGFLAVLSSELSVYTLAVITLERNYAITHAIHLNKRLSLKQAGYIMSVGWVFALIMALMPLVGVSDYRKFAVCLPFETTTGPASLTYVISLMFINGCAFLTLMGCYLKMYWAIRGSQAWNTNDSRIAKRMALLVFTDFLCWSPIAFFSITAIFGLQLISLEQAKIFTVFVLPLNSCCNPFLYAIMTKQFKKDCVTLCKHFEESRVVGGGGPGGRGAVARTKRGDLPPPLLPAAAVAHPPGCRCLRMLPSEMPNWHKMEQTPSMWQRLRTFCCGENRRRRKQRRQPQQRRQRAYTAAAANPYQYQFAELRQQRQNRASSISSENFCSSRSSSWRHGPPSSAPVPPGNCSMPLKMLEPHAHPHGHGRRRHSAWLITRKTSQDSNLSSSRNDSSASATTASTSTFRLSRSSAGSSTPLPSIIAHNGKAQLDAVKPRLVRQEAVQEEEDSSPPRLGVRFLPTIPSAADSSVVMEDGDSANTGVASFLGMPLPGASSGFLIAPTTAATTSPPPVVLQPAKPPPDPNDAPL
Protein: Protein FAM170A (Zinc finger domain-containing protein) (Zinc finger protein ZNFD) (A1A519)
Organism: Homo sapiens (Human)
Function: Acts as a nuclear transcription factor that positively regulates the expression of heat shock genes. Binds to heat shock promoter elements (HSE).
Subcellular location: Nucleus {ECO:0000269|PubMed:20162441}.
Interaction partners:
- Zinc finger MYND domain-containing protein 19
- Tubulin alpha-4A chain
- Melanin-concentrating hormone receptor 1
Sequence:
MKRRQKRKHLENEESQETAEKGGGMSKSQEDALQPGSTRVAKGWSQGVGEVTSTSEYCSCVSSSRKLIHSGIQRIHRDSPQPQSPLAQVQERGETPPRSQHVSLSSYSSYKTCVSSLCVNKEERGMKIYYMQVQMNKGVAVSWETEETLESLEKQPRMEEVTLSEVVRVGTPPSDVSTRNLLSDSEPSGEEKEHEERTESDSLPGSPTVEDTPRAKTPDWLVTMENGFRCMACCRVFTTMEALQEHVQFGIREGFSCHVFHLTMAQLTGNMESESTQDEQEEENGNEKEEEEKPEAKEEEGQPTEEDLGLRRSWSQCPGCVFHSPKDRNS
Protein: Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (EC 1.2.1.13) (NADP-dependent glyceraldehydephosphate dehydrogenase subunit A) (P09315)
Organism: Zea mays (Maize)
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Phosphoglycerate kinase
- Phosphoglycerate kinase
- Phosphoglycerate kinase
- phosphoglycerate kinase
- transketolase
- transketolase
- Triosephosphate isomerase
- Triosephosphate isomerase, cytosolic
- Triosephosphate isomerase, cytosolic
- Triose phosphate isomerase5
Sequence:
MASSMLSATTVPLQQGGGLSEFSGLRSSASLPMRRNATSDDFMSAVSFRTHAVGTSGGPRRAPTEAKLKVAINGFGRIGRNFLRCWHGRGDASPLDVIAINDTGGVKQASHLLKYDSTLGIFDADVKPVGDNAISVDGKVIKVVSDRNPSNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADQYNPDEPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPNLKGKLNGIALRVPTPNVSVVDLVVQVSKKTLAEEVNQAFRDAAANELTGILEVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVISWYDNEWGYSQRVVDLADICANQWK
Protein: Splicing factor 1 (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162) (Q15637)
Organism: Homo sapiens (Human)
Function: Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor.
Subcellular location: Nucleus.
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Splicing factor 3A subunit 1
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 3
- Probable ATP-dependent RNA helicase DDX46
- Splicing factor U2AF 35 kDa subunit
- Cell division cycle 5-like protein
- Pre-mRNA-processing factor 40 homolog A
- Splicing factor 3B subunit 1
- Splicing factor 45
Sequence:
MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPANNPPPPSLMSTTQSRPPWMNSGPSESRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN
Protein: Glycoprotein IIIa (P97483)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MRAQWPGQLWAALLALGALAGVVVGESNICTARGVNSCQQCLAVSPVCAWCSDETLSQGSPRCNLKENLLKDNCAPESIEFPVSEAQILEARPLSSKGSGSSA
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC 2.4.1.15) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (Q96WK6)
Organism: Zygosaccharomyces rouxii
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
Interaction partners:
Sequence:
MTVSKKDSGKTSPGNIVVVSNRLPVTISKNAMGKYEYKFSSGGLVTALQGLKKTSTFQWYGWPSLEIPDDEKPVVKKDLLEKFNAIPIFLSDEIADLHYNGFSNSILWPLFHYHPGEINFDENAWLAYNEANATFASEICGNLQDNDLVWVHDYHLMLLPEMLSAHIQRKGLKNIKLGWFLHTPFPSSEIYRILPVRQEILNGVLSCDLIGFHTYDYARHFLSSIQRCLNVNTLPNGVEYQGRFVNVGAFPIGIDVDTFKEGLQKENVKQRIRTLQERFKGCKIMVGVDRLDYIKGVPQKLHAMEVFLNEHPEWIGKVVLVQLAIPSRGDVEEYQYLRSVVNELVGRINGQFGTIEFVPIHFMHKSIPFEELISLYAVSDACIVSSTRDGMNLVSYEYIACRKKGSLILSEFTGAAQSLNGALIVNPWNTDELSDSINEALTLPDEKKDSNWEKLYKYISKYTSAYWGENFVHELNATGTIKTGQ
Protein: Phosphotransferase (EC 2.7.1.-) (O93314)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MGQMGKMPCSLSSVLERVIMVEQILSEFRLKKEQLKEVMKRMMREMDRGLRVETHQEASVKMLPTYVCSTPEGSEVGDFLALDLGGTNFRVMLVKVGEDEERGWKVETKHQMYSISEDAMTGTAEMLFDYIAECISDFLNRQHIKHKKLPLGFTFSFPVRHENIDKGILLNWTKGFKASGAEGNNVVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRSCEVGMIVGTGCNACYMEEMRTVELVEGEEGRMCVNTEWGAFGANGELEEFRLEYDRVVDETSLNPGQQLYEKLISGKYMGELVRLVLLKLVNEELLFNGEASDLLKTRGSFETRYVSQIEGDSGDRKQIYNILSTLGVLPSELDCDIVRLACESVSTRAAHMCGAGLAGVINRMRERRSPAVLKITVGIDGSVYKLHPCFQDRFHKVVRELTPHCDITFIQSEEGSGRGAALISAVACKMAACMLTP
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (A0A8I5ZKC1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MALGKLFTGKSEPQAMCYIETSNLDGETNLKIRQGLPATSDIKDIDSLMRISGRIECESPNRHLYDFVGNIRLDGHGTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILILFCILIAMSLVCSVGSAIWNRRHSGKDWYLHLHYGGASNFGLNFLTFIILFNNLIPISLLVTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQFKKCTIAGVAYGQSSQFGDEKTFNDPSLLENLQNNHPTAPIICEFLTMMAVCHTAVPERDGEKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEERYELLNVLEFTSSRKRMSVVVRTPSGKLRLYCKGADTVIYERLAESSKYKEITLKHLEQFATEGLRTLCFAVAEISESDFEEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIEDKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCRLLRRNMGMIVINEGSLDGTRETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQKSEVVEMVKKQVKVITLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYLKNLLMVHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMFTAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPLKALQYGTVFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVVFFGIYSSLWPAVPMAPDMSGEAAMLFSSGVFWVGLLSIPVASLLLDVLYKVIKRTAFKTLVDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQDENGIVSQSEVIRAYDTTKQRPDEW
Protein: Amidase, putative (EC 3.5.1.-) (Q4WV20)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Nitrilase
- nitrilase
- Cytochrome P450 phenylacetate 2-hydroxylase, putative
- Glutamyl-tRNA
Sequence:
MTLLAVGQATHSPNCLPDSAVGTTWKMISAEYISKRKGNVCLIAAVLSTAAFGVVLAYISTAMLHLSKWFLAPFVYATTTASSPKSSPNGTAARQCVFPSLIEATTAELQEGLTKGCFSSVDLVNAYVTRINEVNSTLHMVLEVNPDAWDIARQLDLERKYGRVRGPLHGLPILVKGNIGTEDKTETAAGSYALVGAKVAADSTVAKKLRQAGVIILGKTSLSEWANFRSLNGSSGWNAQGGQTYAAYYPKQDPSGSSSGSGVAADLGLAFAALGTETNGSILSPSENSNIVGIKPTVGLTSRYMVIPISERQDTIGPMARTVKDAAIILQAIAGPDKNDNYTLASPFGSHLPNYVAACTLSGLKGKRIGIPRNVINTLDASSEPIVSAFEAAVSVISKAGATIVEDADFTGYDEYLNTSITQAVVAADFISDIASYLSKLKTNPNNLHNLEDIRRFTQQSPLEDYPSRDTGIWDLALASGINNTSPEFWPMHLRSLYYGEEGGLTGALSRHKLDAVILPTALAPDIPAIIGAPAITVPLGSFPAGTPIEYNKRGNLVEKAPGIPFGISFLGPKWSEESLIGMAYAFEQRTLVRKKLQRYIEPKSDLSMLL