wanglab/gogpt-training-data huggingface dataset:
Protein: Phytochrome D (P42497)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Interaction partners:
- Transcription factor PIF3
- Cryptochrome-2
- Cryptochrome-1
- E3 ubiquitin-protein ligase COP1
- Phototropin-1
- Phototropin-2
- Adagio protein 2
- Transcription factor PIF5
- Transcription factor PIF4
- Transcription factor HFR1
Sequence:
MVSGGGSKTSGGEAASSGHRRSRHTSAAEQAQSSANKALRSQNQQPQNHGGGTESTNKAIQQYTVDARLHAVFEQSGESGKSFDYSQSLKTAPYDSSVPEQQITAYLSRIQRGGYTQPFGCLIAVEESTFTIIGYSENAREMLGLMSQSVPSIEDKSEVLTIGTDLRSLFKSSSYLLLERAFVAREITLLNPIWIHSNNTGKPFYAILHRVDVGILIDLEPARTEDPALSIAGAVQSQKLAVRAISHLQSLPSGDIKLLCDTVVESVRDLTGYDRVMVYKFHEDEHGEVVAESKRNDLEPYIGLHYPATDIPQASRFLFKQNRVRMIVDCYASPVRVVQDDRLTQFICLVGSTLRAPHGCHAQYMTNMGSIASLAMAVIINGNEEDGNGVNTGGRNSMRLWGLVVCHHTSARCIPFPLRYACEFLMQAFGLQLNMELQLALQVSEKRVLRMQTLLCDMLLRDSPAGIVTQRPSIMDLVKCNGAAFLYQGKYYPLGVTPTDSQINDIVEWLVANHSDSTGLSTDSLGDAGYPRAAALGDAVCGMAVACITKRDFLFWFRSHTEKEIKWGGAKHHPEDKDDGQRMNPRSSFQTFLEVVKSRCQPWETAEMDAIHSLQLILRDSFKESEAMDSKAAAAGAVQPHGDDMVQQGMQEIGAVAREMVRLIETATVPIFAVDIDGCINGWNAKIAELTGLSVEDAMGKSLVRELIYKEYKETVDRLLSCALKGDEGKNVEVKLKTFGSELQGKAMFVVVNACSSKDYLNNIVGVCFVGQDVTGHKIVMDKFINIQGDYKAIIHSPNPLIPPIFAADENTCCLEWNTAMEKLTGWPRSEVIGKLLVREVFGSYCRLKGPDALTKFMIVLHNAIGGQDTDKFPFPFFDRKGEFIQALLTLNKRVSIDGKIIGAFCFLQIPSPELQQALEVQRRQESEYFSRRKELAYIFQVIKNPLSGLRFTNSLLEDMDLNEDQKQLLETSVSCEKQISKIVGDMDVKSIDDGSFLLERTEFFIGNVTNAVVSQVMLVVRERNLQLIRNIPTEVKSMAVYGDQIRLQQVLAEFLLSIVRYAPMEGSVELHLCPTLNQMADGFSAVRLEFRMACAGEGVPPEKVQDMFHSSRWTSPEGLGLSVCRKILKLMNGGVQYIREFERSYFLIVIELPVPLMMMMPSS
Protein: glutamate synthase (NADH) (EC 1.4.1.14) (C8VEZ6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- NADP-specific glutamate dehydrogenase
- NAD-specific glutamate dehydrogenase
- Chitin binding domain protein Peritrophin-A, putative
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Glutamine synthetase
- Multifunctional protein pyrABCN
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
- Glutamine synthetase
- Isocitrate dehydrogenase
- Amidophosphoribosyltransferase
Sequence:
MGLNLEEIYGQTIVEEQRPNEYSEYQPKKGYGWANTLPERQGLYDPEYEKDACGVGFAANIKGKASHKIVSDARNLLCNMTHRGAVGSDARDGDGAGVMTSIPHKFFIKNFAREVGVDLPPLGQYAVGNLFFKPDEEALKESIKQFEEIATSLGLRVLGWREVPRDSTILGPAALSREPTILQPFVVLKSAYGEGNKPDITDPEQFDTKTFELQLYVLRKRATHIIGLANWFYLCSLSNRNIVYKGQLAPIQVYQYYHDLVNVDYEGHFALVHSRFSTNTFPSWDRAQPLRWAAHNGEINTLRGNKNWMRAREGLLKSDIFGEELESLLPIVEDGGSDSAAFDNVLELLMINGVLSLPEAVMIMIPEAWQDNPAMDPAKAAFYEWAACQMEPWDGPALFTFSDGRYCGANLDRNGLRPCRFYVTDDDRIICASEVGAVDIDQERVVQKGRLQPGKMLLVDTVAGRIIDDSELKYTVAHRHDFSSWLNKELVKLPAITEKLVEQNMDLRHDLDNTTVQNDPRLKAFGYSFEQVTLLLGPMGADSKEALGSMGNDAPLACIAKQPRLLYEYFRQLFAQVTNPPIDPIREAVVMSLECYVGPQGNLLEMDPSQCRRLLLPSPILSIPEFNALKNINTVHKDWTVRLIDITFEKKKGVPGYIEALDRICDAATEAIQQGDKILILSDRATSADRVPVSALLATGLVHHHLVRNKWRSLAALIVETAEAREVHHMCVLVGYGADGINPYLAMECILKMNREKLIRKELSDEKVIENYKASCDGGILKVMSKMGISTLASYKGAQIFEALGIDDSVIDRCFTGTASRIRGMNFELIAQDAFAIHERGYPSRAIVDIPGLNESGEYHWRDGGEDHINDPVSIANIQDAVRTKNDKSYEAYAKAAHEQIKNCTLRGMLEFDFDQRTPIPIDQVEPWTEIVRRFVTGAMSYGSISMESHSTLAVAMNRLGGKSNTGEGGEDPERSKRMENGDTMRSAIKQIASGRFGVTSHYLADADELQIKMAQGAKPGEGGELPGHKVVGPIAHTRYSTPGVGLISPPPHHDIYSIEDLKQLIYDLKCSNPRARVSVKLVSEVGVGIVASGVAKAKADHILISGHDGGTGASRWTGIKYAGLPWELGLAETHQTLVLNDLRGRVIVQTDGQIRTGRDVAVACLLGAEEFGFATTPLIAMGCIMMRKCHLNTCPVGIATQDPELRKKFEGQPEHVINFFYYIANELRAIMAKLGIRTINEMVGRAELLKVRDDLTNPKQENIDLSLILTPAHSLRPGVATYNVRKQDHRLHTRLDNKLIAESELALEKGLPCRVECDVVNTDRALGATLSYQVSRRYGGEGLPQDTIHSNIKGSAGQSFGAYLAPGITLELEGDANDYVGKGLSGGRLIVYPPRGAAFKAEENVIVGNTCLYGATRGTCFFRGVAAERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGSTGRNFAAGMSGGIAYILDMNQDFLSKVNMEMVECSGLEDPAEIAFLRGLIEDHHHYTGSELAARILLDFTRALPHFIKVLPTDYKRTLEEEAAKAAAAKKAETTIPQLPSVPVEKQKPKAEGDAKKAELLDIEDSVTDSKVEKKRTALILDKTRGFMKYNRRSEKYRNPATRTRDWAELSSRLTEDELKYQSARCMDCGVPFCQSDTGCPISNIIPKWNELVFQNQWQDALNRLLMTNNFPEFTGRVCPAPCEGACVLGINEDPVGIKSIECAIIDRGFEMGWMVPRPPPVRTGKTVAIIGSGPAGLAAADQLNRVGHSVTVYERADRIGGLLMYGIPNMKLDKKIVQRRVDLMAAEGVKFVTGVSVGPDSEVSLDSLRKSNDAVIIATGATVARDLKVPGRELEGIHFAMQFLHKNTKSLLDSELADGAYISAKDKHVVVIGGGDTGNDCIGTSVRHGAKSVVNFELLPQPPPERARDNPWPQWPRIYRVDYGHSEVKTHMGKDPREYCIMSKEFVDDGNGRVKGINTVRVEWTKSATGGWDMKTVEGSEQFFPADLVLLSMGFLGPEDRLLGEEIERDARKNVKTPPGHYGTNVPGVYAAGDCRRGQSLIVWGINEGRQCAREVDTFLSGISSQLPVTGGIVRRPAVDAVRQATETVTIAA
Protein: Heat stress transcription factor C-1 (AtHsfC1) (AtHsf-08) (Q9LV52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 29
- Zinc finger protein ZAT12
- Zinc finger protein ZAT10
- AT3G10250 protein
- Dehydration-responsive element-binding protein 1C
- Multiprotein-bridging factor 1c
Sequence:
MEDDNSNNNNNNNVIAPFIVKTYQMVNDPSTDWLITWGPAHNSFIVVDPLDFSQRILPAYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEHFLRGQKHLLNNIARRKHARGMYGQDLEDGEIVREIERLKEEQRELEAEIQRMNRRIEATEKRPEQMMAFLYKVVEDPDLLPRMMLEKERTKQQQQVSDKKKRRVTMSTVKSEEEEVEEDEGRVFRVMSSSTPSPSSTENLYRNHSPDGWIVPMTQGQFGSYETGLVAKSMLSNSTSSTSSSLTSTFSLPESVNGGGGGGCGSIQGERRYKETATFGGVVESNPPTTPPYPFSLFRGGF
Protein: Heat shock protein Hsp-16.41 (P06581)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein hsp-16.2
- Heat shock protein 70
- Heat shock protein 12.6
- Heat shock protein 70
- Heat shock protein Hsp-16.1/Hsp-16.11
Sequence:
MLMLRSPYSDSNALDHFLDELTGSVQFPYWRNADHNSFNFSDNIGEIVNDESKFSVQLDVSHFKPENLKIKLDGRELKIEGIQETKSEHGYLKRSFSKMILLPEDADLPSVKSAISNEGKLQIEAPKKTNSSRSIPINFVAKH
Protein: Thyrotropin receptor (C0SKM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Cell membrane {ECO:0000256|RuleBase:RU361222}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361222}.
Interaction partners:
Sequence:
MKTHVMLVLMLPLVSVIGWTNSCPHGCECSQWKALVVSCMDVDSIPTLPERTEVLSLHETRLTRVPKDAFANMVNISRIYLSVDIFLSRLEMHSFHSLRELTHIEIRNTRKLTFIHPEAFKNLPNLQYLGLFNTGLTIFPDLTKIQAENSYFILEISDNPYIAEIPANAFFGITNDLLSLRLYSNGFTKVQPHAFNGTKLDSVYLHRNRELTRLDEKMFAGTSSGPMLLDVSESGVTSLPARGLDSLRELCARNVWALKKLPPIKTFRHLVTADLTYPSHCCAFKNLKKKRGFIEEIICNLTARKNQVQKRSVRAFTIHGLQGSMEPGIDLSDNLFRDTYDHQEFFGNGHYPTYFDRHADENMGFGETLKNPQEDTSREFDSRYDYIVCEKGEEVACFPAPDEFNPCEDIMGFSFLRVSVWFVSLLAVLGNLLVLLVLLTSHYKLSVSRFLMCHLAVADLCMGIYLLLIASVDLHTQSEYYNHAIDWQTGPGCSLAGFFSVFASELSVYTLTTITLERWYAITYAMRLDRKLRLSHASVIMLIGWIFCLLLGLMPLVGVSSYQKVSICLPMDTQTLVDQIYIICVLVLNILAFIVICVCYIKIYCAVHNPSHQSSNKDTNIAKRMAVLIFTDFLCMAPISLYAMTAVLDHPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQGDVFILLSKVGLCQRQAQLFRGQTVSSKASSRGITRHEREQTGANETPISLLDFPGKMAAAQQQEDSDGQGA
Protein: Src-like-adapter (Src-like-adapter protein 1) (SLAP-1) (hSLAP) (Q13239)
Organism: Homo sapiens (Human)
Function: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. Involved in the negative regulation of positive selection and mitosis of T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins.
Subcellular location: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Note=Colocalizes with endosomes. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase CBL
- Sarcolemmal membrane-associated protein
- NACHT, LRR and PYD domains-containing protein 2
- Receptor-type tyrosine-protein kinase FLT3
- Epidermal growth factor receptor
Sequence:
MGNSMKSTPAPAERPLPNPEGLDSDFLAVLSDYPSPDISPPIFRRGEKLRVISDEGGWWKAISLSTGRESYIPGICVARVYHGWLFEGLGRDKAEELLQLPDTKVGSFMIRESETKKGFYSLSVRHRQVKHYRIFRLPNNWYYISPRLTFQCLEDLVNHYSEVADGLCCVLTTPCLTQSTAAPAVRASSSPVTLRQKTVDWRRVSRLQEDPEGTENPLGVDESLFSYGLRESIASYLSLTSEDNTSFDRKKKSISLMYGGSKRKSSFFSSPPYFED
Protein: Mediator of RNA polymerase II transcription subunit 6 (Mediator complex subunit 6) (P38782)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MNVTPLDELQWKSPEWIQVFGLRTENVLDYFAESPFFDKTSNNQVIKMQRQFSQLNDPNAAVNMTQNIMTLPDGKNGNLEEEFAYVDPARRQILFKYPMYMQLEEELMKLDGTEYVLSSVREPDFWVIRKQRRTNNSGVGSAKGPEIIPLQDYYIIGANIYQSPTIFKIVQSRLMSTSYHLNSTLESLYDLIEFQPSQGVHYKVPTDTSTTATAATNGNNAGGGSNKSSVRPTGGANMATVPSTTNVNMTVNTMGTGGQTIDNGTGRTGNGNMGITTEMLDKLMVTSIRSTPNYI
Protein: Cyclin-A1-2 (G2/mitotic-specific cyclin-A1-2) (CycA1;2) (Protein TARDY ASYNCHRONOUS MEIOSIS) (Q9FVX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of male meiosis progression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15557098}. Nucleus {ECO:0000269|PubMed:15557098}.
Interaction partners:
- Cyclin-dependent kinase A-1
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B2-2
- Cell division control protein 6 homolog
- Wee1-like protein kinase
- Protein GIGAS CELL1
- Protein POLLENLESS 3
- Anaphase-promoting complex subunit 10
Sequence:
MSSSSRNLSQENPIPRPNLAKTRTSLRDVGNRRAPLGDITNQKNGSRNPSPSSTLVNCSNKIGQSKKAPKPALSRNWNLGILDSGLPPKPNAKSNIIVPYEDTELLQSDDSLLCSSPALSLDASPTQSDPSISTHDSLTNHVVDYMVESTTDDGNDDDDDEIVNIDSDLMDPQLCASFACDIYEHLRVSEVNKRPALDYMERTQSSINASMRSILIDWLVEVAEEYRLSPETLYLAVNYVDRYLTGNAINKQNLQLLGVTCMMIAAKYEEVCVPQVEDFCYITDNTYLRNELLEMESSVLNYLKFELTTPTAKCFLRRFLRAAQGRKEVPSLLSECLACYLTELSLLDYAMLRYAPSLVAASAVFLAQYTLHPSRKPWNATLEHYTSYRAKHMEACVKNLLQLCNEKLSSDVVAIRKKYSQHKYKFAAKKLCPTSLPQELFL
Protein: Daisho2 (Immune-induced peptide 14) (DIM-14) (DIM4) (P83869)
Organism: Drosophila melanogaster (Fruit fly)
Function: Peptide which plays a role in the humoral immune response to a subset of filamentous fungi, including F.oxysporum and F.verticillioides.
Subcellular location: Secreted {ECO:0000269|PubMed:14645501, ECO:0000269|PubMed:32038657, ECO:0000269|PubMed:9736738}.
Interaction partners:
- Daisho1
- Bomanin tailed 3, isoform A
- Bomanin Short 1
Sequence:
MNCLKICGFFFALIAALATAEAGTQVIHAGGHTLIQTDRSQYIRKN
Protein: Cancer/testis antigen 1 (Autoimmunogenic cancer/testis antigen NY-ESO-1) (Cancer/testis antigen 6.1) (CT6.1) (L antigen family member 2) (LAGE-2) (P78358)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12065688, ECO:0000269|PubMed:31429579}.
Interaction partners:
- Melanoma-associated antigen 3
- Melanoma-associated antigen 4
- Melanoma-associated antigen 1
- Cancer/testis antigen 2
- Melanoma-associated antigen 6
- Tyrosinase
- Melanocyte protein PMEL
- HLA class I histocompatibility antigen, A alpha chain
- Lymphocyte antigen 75
- Melanoma-associated antigen C1
Sequence:
MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPGGGAPRGPHGGAASGLNGCCRCGARGPESRLLEFYLAMPFATPMEAELARRSLAQDAPPLPVPGVLLKEFTVSGNILTIRLTAADHRQLQLSISSCLQQLSLLMWITQCFLPVFLAQPPSGQRR
Protein: Grixazone synthase (EC 1.10.3.15) (Phenoxazinone synthase) (PHS) (o-aminophenol oxidase) (EC 1.10.3.4) (B1VTI5)
Organism: Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)
Function: Involved in the biosynthesis of the parasiticide antibiotic grixazone. Catalyzes the oxidation of 3,4-aminohydroxybenzoate (3,4-AHBOA) to yield the corresponding quinone imine which is then non-enzymatically conjugated with the thiol group of N-acetylcysteine. The resultant compound is oxidized to its quinone imine enzymatically and is then dimerized non-enzymatically with another quinone imine oxidized by GriF to yield grixazone B. 3,4-aminohydroxybenzaldehyde (3,4-AHBAL) can also be used as substrate to yield grixazone A. In the grixazone biosynthetic pathway, it can also function as an o-aminophenol oxidase that catalyzes the formation of the phenoxazinone chromophore from alpha-aminophenol. It can also use 3,4-dihydroxybenzaldehyde, 2-amino-4-methylphenol and 3,4-dihydroxy-L-phenylalanine (L-DOPA) as substrates. In contrast to tyrosinases, it does not display monophenolase activity.
Interaction partners:
Sequence:
MVHVRKNHLTMTAEEKRRFVHAVLEIKRRGIYDRFVKLHIQINSTDYLDKETGKRLGHVNPGFLPWHRQYLLKFEQALQKVDPRVTLPYWDWTTDHGENSPLWSDTFMGGNGRPGDRRVMTGPFARRNGWKLNISVIPEGPEDPALNGNYTHDDRDYLVRDFGTLTPDLPTPQELEQTLDLTVYDCPPWNHTSGGTPPYESFRNHLEGYTKFAWEPRLGKLHGAAHVWTGGHMMYIGSPNDPVFFLNHCMIDRCWALWQARHPDVPHYLPTVPTQDVPDLNTPLGPWHTKTPADLLDHTRFYTYDQ
Protein: Cell growth regulator with EF hand domain protein 1 (Cell growth regulatory gene 11 protein) (Hydrophobestin) (P97586)
Organism: Rattus norvegicus (Rat)
Function: Mediates cell-cell adhesion in a calcium-dependent manner. Able to inhibit growth in several cell lines.
Subcellular location: Secreted {ECO:0000269|PubMed:19473726}.
Interaction partners:
Sequence:
MSRWLMQMLMLPLLLLPLGQAAPKDGVARLDPEAQQQLTTNPFQPGPEQLRRLRDYLKGLEKMEEDPEQMNREQVLLYLFALHDFDQNGQLDGLELLSMLTAALAPGAAHFPINPVILVVDMVLETQDLDGDGLMTPAELINFPGEAPKRAESLPPALQEPQPAGSQPLLANSPLQSETQQSLGTKEEITSQVEAKRALEPEQEAGHHIETKVDALSPEGEARGQAESEGDAPGPREDAERQVESKDNEGEAKDLPAETLETQNTPNVVEAHSIQLENDEI
Protein: Nucleolar protein 14 (Nucleolar complex protein 14) (P78316)
Organism: Homo sapiens (Human)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Bystin
- KRR1 small subunit processome component homolog
- WD repeat-containing protein 46
- Nucleolar complex protein 4 homolog
- Ribosomal RNA small subunit methyltransferase NEP1
- RNA cytidine acetyltransferase
- Nucleolar protein 6
- Protein RRP5 homolog
- Ribosome biogenesis protein BMS1 homolog
- Small subunit processome component 20 homolog
Sequence:
MAKAKKVGARRKASGAPAGARGGPAKANSNPFEVKVNRQKFQILGRKTRHDVGLPGVSRARALRKRTQTLLKEYKERDKSNVFRDKRFGEYNSNMSPEEKMMKRFALEQQRHHEKKSIYNLNEDEELTHYGQSLADIEKHNDIVDSDSDAEDRGTLSAELTAAHFGGGGGLLHKKTQQEGEEREKPKSRKELIEELIAKSKQEKRERQAQREDALELTEKLDQDWKEIQTLLSHKTPKSENRDKKEKPKPDAYDMMVRELGFEMKAQPSNRMKTEAELAKEEQEHLRKLEAERLRRMLGKDEDENVKKPKHMSADDLNDGFVLDKDDRRLLSYKDGKMNVEEDVQEEQSKEASDPESNEEEGDSSGGEDTEESDSPDSHLDLESNVESEEENEKPAKEQRQTPGKGLISGKERAGKATRDELPYTFAAPESYEELRSLLLGRSMEEQLLVVERIQKCNHPSLAEGNKAKLEKLFGFLLEYVGDLATDDPPDLTVIDKLVVHLYHLCQMFPESASDAIKFVLRDAMHEMEEMIETKGRAALPGLDVLIYLKITGLLFPTSDFWHPVVTPALVCLSQLLTKCPILSLQDVVKGLFVCCLFLEYVALSQRFIPELINFLLGILYIATPNKASQGSTLVHPFRALGKNSELLVVSAREDVATWQQSSLSLRWASRLRAPTSTEANHIRLSCLAVGLALLKRCVLMYGSLPSFHAIMGPLQALLTDHLADCSHPQELQELCQSTLTEMESQKQLCRPLTCEKSKPVPLKLFTPRLVKVLEFGRKQGSSKEEQERKRLIHKHKREFKGAVREIRKDNQFLARMQLSEIMERDAERKRKVKQLFNSLATQEGEWKALKRKKFKK
Protein: SIR4-interacting protein SIF2 (A0A1D8PPJ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Snt1p
- Histone-binding protein
- Transcriptional coactivator HFI1/ADA1
- Uncharacterized protein
- Histone deacetylase
- Peptidyl-prolyl cis-trans isomerase
- mRNA-capping enzyme subunit beta
- Hit1p
- Histone deacetylase
- histone deacetylase
Sequence:
MSLTSKELNYLIWRYLQESGYDLSAYALDQQSQCSEYENNPTTQELIQKIKPGCLVDLIQKGILYMAAEQEATDSTTNLSLYGALIQDDLNNLKDNNNISNGSNGSRFALKSEIETNGEQKDSEKQTNNDKDNQDIEMTDALNKEVQQQEIIEFETQLLSPQLKFAPSLTCDWHPTTEVFAYGKDDGTATINAIQDGKIIETRTLTHPNLLNIKNQINIVSWSPQGSLIITCGANSELRAWSPDGKLKNIASTIVDEAISLENTKLISIISSLSWSPTGKFLLSIDSSNQVCIWDGTTISLIKQIKNLEINDDSVVCSCWLSEDKFAVTTNTNGIKIYDILQPPSSHFGNQLDVQPIGLLNGHEHNISLMKLNPVTKLLATCSDFDYSIKVWSSSSSQECLDLNINPEKKYTLKLHAAPMIGLIWLPDSNSNERSLLLSVSMEGILNIWDAKTSENIKSSELFNNKDNFTNELKDDDNNNDNNNNDTTIKDVLVFNAVLSPDGKYLALGDDYCRVTIWDVDTTHYLNEPKDLIRCKAVYKPEISAEDKLKATIGICDMKWDHESKXNMCFLQWYGKCYNQHNIKXPKKKKKSL
Protein: Postacrosomal sheath WW domain-binding protein (WW domain-binding protein 2-like) (Q6ICG8)
Organism: Homo sapiens (Human)
Function: May play a role in meiotic resumption and pronuclear formation, mediated by a WW domain-signaling pathway during fertilization.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 9
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Mitochondrial-processing peptidase subunit beta
- MAX gene-associated protein
Sequence:
MAVNQSHTENRRGALIPNGESLLKRSPNVELSFPQRSEGSNVFSGRKTGTLFLTSYRVIFITSCSISDPMLSFMMPFDLMTNLTVEQPVFAANFIKGTIQAAPYGGWEGQATFKLVFRNGDAIEFAQLMVKAASAAARGFPLRTLNDWFSSMGIYVITGEGNMCTPQMPCSVIVYGAPPAGYGAPPPGYGAPPAGYGAQPVGNEGPPVGYRASPVRYGAPPLGYGAPPAGYGAPPLGYGAPPLGYGTPPLGYGAPPLGYGAPPAGNEGPPAGYRASPAGSGARPQESTAAQAPENEASLPSASSSQVHS
Protein: Tensin-1 (EC 3.1.3.-) (Q9HBL0)
Organism: Homo sapiens (Human)
Function: May act as a protein phosphatase and/or a lipid phosphatase (Probable). Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.
Subcellular location: Cell surface {ECO:0000269|PubMed:21768292}. Cell junction, focal adhesion {ECO:0000269|PubMed:19826001, ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:21768292}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21768292}. Note=Localizes to both focal adhesions and fibrillar adhesions (PubMed:20069572). Localized at the cell periphery preferentially to fibrillar adhesions rather than to focal adhesions. Translocates from the cell edge to the cell center in an ITGB1BP1-dependent manner (PubMed:21768292). {ECO:0000269|PubMed:20069572, ECO:0000269|PubMed:21768292}.
Interaction partners:
- Vinculin
- Proto-oncogene tyrosine-protein kinase Src
- Fibronectin
- Rho GTPase-activating protein 7
- Breast cancer anti-estrogen resistance protein 1
- Talin-1
Sequence:
MTWICLSCMLWPEDLEAPKTHRFKVKTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSNHELVPITTENAPKNVVDKGEGASRGGNTRKSLEDNGSTRVTPSVQPHLQPIRNMSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGMEEVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNATRPTLSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVPGASSATAALSPQEKRELDRLLSGFGLEREKQGAMYHTQHLRSRPAGGSAVPSSGRHVVPAQVHVNGGALASERETDILDDELPNQDGHSAGSMGTLSSLDGVTNTSEGGYPEALSPLTNGLDKSYPMEPMVNGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDPSGMFRSQSFSEAEPQLPPAPVRGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLESLVASRPSPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLNLEGLVAHRVAGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPLSALGLKPHNPADILLHPTGEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLESGFRSGSLGQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGFGWRAINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPGAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSPVASGMSSPSGGSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRDPTDESKDSSGPANSTADLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLNAGQKR
Protein: Cytochrome c-type protein TorC (P33226)
Organism: Escherichia coli (strain K12)
Function: Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity.
Subcellular location: Cell inner membrane; Single-pass type II membrane protein.
Interaction partners:
- Trimethylamine-N-oxide reductase 1
- Chaperone protein TorD
- Trimethylamine-N-oxide reductase 2
- Sensor protein TorS
- Periplasmic nitrate reductase, electron transfer subunit
- TorCAD operon transcriptional regulatory protein TorR
- Cytochrome c-type protein TorY
- Periplasmic protein TorT
- Periplasmic nitrate reductase
- Dimethyl sulfoxide reductase DmsA
Sequence:
MRKLWNALRRPSARWSVLALVAIGIVIGIALIVLPHVGIKVTSTTEFCVSCHSMQPVYEEYKQSVHFQNASGVRAECHDCHIPPDIPGMVKRKLEASNDIYQTFIAHSIDTPEKFEAKRAELAEREWARMKENNSATCRSCHNYDAMDHAKQHPEAARQMKVAAKDNQSCIDCHKGIAHQLPDMSSGFRKQFDELRASANDSGDTLYSIDIKPIYAAKGDKEASGSLLPASEVKVLKRDGDWLQIEITGWTESAGRQRVLTQFPGKRIFVASIRGDVQQQVKTLEKTTVADTNTEWSKLQATAWMKKGDMVNDIKPIWAYADSLYNGTCNQCHGAPEIAHFDANGWIGTLNGMIGFTSLDKREERTLLKYLQMNASDTAGKAHGDKKEEK
Protein: Cell division protein FtsA (Q6GHQ0)
Organism: Staphylococcus aureus (strain MRSA252)
Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02033}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_02033}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_02033}. Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix. {ECO:0000255|HAMAP-Rule:MF_02033}.
Interaction partners:
Sequence:
MEEHYYVSIDIGSSSVKTIVGEKFHNGINVIGTGQTYTSGIKNGLIDDFDIARQAIKDTIKKASIASGVDIKEVFLKLPIIGTEVYDESNEIDFYEDTEINGSHIEKVLEGIREKNDVQETEVINVFPIRFIVDKENEVSDPKELIARHSLKVEAGVIAIQKSILINMIKCVEACGVDVLDVYSDAYNYGSILTATEKELGACVIDIGEDVTQVAFYERGELVDADSIEMAGRDITDDIAQGLNTSYETAEKVKHQYGHAFYDSASDQDIFTVEQVDSDETVQYTQKDLSDFIEARVEEIFFEVFDVLQDLGLTKVNGGFIVTGGSANLLGVKELLSDMVSEKVRIHTPSQMGIRKPEFSSAISTISSSIAFDELLDYVTINYHDNEETEEDVIDVKDKDNESKLGGFDWFKRKTNKKDTHENEVESSDEEIYQSEDNHQEHKQNHEHVQDKDKEESKFKKLMKSLFE