wanglab/gogpt-training-data huggingface dataset:
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (A0A8I5ZXR3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKSCGVSLATAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEEYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQLENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQACKPHHPNTEPVLGLSQTPISQQSLPLHMIPPSQVDDLSSPAKRKRTSSPTKNTSDNWSGGNAVPHPPVQQQTHSWCLTPQKLQMRQTGVAQVRPTGIPNGPTADSSLPTNSASGQQPQLPLTRMPSVSQPGVQPACPRQALANGPFSAGHVPCSTSRTLGSTDTILIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGQSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTLPETNRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDIVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSVSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMVKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCAWKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
Protein: Solute carrier family 12 member 7 (Electroneutral potassium-chloride cotransporter 4) (K-Cl cotransporter 4) (Q5RK27)
Organism: Rattus norvegicus (Rat)
Function: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling (By similarity). May mediate K(+) uptake into Deiters' cells in the cochlea and contribute to K(+) recycling in the inner ear. Important for the survival of cochlear outer and inner hair cells and the maintenance of the organ of Corti. May be required for basolateral Cl(-) extrusion in the kidney and contribute to renal acidification (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q7YRU6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7YRU6}.
Interaction partners:
- STE20/SPS1-related proline-alanine-rich protein kinase
- Serine/threonine-protein kinase WNK3
Sequence:
MPTNFTVVPVEARADGAGDEAAERTEEPGSPESADPACPTPGDGNPRENSPFINNVEVERESYFEGKNMALFEEEMDSNPMVSSLLNKLANYTNLSQGVVEHEEDEDSRRREIKAPRMGTFIGVYLPCLQNILGVILFLRLTWIVGAAGVLESFLIVAMCCTCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEIFLTYISPSAAIFQAETADGEAAALLNNMRVYGSCALALMAVVVFVGVKYVNKLALVFLACVVLSILAIYAGVIKTAFAPPDIPVCLLGNRTLANRNFDTCAKMQVVSNGTVTTALWRLFCNGSSLGASCDEYFVQNNVTEIQGIPGVASGVFLDNLWSTYSDKGAFVEKKGVSSVPVSEESRPGGLPYVLTDIMTYFTMLVGIYFPSVTGIMAGSNRSGDLKDAQKSIPTGTILAIVTTSFIYLSCIVLFGACIEGVVLRDKFGEALQGNLVIGMLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIARDGIIPFLQVFGHGKANGEPTWALLLTALICETGILIASLDSVAPILSMFFLMCYMFVNLACAVQTLLRTPNWRPRFKFYHWTLSFLGMSLCLALMFICSWYYALFAMLIAGCIYKYIEYRGAEKEWGDGIRGLSLNAARYALLRVEHGPPHTKNWRPQVLVMLNLDSEQCVKHPRLLSFTSQLKAGKGLTIVGSVLEGTYLDKHVEAQRAEENIRSLMSAEKMKGFCQLVVSSNLRDGASHLIQSAGLGGMKHNTVLMAWPEAWKQADNPFSWKNFVDTVRDTTAAHQALLVAKNIDLFPQNQERFSDGNIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQVDDNSIQMKKDLQMFLYHLRISAEVEVVEMVENDISAFTYEKTLMMEQRSQMLKQMQLSKNEREREAQLIHDRNTASHTVATARTEAPPTPDKVQMTWTKEKLIAEKHRNKDTGTSGFKDLFSLKPDQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKSRQGDENYMEFLEVLTEGLNRVLLVRGGGREVITIYS
Protein: Outer membrane porin protein OmpD (P37592)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Subcellular location: Cell outer membrane; Multi-pass membrane protein.
Interaction partners:
- Outer membrane protein A
- Outer membrane protein TolC
- RNA-binding protein Hfq
- Outer membrane protein W
- Outer membrane protein X
- Ribonuclease E
- Outer membrane porin
- Lipid A biosynthesis acyltransferase
- Universal stress protein A
- Ail and ompX-like protein
Sequence:
MKLKLVAVAVTSLLAAGVVNAAEVYNKDGNKLDLYGKVHAQHYFSDDNGSDGDKTYARLGFKGETQINDQLTGFGQWEYEFKGNRTESQGADKDKTRLAFAGLKFADYGSFDYGRNYGVAYDIGAWTDVLPEFGGDTWTQTDVFMTGRTTGVATYRNTDFFGLVEGLNFAAQYQGKNDRDGAYESNGDGFGLSATYEYEGFGVGAAYAKSDRTNNQVKAASNLNAAGKNAEVWAAGLKYDANNIYLATTYSETLNMTTFGEDAAGDAFIANKTQNFEAVAQYQFDFGLRPSIAYLKSKGKNLGTYGDQDLVEYIDVGATYYFNKNMSTFVDYKINLLDDSDFTKAAKVSTDNIVAVGLNYQF
Protein: Neuromedin U receptor 3 (Neuromedin-U receptor 2) (A0A286YBK1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MMALICLCESVNTSDQDYEFCNSSTFNFTGNDSAHCYLQTIDEVLFKLLGPRRSPFFFPVTCTYILIFMTGVLGNLLTCAVITKDRKMQTPTNLYLFSLAISDLLVLLFGMPLEIYELWQNYPFPFGESICCFKIFLFETVCFASVLNVTVLSVERYIAVIHPLKTRYAITNKHARRVIAGVWAMSLLCAVPNTSLHGLQYQYLPERVQESATCNLLKPKWMYNLVIQITTVLFYFVPMMMISVLYLMIGLTLGRGQKQKKDKLGSNHSNDSWKIHLDSRRRRQVTKMHFVVVLVFAICWAPFHIDRLLWSFITSWTDHMHNIFEYVHIISGVLFYLSSAVNPIIYNLLSSRFRERFQALVCSRLSTRSSRNDSMPFYIIPKDPPTDFKRTG
Protein: Ferric-chelate reductase 1 (EC 1.-.-.-) (Stromal cell-derived receptor 2) (SDR-2) (Q8K385)
Organism: Mus musculus (Mouse)
Function: Ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS15m
Sequence:
MAAPQITLSVLVIALLTCSVTAYPNGKVPMSCGGMIPQHNHSPQSEPIHQITVSQTTFKPGDQIEVTLSGPPFRGFLLEARDAENLSGPPIGSFTLIDSEESQLLTCTDVQGLAVSHTRSSKKTEIKVYWDAPSPAPDHIRFLATVVQKFKIYWVKIPSPVISQPNAPPFTTPKATTQPLTTPPSVSHLTKPFSAFECGNKKFCVRSPLNCDPEKEPACVFLSFTRDNQSVMVEMSGPSDGYVSFAFSHDQWMGDDDAYLCIREDQTVDIQPSYLTGRSYPVMDSRGTLEDMAWRLADGVIQCSFRRNITLPEAKNRFVLNESYYIFFAEGPSHDGRIFRHSQQPLITYEKYNVTDTPKSVGGSRSSPLLKAHGALMFVAWMTTVSIGVLVARFFRSVWSKAFFLREAAWFQVHRMLMVATSLLTCVAFVLPFVYRGGWSWRAGYHPYLGCTVMTLAVLQPLLATFRPPLHDPRRQVFNWTHWSVGTAARIIAVAAMFLGMDLPGLNLPSPQKTYAMMGFVVWHIGTEVILEIHAYRLSRKVEILDNDRIQILQSLTVAEAEGHVFKKVVLAVYICGNVIFLSIFLSAINHI
Protein: Pleiotrophin (PTN) (Heparin-binding brain mitogen) (HBBM) (Heparin-binding growth factor 8) (HBGF-8) (Heparin-binding growth-associated molecule) (HB-GAM) (Heparin-binding neutrophic factor) (HBNF) (Osteoblast-specific factor 1) (OSF-1) (P63089)
Organism: Mus musculus (Mouse)
Function: Secreted growth factor that mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors (By similarity). Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups (By similarity). Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone. Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation. Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK or AFAP1L2 in order to activate the PI3K-AKT pathway. Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway. Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation (By similarity). In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway. Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion (By similarity). Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition (By similarity). Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation (By similarity). Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway. Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration. In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P21246}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase zeta
- ALK tyrosine kinase receptor
- Receptor-type tyrosine-protein phosphatase beta
- Syndecan-3
- SPARC
- Midkine
- Hepatoma-derived growth factor
- Plexin-B2
- SPARC-like protein 1
- Cystathionine gamma-lyase
Sequence:
MSSQQYQQQRRKFAAAFLALIFILAAVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNADCQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD
Protein: Phosphoheptose isomerase 2 (EC 5.3.1.28) (Sedoheptulose 7-phosphate isomerase 2) (Q9PMN3)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. No activity with L-galacto-heptulose, L-galacto-heptulose 7-phosphate or D-manno-heptulose.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}.
Interaction partners:
- D-glycero-alpha-D-manno-heptose 7-phosphate kinase
- D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Bifunctional protein HldE
- D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- GDP-D-glycero-alpha-D-manno-heptose dehydrogenase
- Methyltransferase family protein
- Histidine biosynthesis bifunctional protein HisB
- Chromosomal replication initiator protein DnaA
- Sugar transferase
Sequence:
MENLNSYIKGHFADSILVKEQILKDENLITLIKNASLEVIKAYKNGNKTLLAGNGGSAADAQHIAGEFVSRFYFDRPGIASIALTTDTSILTAIGNDYGYENLFARQVQAQGVKGDVFIGISTSGNSKNILKALEFCKQKEIISIGLSGASGGAMNELCDYCIKVPSTCTPRIQEAHILIGHIICAIVEEELFGKGFSCKQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4I3K4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- AT3g15480/MJK13_14
- Tetraspanin-3
- Glucan endo-1,3-beta-glucosidase 10
- Tetraspanin-16
- UDP-Glycosyltransferase superfamily protein
Sequence:
MLRLILSLVVWFVFMSGLFHVVRSQNRTTATTDPDEARALNKIFRTWKITATKAWNISGELCSGAAIDDSVSIDNLAFNPLIKCDCSFVDSTICRIVALRARGMDVAGPIPDDLWTLVYISNLNLNQNFLTGPLSPGIGNLTRMQWMTFGANALSGPVPKEIGLLTDLRSLAIDMNNFSGSLPPEIGNCTRLVKMYIGSSGLSGEIPSSFANFVNLEEAWINDIRLTGQIPDFIGNWTKLTTLRILGTSLSGPIPSTFANLISLTELRLGEISNISSSLQFIREMKSISVLVLRNNNLTGTIPSNIGDYLGLRQLDLSFNKLTGQIPAPLFNSRQLTHLFLGNNRLNGSLPTQKSPSLSNIDVSYNDLTGDLPSWVRLPNLQLNLIANHFTVGGSNRRALPRLDCLQKDFRCNRGKGVYFNFFVNCGGRDIRSSSGALYEKDEGALGPATFFVSKTQRWAVSNVGLFTGSNSNQYIALSATQFANTSDSELFQSARLSASSLRYYGLGLENGGYSVTVQFAEIQIQGSNTWKSLGRRIFDIYVQGKLVEKDFDMQKAANGSSIRVIQRVYKANVSENYLEVHLFWAGKGTCCIPAQGTYGPLVSAISATPDFIPTVKNKLPSKSKKNIVIIVGAIVGAGMLCILVIAILLFIRRKRKRAADEEVLNSLHIRPYTFSYSELRTATQDFDPSNKLGEGGFGPVFKGKLNDGREIAVKQLSVASRQGKGQFVAEIATISAVQHRNLVKLYGCCIEGNQRMLVYEYLSNKSLDQALFGKCMRSYMCYPCKKNKCCYLTCCVTVAEEKSLQLGWSQRFEICLGVAKGLAYMHEESNPRIVHRDVKASNILLDSDLVPKLSDFGLAKLYDDKKTHISTRVAGTIGYLSPEYVMLGHLTEKTDVFAFGIVALEIVSGRPNSSPELDDDKQYLLEWAWSLHQEQRDMEVVDPDLTEFDKEEVKRVIGVAFLCTQTDHAIRPTMSRVVGMLTGDVEITEANAKPGYVSERTFENAMSFMSGSTSSSWILPETPKDSSKSQVEEHGRRH
Protein: Spore germination protein 3 (SPG3) (P15521)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Coronin binding protein
- Stalk-specific protein A
- Spore germination protein 270-11
Sequence:
MNIRNSLILIISSIFVLSFINGGLTSDPTCVGAPDGQVYLFSSWDFQGERYVYNISQGYLSLPDGFRNNVQSFISGADVCFVKWYPSEQYQITAGESHRNYAALTNFGQRMDAIIPGNCSNIVCSSK
Protein: Mesothelin (Pre-pro-megakaryocyte-potentiating factor) [Cleaved into: Megakaryocyte-potentiating factor (MPF); Mesothelin, cleaved form] (Q61468)
Organism: Mus musculus (Mouse)
Function: Membrane-anchored forms may play a role in cellular adhesion.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Golgi apparatus {ECO:0000250}.; SUBCELLULAR LOCATION: [Megakaryocyte-potentiating factor]: Secreted {ECO:0000250}.
Interaction partners:
- Mucin 16
- Mucin-1
- Uroplakin-3b
- Glutamate carboxypeptidase 2
- Prostate stem cell antigen
- Epidermal growth factor receptor
- T-cell surface glycoprotein CD3 zeta chain
- Tumor necrosis factor receptor superfamily member 9
Sequence:
MALPTARPLLGSCGSPICSRSFLLLLLSLGWIPRLQTQTTKTSQEATLLHAVNGAADFASLPTGLFLGLTCEEVSDLSMEQAKGLAMAVRQKNITLRGHQLRCLARRLPRHLTDEELNALPLDLLLFLNPAMFPGQQACAHFFSLISKANVDVLPRRSLERQRLLMEALKCQGVYGFQVSEADVRALGGLACDLPGKFVARSSEVLLPWLAGCQGPLDQSQEKAVREVLRSGRTQYGPPSKWSVSTLDALQSLVAVLDESIVQSIPKDVKAEWLQHISRDPSRLGSKLTVIHPRFRRDAEQKACPPGKEPYKVDEDLIFYQNWELEACVDGTMLARQMDLVNEIPFTYEQLSIFKHKLDKTYPQGYPESLIQQLGHFFRYVSPEDIHQWNVTSPDTVKTLLKVSKGQKMNAQAIALVACYLRGGGQLDEDMVKALGDIPLSYLCDFSPQDLHSVPSSVMWLVGPQDLDKCSQRHLGLLYQKACSAFQNVSGLEYFEKIKTFLGGASVKDLRALSQHNVSMDIATFKRLQVDSLVGLSVAEVQKLLGPNIVDLKTEEDKSPVRDWLFRQHQKDLDRLGLGLQGGIPNGYLVLDFNVREAFSSRASLLGPGFVLIWIPALLPALRLS
Protein: Interphotoreceptor matrix proteoglycan 1 (Interphotoreceptor matrix proteoglycan of 150 kDa) (IPM-150) (Sialoprotein associated with cones and rods) (Q8R1W8)
Organism: Mus musculus (Mouse)
Function: Chondroitin sulfate-, heparin- and hyaluronan-binding protein (By similarity). May serve to form a basic macromolecular scaffold comprising the insoluble interphotoreceptor matrix (By similarity).
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q17R60}. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:10995555, ECO:0000269|PubMed:29777959}. Photoreceptor inner segment {ECO:0000269|PubMed:10995555}.
Interaction partners:
- Retinol-binding protein 3
Sequence:
MNLQIKHAIFVLGIFLQVQGIKDTSIKIFSSEIKNIDKTPRIETIESTSTVHKVSTMKRIFDLPKLRTKRSALFPAANICPQESLRQILASLQEYYRLRVCQEVVWEAYRIFLDRIPDTEEYQDWVSLCQKETFCLFDIGKNFSNSQEHLDLLQQRIKQRSFPGRKDETASMETLEAPTEAPVVPTDVSRMSLGPFPLPSDDTDLKEILSVTLKDIQKPTTESKTEPIHVSEFSSEEKVEFSISLPNHRFKAELTNSGSPYYQELVGQSQLQLQKIFKKLPGFGEIRVLGFRPKKEEDGSSSTEIQLMAIFKRDHAEAKSPDSHLLSLDSNKIESERIHHGVIEDKQPETYLTATDLKKLIIQLLDGDLSLVEGKIPFGDEVTGTLFRPVTEPDLPKPLADVTEDATLSPELPFVEPRLEAVDREGSELPGMSSKDSSWSPPVSASISRSENLPSFTPSIFSLDAQSPPPLMTTGPTALIPKPTLPTIDYSTIRQLPLESSHWPASSSDRELITSSHDTIRDLDGMDVSDTPALSEISELSGYDSASGQFLEMTTPIPTVRFITTSSETIATKGQELVVFFSLRVANMPFSYDLFNKSSLEYQALEQRFTDLLVPYLRSNLTGFKQLEILSFRNGSVIVNSKVRFAKAVPYNLTQAVRGVLEDLRSTAAQGLNLEIESYSLDIEPADQADPCKLLDCGKFAQCVKNEWTEEAECRCRQGHESHGTLDYQTLNLCPPGKTCVAGREQATPCRPPDHSTNQAQEPGVKKLRQQNKVVKKRNSKLSAIGFEEFEDQDWEGN
Protein: Stress response protein NST1 (Negatively-affecting salt tolerance protein 1) (P53935)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With MSL1, acts as a negative regulator of salt tolerance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- AP-2 complex subunit mu
- Protein CAF40
- General negative regulator of transcription subunit 3
- Putative uncharacterized protein YNL089C
- Uncharacterized protein YKL075C
- Tubulin beta chain
Sequence:
MPPNSKSKRRKNKSKQHNKKNGNSDPEQSINPTQLVPRMEPELYHTESDYPTSRVIKRAPNGDVIVEPINTDDDKKERTANLTHNKDSMDSASSLAFTLDSHWESLSPEEKKTILRIEKEEVFNVIRNYQDDHSCSCSVCGRRHLAMDQEMERIYNTLYAMDKDKDPETNPIKFHLGIIKELQISKNQQQNDLSSTKGEVVKNFLSSSTVGSLKEEVLHFKQKQLSKQEQAHNETADNTSLLEENLNNIHINKTSSEISANFNSVSDEELQQKYSNFTKTFISSHPKIAEEYVQKMMMYPNIRALTDDLMNSNGQGFLNAIEDFVRDGQIQASKKDDSITEDEASSTDLTDPKEFTTMLHSGKPLTEDEYADLQRNIAERMTNAYDTASKKFKDVSQLEKELFTRFMSGRDKKSFRELIIQSFKNKFDGELGPSVLAATLSSCFSSQSKDTSLDTDSIYEDEDEEDYDDYSEYAEDSEEVSEYEGIEAVEKPEHDEKSNGIRETLHLSYDHDHKRQNHPHHHYHSTSTHSEDELSEEEYISDIELPHDPHKHFHRDDDILDGDEDEPEEEDENEGDDEEDTYDSGLDETDRLEEGRKLIQIAITKLLQSRIMASYHEKQADNNRLKLLQELEEEKRKKREKEEKKQKKREKEKEKKRLQQLAKEEEKRKREEEKERLKKELEEREMRRREAQRKKVEEAKRKKDEERKRRLEEQQRREEMQEKQRKQKEELKRKREEEKKRIREQKRLEQEKLQKEKEEEERQRLIAEDALRKQKLNEEQTSANILSAKPFTENGVGNPVSSQSHPNMTNYQEDNSCSINDEILKMVNSVAASKPVSPTGFNVHDLLLPSTNNQMPAMEQSHLPQPGNQNNHFGTTTIPNALDLATKSSLQTENNYLMNSQTLENTSLLMHNNSSPTKLLPNDFGLSSWGGLTNTMSINPTCKPPVIQTSEMESQAHKSSPQATMPSFGLPNGGTHRKSFTDELNTLTSMLSSSGFADTSLSSSGFPPSQRSVWNDQKSSFSGPSTAGNFNNSSIQSGMLLAPTLGSVESFPNRTSIWDSSTTPMMNKSELSGRNITSTAQDSPAFMASNIWSSNSQYNSPYLTSNVLQSPQISSGVDESHILDSIYNTYLAISPQDSLNPYIAIGTLFQNLVGLNLDYSTFINKLISMQGAYNCEFFTDNNGSITHVRFARQTPAGHSKGLLNQLFSGLNDPTATPFTSRPHTSTRASFPIASSTTQTS
Protein: Putative protein CRIPTO3 (Cripto, EGF-CFC family member 3) (Cripto-3 growth factor) (Epidermal growth factor-like cripto protein CR3) (Teratocarcinoma-derived growth factor 1 pseudogene 3) (Teratocarcinoma-derived growth factor 3) (P51864)
Organism: Homo sapiens (Human)
Function: Could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm. Activates the Nodal-dependent signaling pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18835250}.
Interaction partners:
Sequence:
MDCRKMVRFSYSVIWIMAISKAFELGLVAGLGHQEFARPSRGDLAFRDDSIWPQEEPAIRPRSSQRVLPMGIQHSKELNRTCCLNGGTCMLESFCACPPSFYGRNCEHDVRKENCGSVPHDTWLPKKCSLCKCWHGQLRCFPQAFLPGCDGLVMDEHLVASRTPELPPSARTTTFMLAGICLSIQSYY
Protein: Major carboxysome shell protein CsoS1A (P45689)
Organism: Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Function: The major shell protein of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, ccbL-ccbS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The shell probably limits the diffusion of CO(2) into and out of the carboxysome (Probable). Molecular modeling shows the central pore of this protein is selectively permeable to anions such as HCO(3) rather than CO(2) or O(2) (Probable). There are estimated to be 2970 CsoS1A/CsoS1C proteins per carboxysome (the proteins differ by only 1 residue) (Ref.5).
Subcellular location: Carboxysome {ECO:0000269|PubMed:18258595, ECO:0000269|PubMed:7934888, ECO:0000305|PubMed:29922315}. Note=This bacterium makes alpha-type carboxysomes. {ECO:0000269|PubMed:17518518, ECO:0000269|PubMed:18258595, ECO:0000269|Ref.5}.
Interaction partners:
- TIGRFAM: carboxysome peptide A
- Carboxysome shell protein CsoS1C
- TIGRFAM: carboxysome peptide B
- Carboxysome shell protein CsoS1B
- Carboxysome shell protein CsoS1D
- KEGG: tgr:Tgr7_3201 carboxysome shell protein CsoS2.
Sequence:
MADVTGIALGMIETRGLVPAIEAADAMTKAAEVRLVGRQFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDGLVAAHIIARVHSEVENILPKAPQA
Protein: FK506-binding protein 4 (EC 5.2.1.8) (Histone proline isomerase) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (Q06205)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at 'Pro-17' (H3P16), 'Pro-31' (H3P30) and 'Pro-39 (H3P38) on the histone H3 N-terminal tail. H3P16 and H3P30 are the major proline targets with little activity shown against H3P38. H3P38 isomerization influences SET2-mediated H3K36 methylation thereby regulating gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:14981505, ECO:0000269|PubMed:9371805}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- 25S rRNA
- Ribosome biogenesis protein RPF2
- Ribosome biogenesis protein ERB1
- Histone H3
- Nucleolar complex protein 2
- Periodic tryptophan protein 1
- Nucleolar protein 58
- 60S ribosomal subunit assembly/export protein LOC1
- H/ACA ribonucleoprotein complex subunit CBF5
Sequence:
MSDMLPLATYSLNVEPYSPTPALNFKIPVTIRITMAAIDPEPFDDDKKPSTLRIIKRNPELTRGEYYNQDNNDGLEEDESESEQEADVPKRSVKSKKGKAVEQSESEDSEDENEIDDEFEECVLLTLSPKGQYQQALDITIAPEEDVQFVVTGSYTISLTGNYVKHPFDNSSDSDEDEEDYYSDEESSNGEEEEEEEEEDDEELSSGDDDLDDLVDASDIESRLDELVKKDEKKKNNKKDSKRKHEEDEEESAKPAEKKQTTKKDKKAEKVKDSEESKPKPKTKLLEGGIIIEDRVTGKGPHAKKGTRVGMRYVGKLKNGKVFDKNTKGKPFVFKLGQGEVIKGWDIGVAGMAVGGERRIVIPAPYAYGKQALPGIPANSELTFDVKLVSMK
Protein: Kinectin (CG-1 antigen) (Kinesin receptor) (Q86UP2)
Organism: Homo sapiens (Human)
Function: Receptor for kinesin thus involved in kinesin-driven vesicle motility. Accumulates in integrin-based adhesion complexes (IAC) upon integrin aggregation by fibronectin.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Note=Vesicle membrane protein anchored to the endoplasmic reticulum.
Interaction partners:
- Elongation factor 1-delta
- Transforming protein RhoA
- Rho-related GTP-binding protein RhoG
- Elongation factor 1-gamma
- Kinesin light chain 1
- Kinesin-1 heavy chain
- Cerebellar degeneration-related protein 2
Sequence:
MEFYESAYFIVLIPSIVITVIFLFFWLFMKETLYDEVLAKQKREQKLIPTKTDKKKAEKKKNKKKEIQNGNLHESDSESVPRDFKLSDALAVEDDQVAPVPLNVVETSSSVRERKKKEKKQKPVLEEQVIKESDASKIPGKKVEPVPVTKQPTPPSEAAASKKKPGQKKSKNGSDDQDKKVETLMVPSKRQEALPLHQETKQESGSGKKKASSKKQKTENVFVDEPLIHATTYIPLMDNADSSPVVDKREVIDLLKPDQVEGIQKSGTKKLKTETDKENAEVKFKDFLLSLKTMMFSEDEALCVVDLLKEKSGVIQDALKKSSKGELTTLIHQLQEKDKLLAAVKEDAAATKDRCKQLTQEMMTEKERSNVVITRMKDRIGTLEKEHNVFQNKIHVSYQETQQMQMKFQQVREQMEAEIAHLKQENGILRDAVSNTTNQLESKQSAELNKLRQDYARLVNELTEKTGKLQQEEVQKKNAEQAATQLKVQLQEAERRWEEVQSYIRKRTAEHEAAQQDLQSKFVAKENEVQSLHSKLTDTLVSKQQLEQRLMQLMESEQKRVNKEESLQMQVQDILEQNEALKAQIQQFHSQIAAQTSASVLAEELHKVIAEKDKQIKQTEDSLASERDRLTSKEEELKDIQNMNFLLKAEVQKLQALANEQAAAAHELEKMQQSVYVKDDKIRLLEEQLQHEISNKMEEFKILNDQNKALKSEVQKLQTLVSEQPNKDVVEQMEKCIQEKDEKLKTVEELLETGLIQVATKEEELNAIRTENSSLTKEVQDLKAKQNDQVSFASLVEELKKVIHEKDGKIKSVEELLEAELLKVANKEKTVQDLKQEIKALKEEIGNVQLEKAQQLSITSKVQELQNLLKGKEEQMNTMKAVLEEKEKDLANTGKWLQDLQEENESLKAHVQEVAQHNLKEASSASQFEELEIVLKEKENELKRLEAMLKERESDLSSKTQLLQDVQDENKLFKSQIEQLKQQNYQQASSFPPHEELLKVISEREKEISGLWNELDSLKDAVEHQRKKNNDLREKNWEAMEALASTEKMLQDKVNKTSKERQQQVEAVELEAKEVLKKLFPKVSVPSNLSYGEWLHGFEKKAKECMAGTSGSEEVKVLEHKLKEADEMHTLLQLECEKYKSVLAETEGILQKLQRSVEQEENKWKVKVDESHKTIKQMQSSFTSSEQELERLRSENKDIENLRREREHLEMELEKAEMERSTYVTEVRELKDLLTELQKKLDDSYSEAVRQNEELNLLKAQLNETLTKLRTEQNERQKVAGDLHKAQQSLELIQSKIVKAAGDTTVIENSDVSPETESSEKETMSVSLNQTVTQLQQLLQAVNQQLTKEKEHYQVLE