wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 180 (HHZ168) (Q9UJW8)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MRACAGSTREAGSGAQDLSTLLCLEESMEEQDEKPPEPPKVCAQDSFLPQEIIIKVEGEDTGSLTIPSQEGVNFKIVTVDFTREEQGTCNPAQRTLDRDVILENHRDLVSWDLATAVGKKDSTSKQRIFDEEPANGVKIERFTRDDPWLSSCEEVDDCKDQLEKQQEKQEILLQEVAFTQRKAVIHERVCKSDETGEKSGLNSSLFSSPVIPIRNHFHKHVSHAKKWHLNAAVNSHQKINENETLYENNECGKPPQSIHLIQFTRTQTKDKSYGFSDRIQSFCHGTPLHIHEKIHGGGKTFDFKECGQVLNPKISHNEQQRIPFEESQYKCSETSHSSSLTQNMRNNSEEKPFECNQCGKSFSWSSHLVAHQRTHTGEKPYECSECGKSFSRSSHLVSHQRTHTGEKPYRCNQCGKSFSQSYVLVVHQRTHTGEKPYECNQCGKSFRQSYKLIAHQRTHTGEKPYECNQCGKSFIQSYKLIAHQRIHTGEKPYECNQCGKSFSQSYKLVAHQRTHTGEKPFECNQCGKSFSWSSQLVAHQRTHTGEKPYECSECGKSFNRSSHLVMHQRIHTGEKPYECNQCGKSFSQSYVLVVHQRTHTGEKPYECSQCGKSFRQSSCLTQHQRTHTGEKPFECNQCGKTFSLSARLIVHQRTHTGEKPFTCIQCGKAFINSYKLIRHQATHTEEKLYECN
Protein: Carboxypeptidase D (EC 3.4.17.22) (Metallocarboxypeptidase D) (gp180) (Q9JHW1)
Organism: Rattus norvegicus (Rat)
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:11181555}.
Interaction partners:
- Prestin
Sequence:
MASGWDERPPWRLESLRLLPPPPLLLLLLLLRSSAQAAHIKKAEATTTTVGGSEAAEGQFDHYYHEAALGEALEAAAAAGPPGLARLFSIGNSVEGRPLWVLRLTAGLGPPPTPAAVGLDAAGPLLPGRPQVKLVGNMHGDETVSRQVLVYLARELASGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGLGDSGPPGTSGRDNSRGRDLNRSFPDQFSTGEPPSLDEVPEVRALIDWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKTTGIYSKTSDDEVFRYLAKAYASNHPIMRTGEPHCPGDEEETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGIKGFVKDSVTGSGLENATISVAGINHNITTGRFGDFHRLLIPGSYNLTAVSPGYMPLTINNIVVKEGPATEIDFSLQPTVMSVVPDSTEAVTTPGTVAVPNIPPGTPSSHQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVRSTRIHLMPSMNPDGYEKSQEGDSISVVGRNNSNNFDLNRNFPDQFVPITDPTQPETIAVMSWVKAYPFVLSANLHGGSLVVNYPYDDNEQGVATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKDMYLNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPFEKELPKYWEQNRRSLIQFMKQVHQGVKGFVLDATDGRGILNATLSVAEINHPVTTYKAGDYWRLLVPGTYKITASARGYNPVTKNVTVRSEGAIQVNFTLVRSSTDANNESKKGKGHSTSTDDTSDPTSKEFEALIKHLSAENGLEGFMLSSSSDLALYRYHSYKDLSEFLRGLVMNYPHITNLTTLGQSVEYRHIWSLEISNKPNISEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPVVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKTGHTNARGRDLDTDFTSNASQPETKAIIENLIQKQDFSLSIALDGGSVLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNNSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAAQLPALWAENKKSLLSMLVEVHKGVHGLVKDKTGKPISKAVIVLNEGIRVHTKEGGYFHVLLAPGVHNINAIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH
Protein: BZIP domain-containing protein (H2L0F5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQQNIQYTYSSDPRSGGNQNQQLHGISQFQQNSYQPTTYSNSNANNFHSSNSATFIPNSVTQTPQRRMGEEKSLVNMLDAYFIDSTTPSTSTSWNNQQPVQDLQVEGMNVKLSSSPDKGEKDRVKKARQAEAARMRYHRLSNEEKRELNLKRTLAQKRKRQREKEMEELESILRETNDIQEDPDITEQLREKRMRAKWAEAARTRYARMTPEERRAHNTRRRMRQMQNAMSAIKACGMATGDPQKDDEAVRLHIKTQNAKKAEAARQRYHRMNDDEKRVYNQRRTEAFRRRRMEEEMLLAMPIGRINGEALDRAQQIVVRNAKRAEAARLRYQRMTPDQRKVAKQEPKEESWPSHEQSDTQIDHDLDLGDSYNQKRYTPKRRRNEMDDMISAGQMAVGSSGTITMGTGTPAKKDDMDALSSLERDVVKRTQHAQQILLRQRANQSSGTPRSVTPPPQAYIISNGQQQHQQLVGNQGNNGIGQHQVLHQGHMQQQQIQVSHQQSSQSIPQNIYTSGMIIQNQGQQQQGQQQQQGQSQQILNNPYRT
Protein: Non-specific lipid-transfer protein (Q9M6B8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASSMSLKLACVVVLCMVVGAPLAQGTVTCGQVTGSLAPCINYLRGNGAGAVPQGCCSGIKSLNSAAQTTPDRQAACKCIKSAAAGIPGINYGIASGLPGKCGVNIPYKISPSTDCSRVK
Protein: Immunoglobulin lambda variable 2-14 (Ig lambda chain V-II region NIG-84) (Ig lambda chain V-II region TOG) (Ig lambda chain V-II region VIL) (P01704)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWALLLLTLLTQGTGSWAQSALTQPASVSGSPGQSITISCTGTSSDVGGYNYVSWYQQHPGKAPKLMIYEVSNRPSGVSNRFSGSKSGNTASLTISGLQAEDEADYYCSSYTSSSTLHS
Protein: superoxide dismutase (EC 1.15.1.1) (P93800)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MVKAVAVLGSSEGVKGTIFFTQEGDGPTTVTGSVSGLKPGLHGFHVHALGDTTNGCMSTGPHYNPASKEHGAPEDENRHAGDLGNVTAGADGVANINVTDSQIPLTGPNSIIGRAVVVHADPDD
Protein: Elongation factor 2 (EF-2) (EC 3.6.5.-) (P55823)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus {ECO:0000250|UniProtKB:P13639}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000250|UniProtKB:P13639}.
Interaction partners:
Sequence:
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEIPALDNFLDKL
Protein: Zinc finger protein 473 (F8WEC7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDFTLGDWEQLGLEQGDTFWDTALDNCQDLFLLDPPRPNLTSHPDGSEDLEPLAGGSPEATSPDVTETKNSPLMEDFFEEGFSQEIIEMLSKDGFWNSNFGEACIEDTWLDSLLGDPESLLRSDIATNGESPTECKSHELKRGLSPVSTVSTGEDSMVHNVSEKTLTPAKSKEYRGEFFSYSDHSQQDSVQEGEKPYQCSECGKSFSGSYRLTQHWITHTREKPTVHQECEQGFDRNASLSVYPKTHTGYKFYVCNEYGTTFSQSTYLWHQKTHTGEKPCKSQDSDHPPSHDTQPGEHQKTHTDSKSYNCNECGKAFTRIFHLTRHQKIHTRKRYECSKCQATFNLRKHLIQHQKTHAAKTTSECQECGKIFRHSSLLIEHQALHAGEEPYKCNERGKSFRHNSTLKIHQRVHSGEKPYKCSECGKAFHRHTHLNEHRRIHTGYRPHKCQECVRSFSRPSHLMRHQAIHTAEKPYSCAECKETFSDNNRLVQHQKMHTVKTPYECQECGERFICGSTLKCHESVHAREKQGFFVSGKILDQNPEQKEKCFKCNKCEKTFSCSKYLTQHERIHTRGVKPFECDQCGKAFGQSTRLIHHQRIHSRVRLYKWGEQGKAISSASLIKLQSFHTKEHPFKCNECGKTFSHSAHLSKHQLIHAGENPFKCSKCDRVFTQRNYLVQHERTHARKKPLVCNECGKTFRQSSCLSKHQRIHSGEKPYVCDYCGKAFGLSAELVRHQRIHTGEKPYVCQECGKAFTQSSCLSIHRRVHTGEKPYRCGECGKAFAQKANLTQHQRIHTGEKPYSCNVCGKAFVLSAHLNQHLRVHTQETLYQCQRCQKAFRCHSSLSRHQRVHNKQQYCL
Protein: Secreted protein (B6VQ74)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNSFVILAIVLAIVNAMPVEQDGLTGGRGVPHPNSAAGQALSGKTGGSSVPHPNSAAGQALSGGMTGGSAVPHPNSAAGQELTNKNLEEKSVLEGGTQVKPWLKNQPDLANIREQNHQ
Protein: Ethylene-responsive transcription factor ERF039 (Q9SUK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At1g49010
Sequence:
MQDSSSHESQRNLRSPVPEKTGKSSKTKNEQKGVSKQPNFRGVRMRQWGKWVSEIREPRKKSRIWLGTFSTPEMAARAHDVAALAIKGGSAHLNFPELAYHLPRPASADPKDIQEAAAAAAAVDWKAPESPSSTVTSSPVADDAFSDLPDLLLDVNDHNKNDGFWDSFPYEDPFFLENY
Protein: Cytochrome c oxidase subunit 2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide II) (P00410)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (Probable). COX2 is a catalytic core subunit which transfers the electrons from cytochrome c via its dinuclear copper A center (CU(A)) to the BNC of the COX1.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Multi-pass membrane protein {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b
- Intron-encoded DNA endonuclease aI4
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase assembly factor 6
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MLDLLRLQLTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFINDSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVSLPKFLEWLNEQ
Protein: Dynein heavy chain, putative (Q57ZY4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSAEKDISDVCVDVAGETLKQLGASVSSTNRRSDVVELQIAVGSEKCPPIAAALFSGFVKAACGSEAGTTKVGLTDVNIDARENFTVLRFAEAVRVRDLDFNELPGDSPPITSVVEVTYMRYLIKHSELQVFQVSDFPKCLTPRGGQRLDTVVAGYVLFSLQSSEEDDTKVLLYMKSLRRVLGGMCTSSFAETVLSQAWGNMDSVEPSHVTDMLEDAQMAITDFWNDSDQDTAIRTKVVFLMKTVGSNLREYFAKKTLDAGGVFSGSKNITEVALGCCDEWVNMCKRLTTVDWGSSWGTAFEDVQLITVRDRLSVVVSIRDLVDEIVELLTAADKLQSLRTETLWETFDSLDIFATTPAVEQLWTNCLDAFYRRLQPVEHRCASALSDFFGERGNLAPQTILNEVVKFRQLIRRPAVSKELVNERDALLAKLNERLQSIRMEFERRSESVEDDVALDEEDRRCQAGRFM
Protein: KRAB zinc finger protein 6D (Q8CIP9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDAVTFDDVHMNFTKEEWNLLDPSQMNLYKDVMLETYWNLTSIGYKWEDHHIEEPCQSSRRHTRHVRSHSWKKLYECNQCGKAFSSHSSLRYHKRTHTGEKPYECNHCGKAFATPSHLQRHKRTHTGEKPYECNQCGKAFSSHSNLKYHKRNHTGVKPYECNQCGKVFVATTTLRRHKRTHTGEKPYECNQCGKAFSCHSSLIYHKRTHTGEKPYECNQCGKAFSCHSSLRCHERTHTGEKPYECNQCGKTFATSSHLQCHKRTHTGARNS
Protein: Nuclear GTP-binding protein NUG1 (Nuclear GTPase 1) (P40010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTPase required for 60S ribosomal subunit export to the cytoplasm.
Subcellular location: Nucleus {ECO:0000269|PubMed:11583615}.
Interaction partners:
- 27S pre-rRNA
- 60S ribosome subunit biogenesis protein NIP7
- Ribosome production factor 1
- Ribosome biogenesis protein RLP24
- Ribosome biogenesis protein YTM1
- Nucleolar GTP-binding protein 1
- Nucleolar GTP-binding protein 2
- Ribosome biogenesis protein NSA2
- Probable metalloprotease ARX1
- Nucleolar complex-associated protein 3
Sequence:
MRVRKRQSRRTSTKLKEGIKKKASAHRKKEKKMAKKDVTWRSRSKKDPGIPSNFPYKAKILEEIEAKKMKDLEERELAKQQRLEARKAAKEQGVDAMDEDMIEDDENGLAALVESAQQAAAEYEGTPSNDADVRDDELDVIDYNIDFYGEDVEGESELEKSRKAYDKIFKSVIDASDVILYVLDARDPESTRSRKVEEAVLQSQGKRLILILNKVDLIPPHVLEQWLNYLKSSFPTIPLRASSGAVNGTSFNRKLSQTTTASALLESLKTYSNNSNLKRSIVVGVIGYPNVGKSSVINALLARRGGQSKACPVGNEAGVTTSLREIKIDNKLKILDSPGICFPSENKKRSKVEHEAELALLNALPAKHIVDPYPAVLMLVKRLAKSDEMTESFKKLYEIPPIPANDADTFTKHFLIHVARKRGRLGKGGIPNLASAGLSVLNDWRDGKILGWVLPNTSAAASQQDKQNLSTINTGTKQAPIAANESTIVSEWSKEFDLDGLFSSLDKAIDASKDQDTMME
Protein: VirB4 homolog (VirB4) (O24862)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- TrbI protein
- Cag pathogenicity island protein
- Conjugative transfer regulon protein
- Conjugal transfer protein
- Competence protein ComB
- Competence protein ComB
- VirB11 homolog
- Cag pathogenicity island protein
- Conjugal transfer protein
Sequence:
MLEKLLSAIKQKVSNYFLGVLPKSYSMSEENNILGLYDEHFLLTKNENLVGILRLEGVSYTHLSTEQLQDLFTERQMALDSLEKVVARLVVKRRKIDHQQNIQSDSQYLQAILNQFENKEVYENQYFLVLESTHSLHGVLEHKKKSLMHANRENFKDILSYKAHFLQETLKSLEIQLKNYAPKLLSSKEVLNFYAEYINGFDLPLKPLVGGYLSDSYIASSITFEKDYFIQESFNQKTYNRLIGIKAYESERITSIAIGALLYQETPLDIIFSIEPMSVHKTLSFLKERAKFSMSNLVKNELLEYQELVKTKRLSMQKFALNILIKAPSLENLDAQTSLVLGLLFKENLVGVIETFGLKGGYFSFFPERIHLNHRLRFLTSKALACLMVFERQNLGFKANSWGNSPLSVFKNLDYSPFLFNFHNQEVSHKNAKEIARVNGHTLIIGATGSGKSTLISFLMMSALKYQNMRLLAFDRMQGLYSFTKFFKGHYHDGQSFSINPFCLEPNLQNLEFLQSFFLSMFDLAPSRDKEALEDMNAISSAIKSLYETLYPKAFSLLDFKETLKRTSSNQLGLSLEPYLNNPLFNALNDAFNSNAFLNVINLDTITQNPKDLGLLAYYLFYKILEESRKNDSGFLVFLDEFKSYVENDLLNTKINALITQARKANGVVVLALQDIYQLSGVKNAHSFLSNMGTLILYPQKNARELKHNFNVPLSETEISFLENTPLYARQVLVKNLGNGSSNMIDVSLESLGRYLKIFNSDSSHVSKVKALQKDYPTEWREKLLRS
Protein: Protein Mis18-alpha (FAPP1-associated protein 1) (Q9NYP9)
Organism: Homo sapiens (Human)
Function: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17199038}. Chromosome {ECO:0000269|PubMed:17199038}. Chromosome, centromere {ECO:0000269|PubMed:17199038}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin.
Interaction partners:
- Mis18-binding protein 1
- Protein Mis18-beta
- Holliday junction recognition protein
- Histone H3-like centromeric protein A
- Centromere protein C
- Histone-binding protein RBBP7
- Centromere protein I
- Centromere protein W
- Centromere protein K
- Centromere protein Q
Sequence:
MAGVRSLRCSRGCAGGCECGDKGKCSDSSLLGKRLSEDSSRHQLLQKWASMWSSMSEDASVADMERAQLEEEAAAAEERPLVFLCSGCRRPLGDSLSWVASQEDTNCILLRCVSCNVSVDKEQKLSKREKENGCVLETLCCAGCSLNLGYVYRCTPKNLDYKRDLFCLSVEAIESYVLGSSEKQIVSEDKELFNLESRVEIEKSLTQMEDVLKALQMKLWEAESKLSFATCKS
Protein: Anaphase-promoting complex subunit 2 (APC2) (Cyclosome subunit 2) (Q9UJX6)
Organism: Homo sapiens (Human)
Function: Together with the RING-H2 protein ANAPC11, constitutes the catalytic component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 drives presynaptic differentiation.
Interaction partners:
- Anaphase-promoting complex subunit 11
- Cell division cycle protein 16 homolog
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 23 homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Anaphase-promoting complex subunit CDC26
- Cell division cycle protein 27 homolog
- Fizzy-related protein homolog
Sequence:
MAAAVVVAEGDSDSRPGQELLVAWNTVSTGLVPPAALGLVSSRTSGAVPPKEEELRAAVEVLRGHGLHSVLEEWFVEVLQNDLQANISPEFWNAISQCENSADEPQCLLLLLDAFGLLESRLDPYLRSLELLEKWTRLGLLMGTGAQGLREEVHTMLRGVLFFSTPRTFQEMIQRLYGCFLRVYMQSKRKGEGGTDPELEGELDSRYARRRYYRLLQSPLCAGCSSDKQQCWCRQALEQFHQLSQVLHRLSLLERVSAEAVTTTLHQVTRERMEDRCRGEYERSFLREFHKWIERVVGWLGKVFLQDGPARPASPEAGNTLRRWRCHVQRFFYRIYASLRIEELFSIVRDFPDSRPAIEDLKYCLERTDQRQQLLVSLKAALETRLLHPGVNTCDIITLYISAIKALRVLDPSMVILEVACEPIRRYLRTREDTVRQIVAGLTGDSDGTGDLAVELSKTDPASLETGQDSEDDSGEPEDWVPDPVDADPGKSSSKRRSSDIISLLVSIYGSKDLFINEYRSLLADRLLHQFSFSPEREIRNVELLKLRFGEAPMHFCEVMLKDMADSRRINANIREEDEKRPAEEQPPFGVYAVILSSEFWPPFKDEKLEVPEDIRAALEAYCKKYEQLKAMRTLSWKHTLGLVTMDVELADRTLSVAVTPVQAVILLYFQDQASWTLEELSKAVKMPVALLRRRMSVWLQQGVLREEPPGTFSVIEEERPQDRDNMVLIDSDDESDSGMASQADQKEEELLLFWTYIQAMLTNLESLSLDRIYNMLRMFVVTGPALAEIDLQELQGYLQKKVRDQQLVYSAGVYRLPKNCS
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, mitochondrial (EC 1.1.1.8) (P41911)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism.
Subcellular location: Cytoplasm. Mitochondrion.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Glycerol-3-phosphate O-acyltransferase 1
- Glycerol-3-phosphate O-acyltransferase 2
- Dihydroxyacetone kinase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Dihydroxyacetone kinase 2
- Lipid phosphate phosphatase 1
- Diacylglycerol pyrophosphate phosphatase 1
- Lysophospholipid acyltransferase
Sequence:
MLAVRRLTRYTFLKRTHPVLYTRRAYKILPSRSTFLRRSLLQTQLHSKMTAHTNIKQHKHCHEDHPIRRSDSAVSIVHLKRAPFKVTVIGSGNWGTTIAKVIAENTELHSHIFEPEVRMWVFDEKIGDENLTDIINTRHQNVKYLPNIDLPHNLVADPDLLHSIKGADILVFNIPHQFLPNIVKQLQGHVAPHVRAISCLKGFELGSKGVQLLSSYVTDELGIQCGALSGANLAPEVAKEHWSETTVAYQLPKDYQGDGKDVDHKILKLLFHRPYFHVNVIDDVAGISIAGALKNVVALACGFVEGMGWGNNASAAIQRLGLGEIIKFGRMFFPESKVETYYQESAGVADLITTCSGGRNVKVATYMAKTGKSALEAEKELLNGQSAQGIITCREVHEWLQTCELTQEFPLFEAVYQIVYNNVRMEDLPEMIEELDIDDE
Protein: Matrin-type domain-containing protein (Q22469)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PSP proline-rich domain-containing protein
- Splicing factor 3A subunit 2
- Pre-RNA processing 21
- Splicing factor 3B subunit 3
- Probable U2 small nuclear ribonucleoprotein A'
- Cell division cycle 5-like protein
- Splicing factor 3B subunit 4
- Pre-mRNA-splicing factor SYF1
- RNA helicase
- Pre-mRNA-processing factor 19
Sequence:
MDSCLETIRNLHEERERLIDITVKEKIAEKLTHKAKVNSEQRVKTFVDRYYSVSAELAKFYKDEDGSKSMEMDSVSGPNEFAEFYSRLKVIKDAHRRNPDELAEPLTVEFQKINEEIINPERAEPDMVEFSDEEAYGRFLDLHAQYDKFINLKNIKRVDYMTYLLNFEKFTEIPKNTTKKTGAYKEYINSLKDYLVSFMQRTRPLHDLDSVFSEVNQTVERAFKAGNLPGWEADKNKNGPQAAAVDLSPYNSAEELEGLGLERLKGALMAIGLKCGGTLKERADRLFATKGHKLSDLEKAAMSSNNSDAEKQNAKNLTLAQTEAHIMALADILAEERTGTRENVERKQARSAGEVEEEEEEEIVIEEEEEIDESAPYNPKNLPLGWDGKPIPYWLYKLHGLNLSYSCEICGNQTYKGPKAFQKHFNEWRHSHGMRCLGIPNTSHFANITKIKDALDLWNKLKTEKEMAKWNPDIDEEYEDSSGNVVTRKMYEDLKRQGLL
Protein: Beta-hexosaminidase subunit beta (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit beta) (Hexosaminidase subunit B) (Cervical cancer proto-oncogene 7 protein) (HCC-7) (N-acetyl-beta-glucosaminidase subunit beta) [Cleaved into: Beta-hexosaminidase subunit beta chain B; Beta-hexosaminidase subunit beta chain A] (P07686)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A. During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity).
Subcellular location: Lysosome {ECO:0000269|PubMed:9694901}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:P20060}.
Interaction partners:
- Beta-hexosaminidase subunit alpha
- Beta-galactosidase
- Ganglioside GM2 activator
- Alpha-N-acetylgalactosaminidase
- N-acetylglucosamine-6-sulfatase
- Alpha-galactosidase A
- Chitotriosidase-1
- Acidic mammalian chitinase
- Hexosaminidase D
- Beta-1,4 N-acetylgalactosaminyltransferase 1
Sequence:
MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTJ1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Ubiquitin-activating enzyme E1 1
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
Sequence:
MSKQWADGKDGVFRRQVSSFRETISNSHPVFKPAKGRYWLYVCLACPWAHRTLIARALKGLTSAIGVSVVHWHLDEKGWRFLQGDAQELLAGKAYEIAGGIEGANSDVSTRVGDIKNDSERLFVDGSVEPHHHFERLSELYLKSNPDYKDRFTVPVLWDTETQTIVNNESSEIIRILNSDAFDQFRDSDAEVPDLVPKELEAEIDEVNKWTYDNINNGVYKAGFSENGSNYEDEVTNVFTHLDKVESLLADKYKKLEKELGDKAKILSKYFIVGNQITETDIRLYTTIVRFDPVYVQHFKCNFTSIREGYPYIHLWLQNLYWNYPAFGKTTDFNHIKLHYTRSHPRINPLGLTPLGPKPDIRPL
Protein: Mitochondrial outer membrane protein porin (Cytoplasmic antigenic protein 4) (P83781)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Forms a channel through the cell membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}.
Interaction partners:
- Translocase of outer membrane 40 kDa subunit
- Mitochondrial import receptor subunit TOM20
- Protein channel
- Mitofusin
- Tom22p
- Mitochondrial Rho GTPase 1
- SAM complex subunit
- asparagine synthase
- Mitochondrial distribution and morphology protein 10
- Autophagy protein 5
Sequence:
MAPAAYSDLSKASNDLINKDFYHLSTAAVDVKTVAPNGVTFTVKGKTTKDDTISASVDAKYLDKATGLTLTQGWNNANALNTKIELSELLTPGLKGELDTSVVPNGARNAKLNFFYQQSAVNARLFFDLLKGPIATADLVVAHDGFTAGAELGYDISSAKVNKYSVGVGYANLNYGLAATATSNLSVFSAAYFHKVSPLVQVGAKATWDSIKSSNVNVEFATKYALDNTSFIKAKIADSGLTALSYTQELRPGVKLGLGASFDALKLAEPVHKLGFSLSFAA