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Q68CJ9

- CR3L3_HUMAN

UniProt

Q68CJ9 - CR3L3_HUMAN

Protein

Cyclic AMP-responsive element-binding protein 3-like protein 3

Gene

CREB3L3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
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    Functioni

    Transcription factor that may act during endoplasmic reticulum stress by activating unfolded protein response target genes. Activated in response to cAMP stimulation. In vitro, binds to the cAMP response element (CRE) and box-B element. Activates transcription through box-B element. Activates transcription through CRE By similarity. Seems to function synergistically with ATF6. In acute inflammatory response, may activate expression of acute phase response (APR) genes. May be involved in growth suppression.By similarity3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei363 – 3642Cleavage; by PS1By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
    3. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB

    GO - Biological processi

    1. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    2. response to unfolded protein Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation, Unfolded protein response

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic AMP-responsive element-binding protein 3-like protein 3
    Short name:
    cAMP-responsive element-binding protein 3-like protein 3
    Alternative name(s):
    Transcription factor CREB-H
    Cleaved into the following chain:
    Gene namesi
    Name:CREB3L3
    Synonyms:CREBH
    ORF Names:HYST1481
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:18855. CREB3L3.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Chain Processed cyclic AMP-responsive element-binding protein 3-like protein 3 : Nucleus
    Note: Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi361 – 3611R → A: Decreases proteolytic cleavage upon ER stress. 1 Publication

    Organism-specific databases

    Orphaneti70470. Hyperlipoproteinemia type 5.
    PharmGKBiPA134882161.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Cyclic AMP-responsive element-binding protein 3-like protein 3PRO_0000288074Add
    BLAST
    Chaini1 – ?Processed cyclic AMP-responsive element-binding protein 3-like protein 3PRO_0000296216

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi379 – 3791O-linked (GalNAc...)1 Publication
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi413 – 4131N-linked (GlcNAc...)1 Publication
    Glycosylationi420 – 4201N-linked (GlcNAc...)1 Publication
    Glycosylationi427 – 4271N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Controlled by regulated intramembrane proteolysis (RIP). Following ER stress a fragment containing the cytoplasmic transcription factor domain is released by proteolysis. The cleavage seems to be performed sequentially by site-1 and site-2 proteases (PS1 and PS2).1 Publication
    N- and O-glycosylated. N-glycosylation is required for optimal proteolytic activation. O-glycosylated with core 1 or possibly core 8 glycans.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ68CJ9.
    PRIDEiQ68CJ9.

    PTM databases

    PhosphoSiteiQ68CJ9.

    Expressioni

    Tissue specificityi

    Exclusively expressed in liver. Underexpressed in hepatocellular carcinoma tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ68CJ9.
    BgeeiQ68CJ9.
    CleanExiHS_CREB3L3.
    GenevestigatoriQ68CJ9.

    Organism-specific databases

    HPAiHPA040671.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer By similarity. Probably homodimerizes. Probably forms a heterodimer with ATF6. Interacts with ATF6.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATF6P188502EBI-852194,EBI-852157

    Protein-protein interaction databases

    BioGridi124213. 10 interactions.
    IntActiQ68CJ9. 7 interactions.
    MINTiMINT-2877373.
    STRINGi9606.ENSP00000078445.

    Structurei

    3D structure databases

    ProteinModelPortaliQ68CJ9.
    SMRiQ68CJ9. Positions 249-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 322322CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini344 – 461118LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei323 – 34321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini243 – 30664bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni245 – 27430Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni285 – 30622Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family. ATF subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG288874.
    HOGENOMiHOG000059566.
    HOVERGENiHBG090496.
    InParanoidiQ68CJ9.
    KOiK09048.
    OMAiDLEMWSP.
    OrthoDBiEOG7KM5SZ.
    PhylomeDBiQ68CJ9.
    TreeFamiTF316079.

    Family and domain databases

    InterProiIPR004827. bZIP.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q68CJ9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNTDLAAGKM ASAACSMDPI DSFELLDLLF DRQDGILRHV ELGEGWGHVK    50
    DQQVLPNPDS DDFLSSILGS GDSLPSSPLW SPEGSDSGIS EDLPSDPQDT 100
    PPRSGPATSP AGCHPAQPGK GPCLSYHPGN SCSTTTPGPV IQVPEASVTI 150
    DLEMWSPGGR ICAEKPADPV DLSPRCNLTV KDLLLSGSSG DLQQHHLGAS 200
    YLLRPGAGHC QELVLTEDEK KLLAKEGITL PTQLPLTKYE ERVLKKIRRK 250
    IRNKQSAQES RKKKKEYIDG LETRMSACTA QNQELQRKVL HLEKQNLSLL 300
    EQLKKLQAIV VQSTSKSAQT GTCVAVLLLS FALIILPSIS PFGPNKTESP 350
    GDFAPVRVFS RTLHNDAASR VAADAVPGSE APGPRPEADT TREESPGSPG 400
    ADWGFQDTAN LTNSTEELDN ATLVLRNATE GLGQVALLDW VAPGPSTGSG 450
    RAGLEAAGDE L 461
    Length:461
    Mass (Da):49,077
    Last modified:May 29, 2007 - v2
    Checksum:iC40F5AA626661F80
    GO
    Isoform 2 (identifier: Q68CJ9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-53: Missing.

    Show »
    Length:460
    Mass (Da):48,949
    Checksum:i53E643AF4D09C329
    GO
    Isoform 3 (identifier: Q68CJ9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         193-194: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:459
    Mass (Da):48,821
    Checksum:iEBED4351D3DD72C3
    GO
    Isoform 4 (identifier: Q68CJ9-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         239-337: YEERVLKKIR...LLSFALIILP → DVSLHCSESG...AQRCCLPRGC
         338-461: Missing.

    Show »
    Length:337
    Mass (Da):35,845
    Checksum:i11A7E28F406DE1FC
    GO

    Sequence cautioni

    The sequence BAD18804.1 differs from that shown. Reason: Aberrant splicing.
    The sequence BAD18804.1 differs from that shown. Reason: Frameshift at position 445.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti437 – 4371L → P in BAD18804. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei53 – 531Missing in isoform 2. 1 PublicationVSP_025637
    Alternative sequencei193 – 1942Missing in isoform 3. 1 PublicationVSP_054876
    Alternative sequencei239 – 33799YEERV…LIILP → DVSLHCSESGVTEESLASRE AKPVPLGATEETPGHCGAVH QQVSPDRHLCRSPVAVLCPH HPPLHQPFWPQQNREPWGLC ACTSVLQNFAQRCCLPRGC in isoform 4. 1 PublicationVSP_055635Add
    BLAST
    Alternative sequencei338 – 461124Missing in isoform 4. 1 PublicationVSP_055636Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050902 mRNA. Translation: BAB47242.1.
    AB073612 mRNA. Translation: BAD38649.1.
    AK172839 mRNA. Translation: BAD18804.1. Sequence problems.
    AK313099 mRNA. Translation: BAG35923.1.
    AC016586 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW69260.1.
    BC101508 mRNA. Translation: AAI01509.1.
    BC101504 mRNA. Translation: AAI01505.1.
    BC143609 mRNA. Translation: AAI43610.1.
    BC143610 mRNA. No translation available.
    CCDSiCCDS12121.1. [Q68CJ9-1]
    CCDS62499.1. [Q68CJ9-4]
    CCDS62500.1. [Q68CJ9-2]
    RefSeqiNP_001258924.1. NM_001271995.1. [Q68CJ9-2]
    NP_001258925.1. NM_001271996.1. [Q68CJ9-4]
    NP_001258926.1. NM_001271997.1.
    NP_115996.1. NM_032607.2. [Q68CJ9-1]
    UniGeneiHs.247744.

    Genome annotation databases

    GeneIDi84699.
    KEGGihsa:84699.
    UCSCiuc002lzl.4. human. [Q68CJ9-1]
    uc002lzm.4. human. [Q68CJ9-2]

    Polymorphism databases

    DMDMi148886847.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050902 mRNA. Translation: BAB47242.1 .
    AB073612 mRNA. Translation: BAD38649.1 .
    AK172839 mRNA. Translation: BAD18804.1 . Sequence problems.
    AK313099 mRNA. Translation: BAG35923.1 .
    AC016586 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW69260.1 .
    BC101508 mRNA. Translation: AAI01509.1 .
    BC101504 mRNA. Translation: AAI01505.1 .
    BC143609 mRNA. Translation: AAI43610.1 .
    BC143610 mRNA. No translation available.
    CCDSi CCDS12121.1. [Q68CJ9-1 ]
    CCDS62499.1. [Q68CJ9-4 ]
    CCDS62500.1. [Q68CJ9-2 ]
    RefSeqi NP_001258924.1. NM_001271995.1. [Q68CJ9-2 ]
    NP_001258925.1. NM_001271996.1. [Q68CJ9-4 ]
    NP_001258926.1. NM_001271997.1.
    NP_115996.1. NM_032607.2. [Q68CJ9-1 ]
    UniGenei Hs.247744.

    3D structure databases

    ProteinModelPortali Q68CJ9.
    SMRi Q68CJ9. Positions 249-294.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124213. 10 interactions.
    IntActi Q68CJ9. 7 interactions.
    MINTi MINT-2877373.
    STRINGi 9606.ENSP00000078445.

    PTM databases

    PhosphoSitei Q68CJ9.

    Polymorphism databases

    DMDMi 148886847.

    Proteomic databases

    PaxDbi Q68CJ9.
    PRIDEi Q68CJ9.

    Protocols and materials databases

    DNASUi 84699.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 84699.
    KEGGi hsa:84699.
    UCSCi uc002lzl.4. human. [Q68CJ9-1 ]
    uc002lzm.4. human. [Q68CJ9-2 ]

    Organism-specific databases

    CTDi 84699.
    GeneCardsi GC19P004153.
    HGNCi HGNC:18855. CREB3L3.
    HPAi HPA040671.
    MIMi 611998. gene.
    neXtProti NX_Q68CJ9.
    Orphaneti 70470. Hyperlipoproteinemia type 5.
    PharmGKBi PA134882161.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288874.
    HOGENOMi HOG000059566.
    HOVERGENi HBG090496.
    InParanoidi Q68CJ9.
    KOi K09048.
    OMAi DLEMWSP.
    OrthoDBi EOG7KM5SZ.
    PhylomeDBi Q68CJ9.
    TreeFami TF316079.

    Miscellaneous databases

    GenomeRNAii 84699.
    NextBioi 35481244.
    PROi Q68CJ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q68CJ9.
    Bgeei Q68CJ9.
    CleanExi HS_CREB3L3.
    Genevestigatori Q68CJ9.

    Family and domain databases

    InterProi IPR004827. bZIP.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CREB-H: a novel mammalian transcription factor belonging to the CREB/ATF family and functioning via the box-B element with a liver-specific expression."
      Omori Y., Imai J., Watanabe M., Komatsu T., Suzuki Y., Kataoka K., Watanabe S., Tanigami A., Sugano S.
      Nucleic Acids Res. 29:2154-2162(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas."
      Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.
      Oncogene 23:5901-5911(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Ileal mucosa and Thalamus.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
      Tissue: Brain.
    7. "The liver-enriched transcription factor CREB-H is a growth suppressor protein underexpressed in hepatocellular carcinoma."
      Chin K.-T., Zhou H.-J., Wong C.-M., Lee J.M.-F., Chan C.-P., Qiang B.-Q., Yuan J.-G., Ng I.-O., Jin D.-Y.
      Nucleic Acids Res. 33:1859-1873(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response."
      Zhang K., Shen X., Wu J., Sakaki K., Saunders T., Rutkowski D.T., Back S.H., Kaufman R.J.
      Cell 124:587-599(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SELF-ASSOCIATION, INTERACTION WITH ATF6, MUTAGENESIS OF ARG-361.
    9. "N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H."
      Chan C.P., Mak T.Y., Chin K.T., Ng I.O., Jin D.Y.
      J. Cell Sci. 123:1438-1448(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-413; ASN-420 AND ASN-427.
    10. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-379, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCR3L3_HUMAN
    AccessioniPrimary (citable) accession number: Q68CJ9
    Secondary accession number(s): B2R7S6
    , B7ZL69, M0QYW7, Q6ZMC5, Q96TB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3