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Q13201

- MMRN1_HUMAN

UniProt

Q13201 - MMRN1_HUMAN

Protein

Multimerin-1

Gene

MMRN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein.3 Publications

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell adhesion Source: ProtInc
    3. platelet activation Source: Reactome
    4. platelet degranulation Source: Reactome

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multimerin-1
    Alternative name(s):
    EMILIN-4
    Elastin microfibril interface located protein 4
    Short name:
    Elastin microfibril interfacer 4
    Endothelial cell multimerin
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MMRN1
    Synonyms:ECM, EMILIN4, GPIA*, MMRN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:7178. MMRN1.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Deficiency in multimerin-1 due to proteolytic degradation within the platelet alpha granules is associated with an autosomal dominant bleeding disorder (factor V Quebec).1 Publication

    Organism-specific databases

    PharmGKBiPA30891.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 12281209Multimerin-1PRO_0000007821Add
    BLAST
    Chaini184 – 12281045Platelet glycoprotein Ia*PRO_0000367047Add
    BLAST
    Chaini318 – 1228911155 kDa platelet multimerinPRO_0000367048Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi21 – 211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi114 – 1141N-linked (GlcNAc...)2 Publications
    Glycosylationi120 – 1201N-linked (GlcNAc...)1 Publication
    Glycosylationi136 – 1361N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi211 ↔ 272By similarity
    Disulfide bondi238 ↔ 245By similarity
    Disulfide bondi271 ↔ 280By similarity
    Glycosylationi344 – 3441N-linked (GlcNAc...)1 Publication
    Glycosylationi431 – 4311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi507 – 5071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi576 – 5761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi618 – 6181N-linked (GlcNAc...)1 Publication
    Glycosylationi680 – 6801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi729 – 7291N-linked (GlcNAc...)2 Publications
    Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi816 – 8161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi840 – 8401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi921 – 9211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi933 – 9331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi942 – 9421N-linked (GlcNAc...)1 Publication
    Glycosylationi981 – 9811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1020 – 10201N-linked (GlcNAc...)1 Publication
    Disulfide bondi1045 ↔ 1056By similarity
    Disulfide bondi1050 ↔ 1065By similarity
    Disulfide bondi1067 ↔ 1076By similarity
    Glycosylationi1075 – 10751N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.
    Extensively N-glycosylated.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ13201.
    PRIDEiQ13201.

    2D gel databases

    OGPiQ13201.

    PTM databases

    PhosphoSiteiQ13201.

    Expressioni

    Tissue specificityi

    Synthesized by endothelial cells and megakaryocytes. Stored in platelet alpha granules and endothelial cell Weibel-Palade bodies, following activation of these cells, it is released and attached to megakaryocytes, platelets, endothelium and subendothelium of blood vessels. Not found in plasma. Found in vascular tissues such as placenta, lung, and liver.2 Publications

    Gene expression databases

    ArrayExpressiQ13201.
    BgeeiQ13201.
    CleanExiHS_MMRN1.
    GenevestigatoriQ13201.

    Organism-specific databases

    HPAiHPA035769.

    Interactioni

    Subunit structurei

    Multimeric. Composed of varying sized, disulfide-linked multimers, the smallest of which is a homotrimer. Proteolysis of the promultimerin in the N-terminal region, leads to the mature p155 form that is stored in platelets. Interacts with factor V/Va.3 Publications

    Protein-protein interaction databases

    BioGridi116577. 1 interaction.
    IntActiQ13201. 1 interaction.
    STRINGi9606.ENSP00000264790.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13201.
    SMRiQ13201. Positions 1100-1227.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini207 – 28276EMIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1041 – 107737EGF-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini1096 – 1228133C1qPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili333 – 36533Sequence AnalysisAdd
    BLAST
    Coiled coili400 – 43031Sequence AnalysisAdd
    BLAST
    Coiled coili503 – 52321Sequence AnalysisAdd
    BLAST
    Coiled coili580 – 65071Sequence AnalysisAdd
    BLAST
    Coiled coili675 – 72652Sequence AnalysisAdd
    BLAST
    Coiled coili819 – 86951Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi186 – 1883Cell attachment siteSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi189 – 1924Poly-Ser
    Compositional biasi309 – 3135Poly-Gln

    Sequence similaritiesi

    Contains 1 C1q domain.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 EMI domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, EGF-like domain, Signal

    Phylogenomic databases

    eggNOGiNOG45481.
    HOGENOMiHOG000113610.
    HOVERGENiHBG108139.
    InParanoidiQ13201.
    OMAiCACRHPF.
    OrthoDBiEOG7CCBQ6.
    PhylomeDBiQ13201.
    TreeFamiTF336041.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR001073. C1q.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR011489. EMI_domain.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00386. C1q. 1 hit.
    PF00008. EGF. 1 hit.
    PF07546. EMI. 1 hit.
    [Graphical view]
    PRINTSiPR00007. COMPLEMNTC1Q.
    SMARTiSM00110. C1Q. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50871. C1Q. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS51041. EMI. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13201-1) [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

    MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ     50
    SLQILPTTRV MSAEIATTPE ARTSEDSLLK STLPPSETSA PAEGVRNQTL 100
    TSTEKAEGVV KLQNLTLPTN ASIKFNPGAE SVVLSNSTLK FLQSFARKSN 150
    EQATSLNTVG GTGGIGGVGG TGGVGNRAPR ETYLSRGDSS SSQRTDYQKS 200
    NFETTRGKNW CAYVHTRLSP TVILDNQVTY VPGGKGPCGW TGGSCPQRSQ 250
    KISNPVYRMQ HKIVTSLDWR CCPGYSGPKC QLRAQEQQSL IHTNQAESHT 300
    AVGRGVAEQQ QQQGCGDPEV MQKMTDQVNY QAMKLTLLQK KIDNISLTVN 350
    DVRNTYSSLE GKVSEDKSRE FQSLLKGLKS KSINVLIRDI VREQFKIFQN 400
    DMQETVAQLF KTVSSLSEDL ESTRQIIQKV NESVVSIAAQ QKFVLVQENR 450
    PTLTDIVELR NHIVNVRQEM TLTCEKPIKE LEVKQTHLEG ALEQEHSRSI 500
    LYYESLNKTL SKLKEVHEQL LSTEQVSDQK NAPAAESVSN NVTEYMSTLH 550
    ENIKKQSLMM LQMFEDLHIQ ESKINNLTVS LEMEKESLRG ECEDMLSKCR 600
    NDFKFQLKDT EENLHVLNQT LAEVLFPMDN KMDKMSEQLN DLTYDMEILQ 650
    PLLEQGASLR QTMTYEQPKE AIVIRKKIEN LTSAVNSLNF IIKELTKRHN 700
    LLRNEVQGRD DALERRINEY ALEMEDGLNK TMTIINNAID FIQDNYALKE 750
    TLSTIKDNSE IHHKCTSDME TILTFIPQFH RLNDSIQTLV NDNQRYNFVL 800
    QVAKTLAGIP RDEKLNQSNF QKMYQMFNET TSQVRKYQQN MSHLEEKLLL 850
    TTKISKNFET RLQDIESKVT QTLIPYYISV KKGSVVTNER DQALQLQVLN 900
    SRFKALEAKS IHLSINFFSL NKTLHEVLTM CHNASTSVSE LNATIPKWIK 950
    HSLPDIQLLQ KGLTEFVEPI IQIKTQAALS NLTCCIDRSL PGSLANVVKS 1000
    QKQVKSLPKK INALKKPTVN LTTVLIGRTQ RNTDNIIYPE EYSSCSRHPC 1050
    QNGGTCINGR TSFTCACRHP FTGDNCTIKL VEENALAPDF SKGSYRYAPM 1100
    VAFFASHTYG MTIPGPILFN NLDVNYGASY TPRTGKFRIP YLGVYVFKYT 1150
    IESFSAHISG FLVVDGIDKL AFESENINSE IHCDRVLTGD ALLELNYGQE 1200
    VWLRLAKGTI PAKFPPVTTF SGYLLYRT 1228
    Length:1,228
    Mass (Da):138,110
    Last modified:April 3, 2007 - v3
    Checksum:i270BCFBE85AA2F8F
    GO
    Isoform 2 (identifier: Q13201-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         71-104: Missing.
         377-1039: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:531
    Mass (Da):58,170
    Checksum:i80974ECCBAA1F993
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti217 – 2171R → K in BAC86201. (PubMed:14702039)Curated
    Sequence conflicti223 – 2231I → T in AAC52065. (PubMed:7629143)Curated
    Sequence conflicti982 – 9821L → S in AAC52065. (PubMed:7629143)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581T → A.
    Corresponds to variant rs1442138 [ dbSNP | Ensembl ].
    VAR_031471
    Natural varianti805 – 8051T → A.
    Corresponds to variant rs3756065 [ dbSNP | Ensembl ].
    VAR_031472
    Natural varianti883 – 8831G → D.
    Corresponds to variant rs12646270 [ dbSNP | Ensembl ].
    VAR_031473
    Natural varianti964 – 9641T → R.1 Publication
    Corresponds to variant rs17855885 [ dbSNP | Ensembl ].
    VAR_031474

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei71 – 10434Missing in isoform 2. 1 PublicationVSP_036610Add
    BLAST
    Alternative sequencei377 – 1039663Missing in isoform 2. 1 PublicationVSP_036611Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27109 mRNA. Translation: AAC52065.1.
    AK125557 mRNA. Translation: BAC86201.1.
    AK313566 mRNA. Translation: BAG36340.1.
    AC093759 Genomic DNA. Translation: AAY40957.1.
    CH471057 Genomic DNA. Translation: EAX06038.1.
    BC063848 mRNA. Translation: AAH63848.1.
    CCDSiCCDS3635.1. [Q13201-1]
    PIRiA57384.
    RefSeqiNP_031377.2. NM_007351.2. [Q13201-1]
    UniGeneiHs.268107.

    Genome annotation databases

    EnsembliENST00000264790; ENSP00000264790; ENSG00000138722. [Q13201-1]
    ENST00000394980; ENSP00000378431; ENSG00000138722. [Q13201-1]
    GeneIDi22915.
    KEGGihsa:22915.
    UCSCiuc003hst.3. human. [Q13201-1]
    uc010iku.3. human. [Q13201-2]

    Polymorphism databases

    DMDMi143811421.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27109 mRNA. Translation: AAC52065.1 .
    AK125557 mRNA. Translation: BAC86201.1 .
    AK313566 mRNA. Translation: BAG36340.1 .
    AC093759 Genomic DNA. Translation: AAY40957.1 .
    CH471057 Genomic DNA. Translation: EAX06038.1 .
    BC063848 mRNA. Translation: AAH63848.1 .
    CCDSi CCDS3635.1. [Q13201-1 ]
    PIRi A57384.
    RefSeqi NP_031377.2. NM_007351.2. [Q13201-1 ]
    UniGenei Hs.268107.

    3D structure databases

    ProteinModelPortali Q13201.
    SMRi Q13201. Positions 1100-1227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116577. 1 interaction.
    IntActi Q13201. 1 interaction.
    STRINGi 9606.ENSP00000264790.

    PTM databases

    PhosphoSitei Q13201.

    Polymorphism databases

    DMDMi 143811421.

    2D gel databases

    OGPi Q13201.

    Proteomic databases

    PaxDbi Q13201.
    PRIDEi Q13201.

    Protocols and materials databases

    DNASUi 22915.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264790 ; ENSP00000264790 ; ENSG00000138722 . [Q13201-1 ]
    ENST00000394980 ; ENSP00000378431 ; ENSG00000138722 . [Q13201-1 ]
    GeneIDi 22915.
    KEGGi hsa:22915.
    UCSCi uc003hst.3. human. [Q13201-1 ]
    uc010iku.3. human. [Q13201-2 ]

    Organism-specific databases

    CTDi 22915.
    GeneCardsi GC04P090800.
    H-InvDB HIX0024584.
    HGNCi HGNC:7178. MMRN1.
    HPAi HPA035769.
    MIMi 601456. gene.
    neXtProti NX_Q13201.
    PharmGKBi PA30891.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45481.
    HOGENOMi HOG000113610.
    HOVERGENi HBG108139.
    InParanoidi Q13201.
    OMAi CACRHPF.
    OrthoDBi EOG7CCBQ6.
    PhylomeDBi Q13201.
    TreeFami TF336041.

    Miscellaneous databases

    GeneWikii MMRN1.
    GenomeRNAii 22915.
    NextBioi 43599.
    PROi Q13201.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13201.
    Bgeei Q13201.
    CleanExi HS_MMRN1.
    Genevestigatori Q13201.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR011489. EMI_domain.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF00008. EGF. 1 hit.
    PF07546. EMI. 1 hit.
    [Graphical view ]
    PRINTSi PR00007. COMPLEMNTC1Q.
    SMARTi SM00110. C1Q. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS51041. EMI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cDNA sequence of human endothelial cell multimerin. A unique protein with RGDS, coiled-coil, and epidermal growth factor-like domains and a carboxyl terminus similar to the globular domain of complement C1q and collagens type VIII and X."
      Hayward C.P.M., Hassell J.A., Denomme G.A., Rachubinski R.A., Brown C., Kelton J.G.
      J. Biol. Chem. 270:18246-18251(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 368-376, FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Endothelial cell.
    2. "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] (ISOFORMS 1 AND 2).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1), VARIANT ARG-964.
      Tissue: PNS.
    6. "Platelet glycoprotein Ia* is the processed form of multimerin --isolation and determination of N-terminal sequences of stored and released forms."
      Polgar J., Magnenat E., Wells T.N.C., Clemetson K.J.
      Thromb. Haemost. 80:645-648(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 184-198 AND 318-326.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 461-467.
      Tissue: Platelet.
    8. "Multimerin is found in the alpha-granules of resting platelets and is synthesized by a megakaryocytic cell line."
      Hayward C.P.M., Bainton D.F., Smith J.W., Horsewood P., Stead R.H., Podor T.J., Warkentin T.E., Kelton J.G.
      J. Clin. Invest. 91:2630-2639(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Platelet multimerin and its proteolytic processing."
      Hayward C.P.M.
      Thromb. Haemost. 82:1779-1780(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-120; ASN-136; ASN-618 AND ASN-729.
      Tissue: Plasma.
    11. "Analyses of cellular multimerin 1 receptors: in vitro evidence of binding mediated by alphaIIbbeta3 and alphavbeta3."
      Adam F., Zheng S., Joshi N., Kelton D.S., Sandhu A., Suehiro Y., Jeimy S.B., Santos A.V., Masse J.-M., Kelton J.G., Cramer E.M., Hayward C.P.M.
      Thromb. Haemost. 94:1004-1011(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114.
      Tissue: Platelet.
    13. "Multimerin 1 binds factor V and activated factor V with high affinity and inhibits thrombin generation."
      Jeimy S.B., Fuller N., Tasneem S., Segers K., Stafford A.R., Weitz J.I., Camire R.M., Nicolaes G.A.F., Hayward C.P.M.
      Thromb. Haemost. 100:1058-1067(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FACTOR V.
    14. "An autosomal dominant, qualitative platelet disorder associated with multimerin deficiency, abnormalities in platelet factor V, thrombospondin, von Willebrand factor, and fibrinogen and an epinephrine aggregation defect."
      Hayward C.P.M., Rivard G.E., Kane W.H., Drouin J., Zheng S., Moore J.C., Kelton J.G.
      Blood 87:4967-4978(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE.
    15. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-344; ASN-729; ASN-942 AND ASN-1020.
      Tissue: Liver.
    16. Cited for: GLYCOSYLATION AT ASN-136.

    Entry informationi

    Entry nameiMMRN1_HUMAN
    AccessioniPrimary (citable) accession number: Q13201
    Secondary accession number(s): Q4W5L1, Q6P3T8, Q6ZUL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3