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Q13201

- MMRN1_HUMAN

UniProt

Q13201 - MMRN1_HUMAN

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Protein

Multimerin-1

Gene

MMRN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

MaxQBiQ13201.
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

BgeeiQ13201.
CleanExiHS_MMRN1.
ExpressionAtlasiQ13201. baseline and differential.
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. 13 interactions.
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.
GeneTreeiENSGT00660000095560.
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

        10         20         30         40         50
MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ
60 70 80 90 100
SLQILPTTRV MSAEIATTPE ARTSEDSLLK STLPPSETSA PAEGVRNQTL
110 120 130 140 150
TSTEKAEGVV KLQNLTLPTN ASIKFNPGAE SVVLSNSTLK FLQSFARKSN
160 170 180 190 200
EQATSLNTVG GTGGIGGVGG TGGVGNRAPR ETYLSRGDSS SSQRTDYQKS
210 220 230 240 250
NFETTRGKNW CAYVHTRLSP TVILDNQVTY VPGGKGPCGW TGGSCPQRSQ
260 270 280 290 300
KISNPVYRMQ HKIVTSLDWR CCPGYSGPKC QLRAQEQQSL IHTNQAESHT
310 320 330 340 350
AVGRGVAEQQ QQQGCGDPEV MQKMTDQVNY QAMKLTLLQK KIDNISLTVN
360 370 380 390 400
DVRNTYSSLE GKVSEDKSRE FQSLLKGLKS KSINVLIRDI VREQFKIFQN
410 420 430 440 450
DMQETVAQLF KTVSSLSEDL ESTRQIIQKV NESVVSIAAQ QKFVLVQENR
460 470 480 490 500
PTLTDIVELR NHIVNVRQEM TLTCEKPIKE LEVKQTHLEG ALEQEHSRSI
510 520 530 540 550
LYYESLNKTL SKLKEVHEQL LSTEQVSDQK NAPAAESVSN NVTEYMSTLH
560 570 580 590 600
ENIKKQSLMM LQMFEDLHIQ ESKINNLTVS LEMEKESLRG ECEDMLSKCR
610 620 630 640 650
NDFKFQLKDT EENLHVLNQT LAEVLFPMDN KMDKMSEQLN DLTYDMEILQ
660 670 680 690 700
PLLEQGASLR QTMTYEQPKE AIVIRKKIEN LTSAVNSLNF IIKELTKRHN
710 720 730 740 750
LLRNEVQGRD DALERRINEY ALEMEDGLNK TMTIINNAID FIQDNYALKE
760 770 780 790 800
TLSTIKDNSE IHHKCTSDME TILTFIPQFH RLNDSIQTLV NDNQRYNFVL
810 820 830 840 850
QVAKTLAGIP RDEKLNQSNF QKMYQMFNET TSQVRKYQQN MSHLEEKLLL
860 870 880 890 900
TTKISKNFET RLQDIESKVT QTLIPYYISV KKGSVVTNER DQALQLQVLN
910 920 930 940 950
SRFKALEAKS IHLSINFFSL NKTLHEVLTM CHNASTSVSE LNATIPKWIK
960 970 980 990 1000
HSLPDIQLLQ KGLTEFVEPI IQIKTQAALS NLTCCIDRSL PGSLANVVKS
1010 1020 1030 1040 1050
QKQVKSLPKK INALKKPTVN LTTVLIGRTQ RNTDNIIYPE EYSSCSRHPC
1060 1070 1080 1090 1100
QNGGTCINGR TSFTCACRHP FTGDNCTIKL VEENALAPDF SKGSYRYAPM
1110 1120 1130 1140 1150
VAFFASHTYG MTIPGPILFN NLDVNYGASY TPRTGKFRIP YLGVYVFKYT
1160 1170 1180 1190 1200
IESFSAHISG FLVVDGIDKL AFESENINSE IHCDRVLTGD ALLELNYGQE
1210 1220
VWLRLAKGTI PAKFPPVTTF SGYLLYRT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 13 interactions.
IntActi Q13201. 1 interaction.
STRINGi 9606.ENSP00000264790.

PTM databases

PhosphoSitei Q13201.

Polymorphism databases

DMDMi 143811421.

2D gel databases

OGPi Q13201.

Proteomic databases

MaxQBi Q13201.
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.
GeneTreei ENSGT00660000095560.
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

Bgeei Q13201.
CleanExi HS_MMRN1.
ExpressionAtlasi Q13201. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 137 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