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Q13201 (MMRN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Platelet glycoprotein Ia*
  2. 155 kDa platelet multimerin
    Short name=p-155
    Short name=p155
Gene names
Name:MMRN1
Synonyms:ECM, EMILIN4, GPIA*, MMRN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.11 Ref.13

Subunit structure

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. Ref.1 Ref.9 Ref.13

Subcellular location

Secreted Potential.

Tissue specificity

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. Ref.1 Ref.8

Post-translational modification

The N-terminus is blocked.

Extensively N-glycosylated. Ref.16

Involvement in disease

Deficiency in multimerin-1 due to proteolytic degradation within the platelet alpha granules is associated with an autosomal dominant bleeding disorder (factor V Quebec). Ref.14

Sequence similarities

Contains 1 C1q domain.

Contains 1 EGF-like domain.

Contains 1 EMI domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13201-1)

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.
Isoform 2 (identifier: Q13201-2)

The sequence of this isoform differs from the canonical sequence as follows:
     71-104: Missing.
     377-1039: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 12281209Multimerin-1
PRO_0000007821
Chain184 – 12281045Platelet glycoprotein Ia*
PRO_0000367047
Chain318 – 1228911155 kDa platelet multimerin
PRO_0000367048

Regions

Domain207 – 28276EMI
Domain1041 – 107737EGF-like
Domain1096 – 1228133C1q
Coiled coil333 – 36533 Potential
Coiled coil400 – 43031 Potential
Coiled coil503 – 52321 Potential
Coiled coil580 – 65071 Potential
Coiled coil675 – 72652 Potential
Coiled coil819 – 86951 Potential
Motif186 – 1883Cell attachment site Potential
Compositional bias189 – 1924Poly-Ser
Compositional bias309 – 3135Poly-Gln

Amino acid modifications

Glycosylation211N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Ref.10 Ref.12
Glycosylation1201N-linked (GlcNAc...) Ref.10
Glycosylation1361N-linked (GlcNAc...) (complex) Ref.10 Ref.16
Glycosylation3441N-linked (GlcNAc...) Ref.15
Glycosylation4311N-linked (GlcNAc...) Potential
Glycosylation5071N-linked (GlcNAc...) Potential
Glycosylation5411N-linked (GlcNAc...) Potential
Glycosylation5761N-linked (GlcNAc...) Potential
Glycosylation6181N-linked (GlcNAc...) Ref.10
Glycosylation6801N-linked (GlcNAc...) Potential
Glycosylation7291N-linked (GlcNAc...) Ref.10 Ref.15
Glycosylation7831N-linked (GlcNAc...) Potential
Glycosylation8161N-linked (GlcNAc...) Potential
Glycosylation8281N-linked (GlcNAc...) Potential
Glycosylation8401N-linked (GlcNAc...) Potential
Glycosylation9211N-linked (GlcNAc...) Potential
Glycosylation9331N-linked (GlcNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Ref.15
Glycosylation9811N-linked (GlcNAc...) Potential
Glycosylation10201N-linked (GlcNAc...) Ref.15
Glycosylation10751N-linked (GlcNAc...) Potential
Disulfide bond211 ↔ 272 By similarity
Disulfide bond238 ↔ 245 By similarity
Disulfide bond271 ↔ 280 By similarity
Disulfide bond1045 ↔ 1056 By similarity
Disulfide bond1050 ↔ 1065 By similarity
Disulfide bond1067 ↔ 1076 By similarity

Natural variations

Alternative sequence71 – 10434Missing in isoform 2.
VSP_036610
Alternative sequence377 – 1039663Missing in isoform 2.
VSP_036611
Natural variant581T → A.
Corresponds to variant rs1442138 [ dbSNP | Ensembl ].
VAR_031471
Natural variant8051T → A.
Corresponds to variant rs3756065 [ dbSNP | Ensembl ].
VAR_031472
Natural variant8831G → D.
Corresponds to variant rs12646270 [ dbSNP | Ensembl ].
VAR_031473
Natural variant9641T → R. Ref.5
Corresponds to variant rs17855885 [ dbSNP | Ensembl ].
VAR_031474

Experimental info

Sequence conflict2171R → K in BAC86201. Ref.2
Sequence conflict2231I → T in AAC52065. Ref.1
Sequence conflict9821L → S in AAC52065. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 270BCFBE85AA2F8F

FASTA1,228138,110
        10         20         30         40         50         60 
MKGARLFVLL SSLWSGGIGL NNSKHSWTIP EDGNSQKTMP SASVPPNKIQ SLQILPTTRV 

        70         80         90        100        110        120 
MSAEIATTPE ARTSEDSLLK STLPPSETSA PAEGVRNQTL TSTEKAEGVV KLQNLTLPTN 

       130        140        150        160        170        180 
ASIKFNPGAE SVVLSNSTLK FLQSFARKSN EQATSLNTVG GTGGIGGVGG TGGVGNRAPR 

       190        200        210        220        230        240 
ETYLSRGDSS SSQRTDYQKS NFETTRGKNW CAYVHTRLSP TVILDNQVTY VPGGKGPCGW 

       250        260        270        280        290        300 
TGGSCPQRSQ KISNPVYRMQ HKIVTSLDWR CCPGYSGPKC QLRAQEQQSL IHTNQAESHT 

       310        320        330        340        350        360 
AVGRGVAEQQ QQQGCGDPEV MQKMTDQVNY QAMKLTLLQK KIDNISLTVN DVRNTYSSLE 

       370        380        390        400        410        420 
GKVSEDKSRE FQSLLKGLKS KSINVLIRDI VREQFKIFQN DMQETVAQLF KTVSSLSEDL 

       430        440        450        460        470        480 
ESTRQIIQKV NESVVSIAAQ QKFVLVQENR PTLTDIVELR NHIVNVRQEM TLTCEKPIKE 

       490        500        510        520        530        540 
LEVKQTHLEG ALEQEHSRSI LYYESLNKTL SKLKEVHEQL LSTEQVSDQK NAPAAESVSN 

       550        560        570        580        590        600 
NVTEYMSTLH ENIKKQSLMM LQMFEDLHIQ ESKINNLTVS LEMEKESLRG ECEDMLSKCR 

       610        620        630        640        650        660 
NDFKFQLKDT EENLHVLNQT LAEVLFPMDN KMDKMSEQLN DLTYDMEILQ PLLEQGASLR 

       670        680        690        700        710        720 
QTMTYEQPKE AIVIRKKIEN LTSAVNSLNF IIKELTKRHN LLRNEVQGRD DALERRINEY 

       730        740        750        760        770        780 
ALEMEDGLNK TMTIINNAID FIQDNYALKE TLSTIKDNSE IHHKCTSDME TILTFIPQFH 

       790        800        810        820        830        840 
RLNDSIQTLV NDNQRYNFVL QVAKTLAGIP RDEKLNQSNF QKMYQMFNET TSQVRKYQQN 

       850        860        870        880        890        900 
MSHLEEKLLL TTKISKNFET RLQDIESKVT QTLIPYYISV KKGSVVTNER DQALQLQVLN 

       910        920        930        940        950        960 
SRFKALEAKS IHLSINFFSL NKTLHEVLTM CHNASTSVSE LNATIPKWIK HSLPDIQLLQ 

       970        980        990       1000       1010       1020 
KGLTEFVEPI IQIKTQAALS NLTCCIDRSL PGSLANVVKS QKQVKSLPKK INALKKPTVN 

      1030       1040       1050       1060       1070       1080 
LTTVLIGRTQ RNTDNIIYPE EYSSCSRHPC QNGGTCINGR TSFTCACRHP FTGDNCTIKL 

      1090       1100       1110       1120       1130       1140 
VEENALAPDF SKGSYRYAPM VAFFASHTYG MTIPGPILFN NLDVNYGASY TPRTGKFRIP 

      1150       1160       1170       1180       1190       1200 
YLGVYVFKYT IESFSAHISG FLVVDGIDKL AFESENINSE IHCDRVLTGD ALLELNYGQE 

      1210       1220 
VWLRLAKGTI PAKFPPVTTF SGYLLYRT 

« Hide

Isoform 2 [UniParc].

Checksum: 80974ECCBAA1F993
Show »

FASTA53158,170

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-136.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3635.1. [Q13201-1]
PIRA57384.
RefSeqNP_031377.2. NM_007351.2. [Q13201-1]
UniGeneHs.268107.

3D structure databases

ProteinModelPortalQ13201.
SMRQ13201. Positions 1100-1227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116577. 1 interaction.
IntActQ13201. 1 interaction.
STRING9606.ENSP00000264790.

PTM databases

PhosphoSiteQ13201.

Polymorphism databases

DMDM143811421.

2D gel databases

OGPQ13201.

Proteomic databases

PaxDbQ13201.
PRIDEQ13201.

Protocols and materials databases

DNASU22915.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264790; ENSP00000264790; ENSG00000138722. [Q13201-1]
ENST00000394980; ENSP00000378431; ENSG00000138722. [Q13201-1]
ENST00000394981; ENSP00000378432; ENSG00000138722. [Q13201-2]
GeneID22915.
KEGGhsa:22915.
UCSCuc003hst.3. human. [Q13201-1]
uc010iku.3. human. [Q13201-2]

Organism-specific databases

CTD22915.
GeneCardsGC04P090800.
H-InvDBHIX0024584.
HGNCHGNC:7178. MMRN1.
HPAHPA035769.
MIM601456. gene.
neXtProtNX_Q13201.
PharmGKBPA30891.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45481.
HOGENOMHOG000113610.
HOVERGENHBG108139.
InParanoidQ13201.
OMACACRHPF.
OrthoDBEOG7CCBQ6.
PhylomeDBQ13201.
TreeFamTF336041.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ13201.
BgeeQ13201.
CleanExHS_MMRN1.
GenevestigatorQ13201.

Family and domain databases

Gene3D2.60.120.40. 1 hit.
InterProIPR001073. 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]
PfamPF00386. C1q. 1 hit.
PF00008. EGF. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
PRINTSPR00007. COMPLEMNTC1Q.
SMARTSM00110. C1Q. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF49842. SSF49842. 1 hit.
PROSITEPS50871. C1Q. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMRN1.
GenomeRNAi22915.
NextBio43599.
PROQ13201.
SOURCESearch...

Entry information

Entry nameMMRN1_HUMAN
AccessionPrimary (citable) accession number: Q13201
Secondary accession number(s): Q4W5L1, Q6P3T8, Q6ZUL9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM