Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Microfibrillar-associated protein 1

Gene

Mfap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Component of the elastin-associated microfibrils.By similarity

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-2129379. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Microfibrillar-associated protein 1
Gene namesi
Name:Mfap1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914782. Mfap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 439438Microfibrillar-associated protein 1PRO_0000096459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei116 – 1161PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Cross-linki249 – 249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei267 – 2671PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CQU1.
MaxQBiQ9CQU1.
PaxDbiQ9CQU1.
PRIDEiQ9CQU1.

PTM databases

iPTMnetiQ9CQU1.
PhosphoSiteiQ9CQU1.

Expressioni

Gene expression databases

BgeeiQ9CQU1.
GenevisibleiQ9CQU1. MM.

Interactioni

Protein-protein interaction databases

BioGridi780109. 1 interaction.
IntActiQ9CQU1. 1 interaction.
STRINGi10090.ENSMUSP00000087372.

Structurei

3D structure databases

ProteinModelPortaliQ9CQU1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi134 – 1396Poly-Glu

Sequence similaritiesi

Belongs to the MFAP1 family.Curated

Phylogenomic databases

eggNOGiKOG1425. Eukaryota.
ENOG410Y1JB. LUCA.
GeneTreeiENSGT00690000102225.
HOGENOMiHOG000231845.
HOVERGENiHBG052462.
InParanoidiQ9CQU1.
KOiK13110.
OMAiFDRPTVK.
OrthoDBiEOG7ZPNKJ.
PhylomeDBiQ9CQU1.
TreeFamiTF314398.

Family and domain databases

InterProiIPR033194. MFAP1.
IPR009730. MFAP1_C.
[Graphical view]
PANTHERiPTHR15327:SF0. PTHR15327:SF0. 1 hit.
PfamiPF06991. MFAP1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CQU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM
60 70 80 90 100
ESSDEEDEEF QFIKKAKEQE AEPEEQEEDS SSDPRLRRLQ NRISEDVEER
110 120 130 140 150
LARHRKIVEP EVVGESDSEV EGDAWRLERE DSSEEEEEEI DDEEIERRRG
160 170 180 190 200
MMRQRAQERK NEEMEVMEVE DEGRSGEESE SESEYEEYTD SEDEMEPRLK
210 220 230 240 250
PVFIRKKDRV TVQEREAEAL KQKELEQEAK RMAEERRKYT LKIVEEETKK
260 270 280 290 300
ELEENKRSLA ALDALNTDDE NDEEEYEAWK VRELKRIKRE REDREALEKE
310 320 330 340 350
KAEIERMRNL TEEERRAELR ANGKVITNKA VKGKYKFLQK YYHRGAFFMD
360 370 380 390 400
EDEEVYKRDF SAPTLEDHFN KTILPKVMQV KNFGRSGRTK YTHLVDQDTT
410 420 430
SFDSAWGQES AQNTKFFKQK AAGVRDVFER PSAKKRKTT
Length:439
Mass (Da):51,954
Last modified:June 1, 2001 - v1
Checksum:i5B57B1F1C42421E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012688 mRNA. Translation: BAB28412.3.
AK014483 mRNA. Translation: BAB29385.1.
AK018514 mRNA. Translation: BAB31249.1.
AK032586 mRNA. Translation: BAC27936.1. Different termination.
AK050561 mRNA. Translation: BAC34325.1.
AK077604 mRNA. Translation: BAC36894.1.
AK088766 mRNA. Translation: BAC40557.1.
AK088946 mRNA. Translation: BAC40667.1.
AK161000 mRNA. Translation: BAE36142.1.
BC005728 mRNA. Translation: AAH05728.1.
CCDSiCCDS16648.1.
RefSeqiNP_001075444.1. NM_001081975.3.
NP_080496.1. NM_026220.4.
UniGeneiMm.270393.
Mm.440764.

Genome annotation databases

EnsembliENSMUST00000056732; ENSMUSP00000049548; ENSMUSG00000048222.
ENSMUST00000089926; ENSMUSP00000087372; ENSMUSG00000068479.
GeneIDi100034361.
67532.
KEGGimmu:100034361.
mmu:67532.
UCSCiuc008lzg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012688 mRNA. Translation: BAB28412.3.
AK014483 mRNA. Translation: BAB29385.1.
AK018514 mRNA. Translation: BAB31249.1.
AK032586 mRNA. Translation: BAC27936.1. Different termination.
AK050561 mRNA. Translation: BAC34325.1.
AK077604 mRNA. Translation: BAC36894.1.
AK088766 mRNA. Translation: BAC40557.1.
AK088946 mRNA. Translation: BAC40667.1.
AK161000 mRNA. Translation: BAE36142.1.
BC005728 mRNA. Translation: AAH05728.1.
CCDSiCCDS16648.1.
RefSeqiNP_001075444.1. NM_001081975.3.
NP_080496.1. NM_026220.4.
UniGeneiMm.270393.
Mm.440764.

3D structure databases

ProteinModelPortaliQ9CQU1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi780109. 1 interaction.
IntActiQ9CQU1. 1 interaction.
STRINGi10090.ENSMUSP00000087372.

PTM databases

iPTMnetiQ9CQU1.
PhosphoSiteiQ9CQU1.

Proteomic databases

EPDiQ9CQU1.
MaxQBiQ9CQU1.
PaxDbiQ9CQU1.
PRIDEiQ9CQU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056732; ENSMUSP00000049548; ENSMUSG00000048222.
ENSMUST00000089926; ENSMUSP00000087372; ENSMUSG00000068479.
GeneIDi100034361.
67532.
KEGGimmu:100034361.
mmu:67532.
UCSCiuc008lzg.1. mouse.

Organism-specific databases

CTDi100034361.
67532.
MGIiMGI:1914782. Mfap1.

Phylogenomic databases

eggNOGiKOG1425. Eukaryota.
ENOG410Y1JB. LUCA.
GeneTreeiENSGT00690000102225.
HOGENOMiHOG000231845.
HOVERGENiHBG052462.
InParanoidiQ9CQU1.
KOiK13110.
OMAiFDRPTVK.
OrthoDBiEOG7ZPNKJ.
PhylomeDBiQ9CQU1.
TreeFamiTF314398.

Enzyme and pathway databases

ReactomeiR-MMU-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

PROiQ9CQU1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQU1.
GenevisibleiQ9CQU1. MM.

Family and domain databases

InterProiIPR033194. MFAP1.
IPR009730. MFAP1_C.
[Graphical view]
PANTHERiPTHR15327:SF0. PTHR15327:SF0. 1 hit.
PfamiPF06991. MFAP1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Colon, Embryo, Embryonic liver, Head, Olfactory bulb, Pancreatic islet and Thymus.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116 AND SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-132 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiMFAP1_MOUSE
AccessioniPrimary (citable) accession number: Q9CQU1
Secondary accession number(s): Q3TU29, Q8CCL1, Q9CSJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.