Skip Header

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

P55081

- MFAP1_HUMAN

UniProt

P55081 - MFAP1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Microfibrillar-associated protein 1

Gene

MFAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Component of the elastin-associated microfibrils.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. extracellular matrix organization Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Microfibrillar-associated protein 1
Gene namesi
Name:MFAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:7032. MFAP1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. microfibril Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 439438Microfibrillar-associated protein 1PRO_0000096458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei52 – 521Phosphoserine4 Publications
Modified residuei53 – 531Phosphoserine4 Publications
Modified residuei116 – 1161Phosphoserine7 Publications
Modified residuei118 – 1181Phosphoserine7 Publications
Modified residuei132 – 1321Phosphoserine4 Publications
Modified residuei133 – 1331Phosphoserine4 Publications
Modified residuei267 – 2671Phosphothreonine8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP55081.
PaxDbiP55081.
PRIDEiP55081.

PTM databases

PhosphoSiteiP55081.

Expressioni

Gene expression databases

BgeeiP55081.
CleanExiHS_MFAP1.
GenevestigatoriP55081.

Organism-specific databases

HPAiHPA042370.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
IKQ131232EBI-1048159,EBI-713456
PRPF3O433952EBI-1048159,EBI-744322

Protein-protein interaction databases

BioGridi110394. 26 interactions.
IntActiP55081. 12 interactions.
MINTiMINT-1682969.
STRINGi9606.ENSP00000267812.

Structurei

3D structure databases

ProteinModelPortaliP55081.
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

eggNOGiNOG122136.
GeneTreeiENSGT00690000102225.
HOGENOMiHOG000231845.
HOVERGENiHBG052462.
InParanoidiP55081.
KOiK13110.
OMAiHRHIHEP.
OrthoDBiEOG7ZPNKJ.
PhylomeDBiP55081.
TreeFamiTF314398.

Family and domain databases

InterProiIPR009730. MFAP1_C.
[Graphical view]
PANTHERiPTHR15327. PTHR15327. 1 hit.
PfamiPF06991. Prp19_bind. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P55081 [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 EGDAWRMERE 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 VRELKRIKRD 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):51,958
Last modified:July 22, 2008 - v2
Checksum:i0EF6F4F091C05A88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381K → Q in AAA92786. (PubMed:7835894)Curated
Sequence conflicti242 – 2421K → Q in AAA92786. (PubMed:7835894)Curated
Sequence conflicti245 – 2451E → G in AAA92786. (PubMed:7835894)Curated
Sequence conflicti249 – 2491K → P in AAA92786. (PubMed:7835894)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04209 mRNA. Translation: AAA92786.1.
AK312867 mRNA. Translation: BAG35719.1.
AC018512 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77247.1.
BC023557 mRNA. Translation: AAH23557.1.
BC050742 mRNA. Translation: AAH50742.1.
CCDSiCCDS10105.1.
PIRiA55565.
RefSeqiNP_005917.2. NM_005926.2.
UniGeneiHs.61418.

Genome annotation databases

EnsembliENST00000267812; ENSP00000267812; ENSG00000140259.
GeneIDi4236.
KEGGihsa:4236.
UCSCiuc001zth.1. human.

Polymorphism databases

DMDMi205831094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U04209 mRNA. Translation: AAA92786.1 .
AK312867 mRNA. Translation: BAG35719.1 .
AC018512 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77247.1 .
BC023557 mRNA. Translation: AAH23557.1 .
BC050742 mRNA. Translation: AAH50742.1 .
CCDSi CCDS10105.1.
PIRi A55565.
RefSeqi NP_005917.2. NM_005926.2.
UniGenei Hs.61418.

3D structure databases

ProteinModelPortali P55081.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110394. 26 interactions.
IntActi P55081. 12 interactions.
MINTi MINT-1682969.
STRINGi 9606.ENSP00000267812.

PTM databases

PhosphoSitei P55081.

Polymorphism databases

DMDMi 205831094.

Proteomic databases

MaxQBi P55081.
PaxDbi P55081.
PRIDEi P55081.

Protocols and materials databases

DNASUi 4236.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000267812 ; ENSP00000267812 ; ENSG00000140259 .
GeneIDi 4236.
KEGGi hsa:4236.
UCSCi uc001zth.1. human.

Organism-specific databases

CTDi 4236.
GeneCardsi GC15M044096.
H-InvDB HIX0026808.
HGNCi HGNC:7032. MFAP1.
HPAi HPA042370.
MIMi 600215. gene.
neXtProti NX_P55081.
PharmGKBi PA30768.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG122136.
GeneTreei ENSGT00690000102225.
HOGENOMi HOG000231845.
HOVERGENi HBG052462.
InParanoidi P55081.
KOi K13110.
OMAi HRHIHEP.
OrthoDBi EOG7ZPNKJ.
PhylomeDBi P55081.
TreeFami TF314398.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi MFAP1. human.
GeneWikii MFAP1.
GenomeRNAii 4236.
NextBioi 16701.
PROi P55081.
SOURCEi Search...

Gene expression databases

Bgeei P55081.
CleanExi HS_MFAP1.
Genevestigatori P55081.

Family and domain databases

InterProi IPR009730. MFAP1_C.
[Graphical view ]
PANTHERi PTHR15327. PTHR15327. 1 hit.
Pfami PF06991. Prp19_bind. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the human gene encoding the associated microfibrillar protein (MFAP1) and localization to chromosome 15q15-q21."
    Yeh H., Chow M., Abrams W.R., Fan J., Foster J., Mitchell H., Muenke M., Rosenbloom J.
    Genomics 23:443-449(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.
  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].
    Tissue: Trachea.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [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].
    Tissue: Muscle and PNS.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118; SER-132; SER-133 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-118 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-118; SER-132; SER-133 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-118; SER-132; SER-133 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116; SER-118; SER-132; SER-133 AND THR-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMFAP1_HUMAN
AccessioniPrimary (citable) accession number: P55081
Secondary accession number(s): Q86TG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 22, 2008
Last modified: October 29, 2014
This is version 111 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 15
    Human chromosome 15: 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