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Protein
Submitted name:

Alpha-2-macroglobulin

Gene

A2M

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Alpha-2-macroglobulinImported
Gene namesi
Name:A2MImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7. A2M.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 168145Sequence analysisPRO_5003379496Add
BLAST

Proteomic databases

PaxDbiF8W7L3.
PeptideAtlasiF8W7L3.
PRIDEiF8W7L3.

Expressioni

Gene expression databases

BgeeiF8W7L3.
ExpressionAtlasiF8W7L3. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000323929.

Structurei

3D structure databases

ProteinModelPortaliF8W7L3.
SMRiF8W7L3. Positions 30-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 16335A2M_NInterPro annotationAdd
BLAST

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.

Family and domain databases

InterProiIPR002890. A2M_N.
IPR010916. TonB_box_CS.
[Graphical view]
PfamiPF01835. A2M_N. 1 hit.
[Graphical view]
PROSITEiPS00430. TONB_DEPENDENT_REC_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

F8W7L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL
60 70 80 90 100
LSYLNETVTV SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV
110 120 130 140 150
MFLTVQVKGP TQEFKKRTTV MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS
160
MDENFHPLNE LIPLVYIQ
Length:168
Mass (Da):18,724
Last modified:September 21, 2011 - v1
Checksum:i9D4E7A221AE5F2F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei168 – 1681Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007436 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENST00000404455; ENSP00000385710; ENSG00000175899.
UCSCiuc058kzv.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC007436 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliF8W7L3.
SMRiF8W7L3. Positions 30-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000323929.

Proteomic databases

PaxDbiF8W7L3.
PeptideAtlasiF8W7L3.
PRIDEiF8W7L3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404455; ENSP00000385710; ENSG00000175899.
UCSCiuc058kzv.1. human.

Organism-specific databases

HGNCiHGNC:7. A2M.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1366. Eukaryota.
ENOG410XRED. LUCA.
GeneTreeiENSGT00760000118982.

Miscellaneous databases

ChiTaRSiA2M. human.

Gene expression databases

BgeeiF8W7L3.
ExpressionAtlasiF8W7L3. baseline and differential.

Family and domain databases

InterProiIPR002890. A2M_N.
IPR010916. TonB_box_CS.
[Graphical view]
PfamiPF01835. A2M_N. 1 hit.
[Graphical view]
PROSITEiPS00430. TONB_DEPENDENT_REC_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The finished DNA sequence of human chromosome 12."
    Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A., null.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
  4. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF8W7L3_HUMAN
AccessioniPrimary (citable) accession number: F8W7L3
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: July 6, 2016
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.