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A8K2U0

- A2ML1_HUMAN

UniProt

A8K2U0 - A2ML1_HUMAN

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Protein
Alpha-2-macroglobulin-like protein 1
Gene
A2ML1, CPAMD9
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase By similarity. Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases.By similarity1 Publication

GO - Molecular functioni

  1. peptidase inhibitor activity Source: UniProtKB
  2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. regulation of endopeptidase activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI39.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-2-macroglobulin-like protein 1
Alternative name(s):
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9
Gene namesi
Name:A2ML1
Synonyms:CPAMD9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:23336. A2ML1.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 14541437Alpha-2-macroglobulin-like protein 1
PRO_0000318074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 78 By similarityBy similarity
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi241 ↔ 291 By similarityBy similarity
Disulfide bondi259 ↔ 279 By similarityBy similarity
Glycosylationi281 – 2811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi409 – 4091N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi464 ↔ 557 By similarityBy similarity
Disulfide bondi589 ↔ 769 By similarityBy similarity
Disulfide bondi819 ↔ 847 By similarityBy similarity
Disulfide bondi845 ↔ 881 By similarityBy similarity
Glycosylationi857 – 8571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi919 ↔ 1307 By similarityBy similarity
Cross-linki970 ↔ 973Isoglutamyl cysteine thioester (Cys-Gln) By similarityBy similarity
Glycosylationi1020 – 10201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1075 ↔ 1123 By similarityBy similarity
Disulfide bondi1338 ↔ 1453 By similarityBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Thioester bond

Proteomic databases

MaxQBiA8K2U0.
PaxDbiA8K2U0.
PRIDEiA8K2U0.

PTM databases

PhosphoSiteiA8K2U0.

Expressioni

Tissue specificityi

In the epidermis, expressed predominantly in the granular layer at the apical edge of keratinocytes (at protein level). Also detected in placenta, testis and thymus but not in epithelia of kidney, lung, small intestine or colon.1 Publication

Developmental stagei

Up-regulated during keratinocyte differentiation.1 Publication

Gene expression databases

ArrayExpressiA8K2U0.
BgeeiA8K2U0.
CleanExiHS_A2ML1.
GenevestigatoriA8K2U0.

Organism-specific databases

HPAiHPA038847.
HPA038848.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiA8K2U0. 1 interaction.
STRINGi9606.ENSP00000299698.

Structurei

3D structure databases

ProteinModelPortaliA8K2U0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni695 – 72632Bait region
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Bait region, Signal

Phylogenomic databases

eggNOGiCOG2373.
HOVERGENiHBG000039.
OMAiATGIVAW.
OrthoDBiEOG7DJSKB.
PhylomeDBiA8K2U0.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A8K2U0-1 [UniParc]FASTAAdd to Basket

« Hide

MWAQLLLGML ALSPAIAEEL PNYLVTLPAR LNFPSVQKVC LDLSPGYSDV     50
KFTVTLETKD KTQKLLEYSG LKKRHLHCIS FLVPPPAGGT EEVATIRVSG 100
VGNNISFEEK KKVLIQRQGN GTFVQTDKPL YTPGQQVYFR IVTMDSNFVP 150
VNDKYSMVEL QDPNSNRIAQ WLEVVPEQGI VDLSFQLAPE AMLGTYTVAV 200
AEGKTFGTFS VEEYVLPKFK VEVVEPKELS TVQESFLVKI CCRYTYGKPM 250
LGAVQVSVCQ KANTYWYREV EREQLPDKCR NLSGQTDKTG CFSAPVDMAT 300
FDLIGYAYSH QINIVATVVE EGTGVEANAT QNIYISPQMG SMTFEDTSNF 350
YHPNFPFSGK IRVRGHDDSF LKNHLVFLVI YGTNGTFNQT LVTDNNGLAP 400
FTLETSGWNG TDVSLEGKFQ MEDLVYNPEQ VPRYYQNAYL HLRPFYSTTR 450
SFLGIHRLNG PLKCGQPQEV LVDYYIDPAD ASPDQEISFS YYLIGKGSLV 500
MEGQKHLNSK KKGLKASFSL SLTFTSRLAP DPSLVIYAIF PSGGVVADKI 550
QFSVEMCFDN QVSLGFSPSQ QLPGAEVELQ LQAAPGSLCA LRAVDESVLL 600
LRPDRELSNR SVYGMFPFWY GHYPYQVAEY DQCPVSGPWD FPQPLIDPMP 650
QGHSSQRSII WRPSFSEGTD LFSFFRDVGL KILSNAKIKK PVDCSHRSPE 700
YSTAMGAGGG HPEAFESSTP LHQAEDSQVR QYFPETWLWD LFPIGNSGKE 750
AVHVTVPDAI TEWKAMSFCT SQSRGFGLSP TVGLTAFKPF FVDLTLPYSV 800
VRGESFRLTA TIFNYLKDCI RVQTDLAKSH EYQLESWADS QTSSCLCADD 850
AKTHHWNITA VKLGHINFTI STKILDSNEP CGGQKGFVPQ KGRSDTLIKP 900
VLVKPEGVLV EKTHSSLLCP KGKVASESVS LELPVDIVPD STKAYVTVLG 950
DIMGTALQNL DGLVQMPSGC GEQNMVLFAP IIYVLQYLEK AGLLTEEIRS 1000
RAVGFLEIGY QKELMYKHSN GSYSAFGERD GNGNTWLTAF VTKCFGQAQK 1050
FIFIDPKNIQ DALKWMAGNQ LPSGCYANVG NLLHTAMKGG VDDEVSLTAY 1100
VTAALLEMGK DVDDPMVSQG LRCLKNSATS TTNLYTQALL AYIFSLAGEM 1150
DIRNILLKQL DQQAIISGES IYWSQKPTPS SNASPWSEPA AVDVELTAYA 1200
LLAQLTKPSL TQKEIAKATS IVAWLAKQHN AYGGFSSTQD TVVALQALAK 1250
YATTAYMPSE EINLVVKSTE NFQRTFNIQS VNRLVFQQDT LPNVPGMYTL 1300
EASGQGCVYV QTVLRYNILP PTNMKTFSLS VEIGKARCEQ PTSPRSLTLT 1350
IHTSYVGSRS SSNMAIVEVK MLSGFSPMEG TNQLLLQQPL VKKVEFGTDT 1400
LNIYLDELIK NTQTYTFTIS QSVLVTNLKP ATIKVYDYYL PDEQATIQYS 1450
DPCE 1454
Length:1,454
Mass (Da):161,107
Last modified:October 5, 2010 - v3
Checksum:i15ED65D000834E33
GO

Sequence cautioni

The sequence BAB71612.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC04793.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC85653.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC85654.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071G → R.
Corresponds to variant rs11047499 [ dbSNP | Ensembl ].
VAR_055463
Natural varianti850 – 8501D → E.2 Publications
Corresponds to variant rs1860926 [ dbSNP | Ensembl ].
VAR_059083
Natural varianti970 – 9701C → Y.
Corresponds to variant rs1558526 [ dbSNP | Ensembl ].
VAR_055464
Natural varianti1131 – 11311T → M.
Corresponds to variant rs7959680 [ dbSNP | Ensembl ].
VAR_055465
Natural varianti1229 – 12291H → R.2 Publications
Corresponds to variant rs10219561 [ dbSNP | Ensembl ].
VAR_059084
Natural varianti1412 – 14121T → A.
Corresponds to variant rs7315591 [ dbSNP | Ensembl ].
VAR_055466

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti733 – 7331F → L in BAC85654. 1 Publication
Sequence conflicti733 – 7331F → L in BAF83044. 1 Publication
Sequence conflicti748 – 7481G → E in AL832139. 1 Publication
Sequence conflicti1122 – 11221R → W in BAC04793. 1 Publication
Sequence conflicti1122 – 11221R → W in BAC85653. 1 Publication
Sequence conflicti1122 – 11221R → W in BAC85654. 1 Publication
Sequence conflicti1122 – 11221R → W in BAF83044. 1 Publication
Sequence conflicti1122 – 11221R → W in AL832139. 1 Publication
Sequence conflicti1150 – 11501M → I in BAF83044. 1 Publication
Sequence conflicti1248 – 12481L → P in BAC85654. 1 Publication
Sequence conflicti1257 – 12571M → V in BAC04793. 1 Publication
Sequence conflicti1257 – 12571M → V in BAC85653. 1 Publication
Sequence conflicti1257 – 12571M → V in BAC85654. 1 Publication
Sequence conflicti1257 – 12571M → V in BAF83044. 1 Publication
Sequence conflicti1257 – 12571M → V in AL832139. 1 Publication
Sequence conflicti1452 – 14521P → L in AL832139. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK057908 mRNA. Translation: BAB71612.1. Different initiation.
AK096448 mRNA. Translation: BAC04793.1. Different initiation.
AK123591 mRNA. Translation: BAC85653.1. Different initiation.
AK123592 mRNA. Translation: BAC85654.1. Different initiation.
AK290355 mRNA. Translation: BAF83044.1.
AL832139 mRNA. No translation available.
AC006513 Genomic DNA. No translation available.
AC006581 Genomic DNA. No translation available.
BC093840 mRNA. Translation: AAH93840.2.
BC112131 mRNA. Translation: AAI12132.1.
CCDSiCCDS8596.2.
UniGeneiHs.620532.

Genome annotation databases

EnsembliENST00000299698; ENSP00000299698; ENSG00000166535.
UCSCiuc001quz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK057908 mRNA. Translation: BAB71612.1 . Different initiation.
AK096448 mRNA. Translation: BAC04793.1 . Different initiation.
AK123591 mRNA. Translation: BAC85653.1 . Different initiation.
AK123592 mRNA. Translation: BAC85654.1 . Different initiation.
AK290355 mRNA. Translation: BAF83044.1 .
AL832139 mRNA. No translation available.
AC006513 Genomic DNA. No translation available.
AC006581 Genomic DNA. No translation available.
BC093840 mRNA. Translation: AAH93840.2 .
BC112131 mRNA. Translation: AAI12132.1 .
CCDSi CCDS8596.2.
UniGenei Hs.620532.

3D structure databases

ProteinModelPortali A8K2U0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A8K2U0. 1 interaction.
STRINGi 9606.ENSP00000299698.

Protein family/group databases

MEROPSi I39.007.

PTM databases

PhosphoSitei A8K2U0.

Proteomic databases

MaxQBi A8K2U0.
PaxDbi A8K2U0.
PRIDEi A8K2U0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299698 ; ENSP00000299698 ; ENSG00000166535 .
UCSCi uc001quz.5. human.

Organism-specific databases

GeneCardsi GC12P008975.
HGNCi HGNC:23336. A2ML1.
HPAi HPA038847.
HPA038848.
MIMi 610627. gene.
neXtProti NX_A8K2U0.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2373.
HOVERGENi HBG000039.
OMAi ATGIVAW.
OrthoDBi EOG7DJSKB.
PhylomeDBi A8K2U0.
TreeFami TF313285.

Miscellaneous databases

ChiTaRSi A2ML1. human.
PROi A8K2U0.
SOURCEi Search...

Gene expression databases

ArrayExpressi A8K2U0.
Bgeei A8K2U0.
CleanExi HS_A2ML1.
Genevestigatori A8K2U0.

Family and domain databases

Gene3Di 1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProi IPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR014756. Ig_E-set.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view ]
Pfami PF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANTS GLU-850 AND ARG-1229.
    Tissue: Brain and Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-850 AND ARG-1229.
    Tissue: Cervix.
  3. "The finished DNA sequence of human chromosome 12."
    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.H., 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.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 1290-1454.
    Tissue: Brain.
  5. "A novel protease inhibitor of the alpha2-macroglobulin family expressed in the human epidermis."
    Galliano M.-F., Toulza E., Gallinaro H., Jonca N., Ishida-Yamamoto A., Serre G., Guerrin M.
    J. Biol. Chem. 281:5780-5789(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiA2ML1_HUMAN
AccessioniPrimary (citable) accession number: A8K2U0
Secondary accession number(s): B5MDD1
, Q2M224, Q6ZW52, Q6ZW53, Q8N1M4, Q96LQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 55 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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