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A8K2U0

- A2ML1_HUMAN

UniProt

A8K2U0 - A2ML1_HUMAN

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Protein

Alpha-2-macroglobulin-like protein 1

Gene

A2ML1

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:A2ML1Imported
Synonyms:CPAMD9Imported
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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 14541437Alpha-2-macroglobulin-like protein 1Sequence AnalysisPRO_0000318074Add
BLAST

Amino acid modifications

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

BgeeiA8K2U0.
CleanExiHS_A2ML1.
ExpressionAtlasiA8K2U0. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni695 – 72632Bait regionSequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Bait region, Signal

Phylogenomic databases

eggNOGiCOG2373.
GeneTreeiENSGT00760000118982.
HOVERGENiHBG000039.
InParanoidiA8K2U0.
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

        10         20         30         40         50
MWAQLLLGML ALSPAIAEEL PNYLVTLPAR LNFPSVQKVC LDLSPGYSDV
60 70 80 90 100
KFTVTLETKD KTQKLLEYSG LKKRHLHCIS FLVPPPAGGT EEVATIRVSG
110 120 130 140 150
VGNNISFEEK KKVLIQRQGN GTFVQTDKPL YTPGQQVYFR IVTMDSNFVP
160 170 180 190 200
VNDKYSMVEL QDPNSNRIAQ WLEVVPEQGI VDLSFQLAPE AMLGTYTVAV
210 220 230 240 250
AEGKTFGTFS VEEYVLPKFK VEVVEPKELS TVQESFLVKI CCRYTYGKPM
260 270 280 290 300
LGAVQVSVCQ KANTYWYREV EREQLPDKCR NLSGQTDKTG CFSAPVDMAT
310 320 330 340 350
FDLIGYAYSH QINIVATVVE EGTGVEANAT QNIYISPQMG SMTFEDTSNF
360 370 380 390 400
YHPNFPFSGK IRVRGHDDSF LKNHLVFLVI YGTNGTFNQT LVTDNNGLAP
410 420 430 440 450
FTLETSGWNG TDVSLEGKFQ MEDLVYNPEQ VPRYYQNAYL HLRPFYSTTR
460 470 480 490 500
SFLGIHRLNG PLKCGQPQEV LVDYYIDPAD ASPDQEISFS YYLIGKGSLV
510 520 530 540 550
MEGQKHLNSK KKGLKASFSL SLTFTSRLAP DPSLVIYAIF PSGGVVADKI
560 570 580 590 600
QFSVEMCFDN QVSLGFSPSQ QLPGAEVELQ LQAAPGSLCA LRAVDESVLL
610 620 630 640 650
LRPDRELSNR SVYGMFPFWY GHYPYQVAEY DQCPVSGPWD FPQPLIDPMP
660 670 680 690 700
QGHSSQRSII WRPSFSEGTD LFSFFRDVGL KILSNAKIKK PVDCSHRSPE
710 720 730 740 750
YSTAMGAGGG HPEAFESSTP LHQAEDSQVR QYFPETWLWD LFPIGNSGKE
760 770 780 790 800
AVHVTVPDAI TEWKAMSFCT SQSRGFGLSP TVGLTAFKPF FVDLTLPYSV
810 820 830 840 850
VRGESFRLTA TIFNYLKDCI RVQTDLAKSH EYQLESWADS QTSSCLCADD
860 870 880 890 900
AKTHHWNITA VKLGHINFTI STKILDSNEP CGGQKGFVPQ KGRSDTLIKP
910 920 930 940 950
VLVKPEGVLV EKTHSSLLCP KGKVASESVS LELPVDIVPD STKAYVTVLG
960 970 980 990 1000
DIMGTALQNL DGLVQMPSGC GEQNMVLFAP IIYVLQYLEK AGLLTEEIRS
1010 1020 1030 1040 1050
RAVGFLEIGY QKELMYKHSN GSYSAFGERD GNGNTWLTAF VTKCFGQAQK
1060 1070 1080 1090 1100
FIFIDPKNIQ DALKWMAGNQ LPSGCYANVG NLLHTAMKGG VDDEVSLTAY
1110 1120 1130 1140 1150
VTAALLEMGK DVDDPMVSQG LRCLKNSATS TTNLYTQALL AYIFSLAGEM
1160 1170 1180 1190 1200
DIRNILLKQL DQQAIISGES IYWSQKPTPS SNASPWSEPA AVDVELTAYA
1210 1220 1230 1240 1250
LLAQLTKPSL TQKEIAKATS IVAWLAKQHN AYGGFSSTQD TVVALQALAK
1260 1270 1280 1290 1300
YATTAYMPSE EINLVVKSTE NFQRTFNIQS VNRLVFQQDT LPNVPGMYTL
1310 1320 1330 1340 1350
EASGQGCVYV QTVLRYNILP PTNMKTFSLS VEIGKARCEQ PTSPRSLTLT
1360 1370 1380 1390 1400
IHTSYVGSRS SSNMAIVEVK MLSGFSPMEG TNQLLLQQPL VKKVEFGTDT
1410 1420 1430 1440 1450
LNIYLDELIK NTQTYTFTIS QSVLVTNLKP ATIKVYDYYL PDEQATIQYS

DPCE
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti733 – 7331F → L in BAC85654. (PubMed:14702039)Curated
Sequence conflicti733 – 7331F → L in BAF83044. (PubMed:14702039)Curated
Sequence conflicti748 – 7481G → E in AL832139. (PubMed:17974005)Curated
Sequence conflicti1122 – 11221R → W in BAC04793. (PubMed:14702039)Curated
Sequence conflicti1122 – 11221R → W in BAC85653. (PubMed:14702039)Curated
Sequence conflicti1122 – 11221R → W in BAC85654. (PubMed:14702039)Curated
Sequence conflicti1122 – 11221R → W in BAF83044. (PubMed:14702039)Curated
Sequence conflicti1122 – 11221R → W in AL832139. (PubMed:17974005)Curated
Sequence conflicti1150 – 11501M → I in BAF83044. (PubMed:14702039)Curated
Sequence conflicti1248 – 12481L → P in BAC85654. (PubMed:14702039)Curated
Sequence conflicti1257 – 12571M → V in BAC04793. (PubMed:14702039)Curated
Sequence conflicti1257 – 12571M → V in BAC85653. (PubMed:14702039)Curated
Sequence conflicti1257 – 12571M → V in BAC85654. (PubMed:14702039)Curated
Sequence conflicti1257 – 12571M → V in BAF83044. (PubMed:14702039)Curated
Sequence conflicti1257 – 12571M → V in AL832139. (PubMed:17974005)Curated
Sequence conflicti1452 – 14521P → L in AL832139. (PubMed:17974005)Curated

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 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.
GeneTreei ENSGT00760000118982.
HOVERGENi HBG000039.
InParanoidi A8K2U0.
OMAi ATGIVAW.
OrthoDBi EOG7DJSKB.
PhylomeDBi A8K2U0.
TreeFami TF313285.

Miscellaneous databases

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

Gene expression databases

Bgeei A8K2U0.
CleanExi HS_A2ML1.
ExpressionAtlasi A8K2U0. baseline and differential.
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: BrainImported and TongueImported.
  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: BrainImported.
  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: October 29, 2014
This is version 57 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

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