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P08519

- APOA_HUMAN

UniProt

P08519 - APOA_HUMAN

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Protein

Apolipoprotein(a)

Gene

LPA

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

Functioni

Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei4369 – 43691Charge relay system
Active sitei4412 – 44121Charge relay system
Active sitei4498 – 44981Charge relay system

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. endopeptidase inhibitor activity Source: ProtInc
  3. fibronectin binding Source: BHF-UCL
  4. heparin binding Source: BHF-UCL
  5. serine-type endopeptidase activity Source: BHF-UCL

GO - Biological processi

  1. blood circulation Source: ProtInc
  2. lipid metabolic process Source: ProtInc
  3. lipid transport Source: UniProtKB-KW
  4. lipoprotein metabolic process Source: Reactome
  5. negative regulation of endopeptidase activity Source: GOC
  6. receptor-mediated endocytosis Source: Reactome
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Lipid transport, Transport

Enzyme and pathway databases

ReactomeiREACT_6934. LDL-mediated lipid transport.

Protein family/group databases

MEROPSiS01.999.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein(a) (EC:3.4.21.-)
Short name:
Apo(a)
Short name:
Lp(a)
Gene namesi
Name:LPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6667. LPA.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. plasma lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Atherosclerosis

Organism-specific databases

MIMi152200. gene+phenotype.
PharmGKBiPA30432.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 45484529Apolipoprotein(a)PRO_0000028097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 105By similarity
Disulfide bondi49 ↔ 88By similarity
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi77 ↔ 100By similarity
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi142 ↔ 219By similarity
Disulfide bondi163 ↔ 202By similarity
Disulfide bondi191 ↔ 214By similarity
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi256 ↔ 333By similarity
Disulfide bondi277 ↔ 316By similarity
Disulfide bondi305 ↔ 328By similarity
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi370 ↔ 447By similarity
Disulfide bondi391 ↔ 430By similarity
Disulfide bondi419 ↔ 442By similarity
Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi484 ↔ 561By similarity
Disulfide bondi505 ↔ 544By similarity
Disulfide bondi533 ↔ 556By similarity
Glycosylationi557 – 5571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi598 ↔ 675By similarity
Disulfide bondi619 ↔ 658By similarity
Disulfide bondi647 ↔ 670By similarity
Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi712 ↔ 789By similarity
Disulfide bondi733 ↔ 772By similarity
Disulfide bondi761 ↔ 784By similarity
Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi826 ↔ 903By similarity
Disulfide bondi847 ↔ 886By similarity
Disulfide bondi875 ↔ 898By similarity
Glycosylationi899 – 8991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi940 ↔ 1017By similarity
Disulfide bondi961 ↔ 1000By similarity
Disulfide bondi989 ↔ 1012By similarity
Glycosylationi1013 – 10131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1054 ↔ 1131By similarity
Disulfide bondi1075 ↔ 1114By similarity
Disulfide bondi1103 ↔ 1126By similarity
Glycosylationi1127 – 11271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1168 ↔ 1245By similarity
Disulfide bondi1189 ↔ 1228By similarity
Disulfide bondi1217 ↔ 1240By similarity
Glycosylationi1241 – 12411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1282 ↔ 1359By similarity
Disulfide bondi1303 ↔ 1342By similarity
Disulfide bondi1331 ↔ 1354By similarity
Glycosylationi1355 – 13551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1396 ↔ 1473By similarity
Disulfide bondi1417 ↔ 1456By similarity
Disulfide bondi1445 ↔ 1468By similarity
Glycosylationi1469 – 14691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1510 ↔ 1587By similarity
Disulfide bondi1531 ↔ 1570By similarity
Disulfide bondi1559 ↔ 1582By similarity
Glycosylationi1583 – 15831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1624 ↔ 1701By similarity
Disulfide bondi1645 ↔ 1684By similarity
Disulfide bondi1673 ↔ 1696By similarity
Glycosylationi1697 – 16971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1738 ↔ 1815By similarity
Disulfide bondi1759 ↔ 1798By similarity
Disulfide bondi1787 ↔ 1810By similarity
Glycosylationi1811 – 18111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1852 ↔ 1929By similarity
Disulfide bondi1873 ↔ 1912By similarity
Disulfide bondi1901 ↔ 1924By similarity
Glycosylationi1925 – 19251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1966 ↔ 2043By similarity
Disulfide bondi1987 ↔ 2026By similarity
Disulfide bondi2015 ↔ 2038By similarity
Glycosylationi2039 – 20391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2080 ↔ 2157By similarity
Disulfide bondi2101 ↔ 2140By similarity
Disulfide bondi2129 ↔ 2152By similarity
Glycosylationi2153 – 21531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2194 ↔ 2271By similarity
Disulfide bondi2215 ↔ 2254By similarity
Disulfide bondi2243 ↔ 2266By similarity
Glycosylationi2267 – 22671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2308 ↔ 2385By similarity
Disulfide bondi2329 ↔ 2368By similarity
Disulfide bondi2357 ↔ 2380By similarity
Glycosylationi2381 – 23811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2422 ↔ 2499By similarity
Disulfide bondi2443 ↔ 2482By similarity
Disulfide bondi2471 ↔ 2494By similarity
Glycosylationi2495 – 24951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2536 ↔ 2613By similarity
Disulfide bondi2557 ↔ 2596By similarity
Disulfide bondi2585 ↔ 2608By similarity
Glycosylationi2609 – 26091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2650 ↔ 2727By similarity
Disulfide bondi2671 ↔ 2710By similarity
Disulfide bondi2699 ↔ 2722By similarity
Glycosylationi2723 – 27231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2764 ↔ 2841By similarity
Disulfide bondi2785 ↔ 2824By similarity
Disulfide bondi2813 ↔ 2836By similarity
Glycosylationi2837 – 28371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2878 ↔ 2955By similarity
Disulfide bondi2899 ↔ 2938By similarity
Disulfide bondi2927 ↔ 2950By similarity
Glycosylationi2951 – 29511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2992 ↔ 3069By similarity
Disulfide bondi3013 ↔ 3052By similarity
Disulfide bondi3041 ↔ 3064By similarity
Glycosylationi3065 – 30651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3106 ↔ 3183By similarity
Disulfide bondi3127 ↔ 3166By similarity
Disulfide bondi3155 ↔ 3178By similarity
Glycosylationi3179 – 31791N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3220 ↔ 3297By similarity
Disulfide bondi3241 ↔ 3280By similarity
Disulfide bondi3269 ↔ 3292By similarity
Glycosylationi3293 – 32931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3334 ↔ 3411By similarity
Disulfide bondi3355 ↔ 3394By similarity
Disulfide bondi3383 ↔ 3406By similarity
Glycosylationi3407 – 34071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3448 ↔ 3525By similarity
Disulfide bondi3469 ↔ 3508By similarity
Disulfide bondi3497 ↔ 3520By similarity
Glycosylationi3521 – 35211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3562 ↔ 3639By similarity
Disulfide bondi3583 ↔ 3622By similarity
Disulfide bondi3611 ↔ 3634By similarity
Glycosylationi3635 – 36351N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3676 ↔ 3753
Disulfide bondi3697 ↔ 3736
Disulfide bondi3725 ↔ 3748
Glycosylationi3749 – 37491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3782 ↔ 3859
Disulfide bondi3803 ↔ 3842
Disulfide bondi3831 ↔ 3854
Glycosylationi3855 – 38551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3889 – 38891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3896 ↔ 3973By similarity
Disulfide bondi3917 ↔ 3956By similarity
Disulfide bondi3945 ↔ 3968By similarity
Glycosylationi3969 – 39691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4010 ↔ 4087By similarity
Disulfide bondi4031 ↔ 4070By similarity
Disulfide bondi4059 ↔ 4082By similarity
Glycosylationi4083 – 40831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4124 ↔ 4201By similarity
Disulfide bondi4145 ↔ 4184By similarity
Disulfide bondi4173 ↔ 4196By similarity
Glycosylationi4197 – 41971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4228 ↔ 4307By similarity
Disulfide bondi4249 ↔ 4290By similarity
Disulfide bondi4278 ↔ 4302By similarity
Disulfide bondi4354 ↔ 4370By similarity
Disulfide bondi4446 ↔ 4504By similarity
Disulfide bondi4476 ↔ 4483By similarity
Disulfide bondi4494 ↔ 4522By similarity

Post-translational modificationi

N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O-glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected.

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP08519.
PaxDbiP08519.
PRIDEiP08519.

PTM databases

PhosphoSiteiP08519.
UniCarbKBiP08519.

Expressioni

Gene expression databases

BgeeiP08519.
CleanExiHS_LPA.
ExpressionAtlasiP08519. baseline and differential.
GenevestigatoriP08519.

Organism-specific databases

HPAiCAB000668.
CAB016072.
CAB016678.

Interactioni

Subunit structurei

Disulfide-linked to apo-B100. Binds to fibronectin and decorin.

Binary interactionsi

WithEntry#Exp.IntActNotes
APOHP027494EBI-9232288,EBI-2114682
FN1P027512EBI-9232288,EBI-1220319

Protein-protein interaction databases

BioGridi110202. 4 interactions.
IntActiP08519. 2 interactions.
STRINGi9606.ENSP00000321334.

Structurei

Secondary structure

1
4548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3665 – 36673
Turni3679 – 36835
Beta strandi3704 – 37063
Helixi3712 – 37143
Turni3716 – 37183
Beta strandi3735 – 37406
Beta strandi3745 – 37495
Turni3818 – 38203
Turni3822 – 38254
Beta strandi3834 – 38363
Beta strandi3841 – 38466
Beta strandi3851 – 38555
Beta strandi3889 – 38935
Beta strandi3912 – 39143
Beta strandi3924 – 39263
Beta strandi3951 – 39533
Beta strandi4129 – 41313
Beta strandi4152 – 41543
Turni4160 – 41623
Beta strandi4183 – 41875
Beta strandi4193 – 41975

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I71X-ray1.45A3781-3863[»]
1JFNNMR-A3665-3770[»]
1KIVX-ray2.10A4124-4201[»]
2FEBNMR-A3885-3980[»]
3KIVX-ray1.80A4123-4201[»]
4BV5X-ray2.10A/B4123-4201[»]
4BV7X-ray1.70A4123-4201[»]
4BVCX-ray1.60A4123-4201[»]
4BVDX-ray1.68A4123-4201[»]
4BVVX-ray1.80A4227-4307[»]
4BVWX-ray2.00A/B3781-3859[»]
4KIVX-ray2.20A4123-4201[»]
ProteinModelPortaliP08519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 130111Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini131 – 244114Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini245 – 358114Kringle 3PROSITE-ProRule annotationAdd
BLAST
Domaini359 – 472114Kringle 4PROSITE-ProRule annotationAdd
BLAST
Domaini473 – 586114Kringle 5PROSITE-ProRule annotationAdd
BLAST
Domaini587 – 700114Kringle 6PROSITE-ProRule annotationAdd
BLAST
Domaini701 – 814114Kringle 7PROSITE-ProRule annotationAdd
BLAST
Domaini815 – 928114Kringle 8PROSITE-ProRule annotationAdd
BLAST
Domaini929 – 1042114Kringle 9PROSITE-ProRule annotationAdd
BLAST
Domaini1043 – 1156114Kringle 10PROSITE-ProRule annotationAdd
BLAST
Domaini1157 – 1270114Kringle 11PROSITE-ProRule annotationAdd
BLAST
Domaini1271 – 1384114Kringle 12PROSITE-ProRule annotationAdd
BLAST
Domaini1385 – 1498114Kringle 13PROSITE-ProRule annotationAdd
BLAST
Domaini1499 – 1612114Kringle 14PROSITE-ProRule annotationAdd
BLAST
Domaini1613 – 1726114Kringle 15PROSITE-ProRule annotationAdd
BLAST
Domaini1727 – 1840114Kringle 16PROSITE-ProRule annotationAdd
BLAST
Domaini1841 – 1954114Kringle 17PROSITE-ProRule annotationAdd
BLAST
Domaini1955 – 2068114Kringle 18PROSITE-ProRule annotationAdd
BLAST
Domaini2069 – 2182114Kringle 19PROSITE-ProRule annotationAdd
BLAST
Domaini2183 – 2296114Kringle 20PROSITE-ProRule annotationAdd
BLAST
Domaini2297 – 2410114Kringle 21PROSITE-ProRule annotationAdd
BLAST
Domaini2411 – 2524114Kringle 22PROSITE-ProRule annotationAdd
BLAST
Domaini2525 – 2638114Kringle 23PROSITE-ProRule annotationAdd
BLAST
Domaini2639 – 2752114Kringle 24PROSITE-ProRule annotationAdd
BLAST
Domaini2753 – 2866114Kringle 25PROSITE-ProRule annotationAdd
BLAST
Domaini2867 – 2980114Kringle 26PROSITE-ProRule annotationAdd
BLAST
Domaini2981 – 3094114Kringle 27PROSITE-ProRule annotationAdd
BLAST
Domaini3095 – 3208114Kringle 28PROSITE-ProRule annotationAdd
BLAST
Domaini3209 – 3322114Kringle 29PROSITE-ProRule annotationAdd
BLAST
Domaini3323 – 3436114Kringle 30PROSITE-ProRule annotationAdd
BLAST
Domaini3437 – 3550114Kringle 31PROSITE-ProRule annotationAdd
BLAST
Domaini3551 – 3664114Kringle 32PROSITE-ProRule annotationAdd
BLAST
Domaini3665 – 3770106Kringle 33PROSITE-ProRule annotationAdd
BLAST
Domaini3771 – 3884114Kringle 34PROSITE-ProRule annotationAdd
BLAST
Domaini3885 – 3998114Kringle 35PROSITE-ProRule annotationAdd
BLAST
Domaini3999 – 4112114Kringle 36PROSITE-ProRule annotationAdd
BLAST
Domaini4113 – 4226114Kringle 37PROSITE-ProRule annotationAdd
BLAST
Domaini4227 – 4327101Kringle 38PROSITE-ProRule annotationAdd
BLAST
Domaini4328 – 4546219Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Plasminogen subfamily.PROSITE-ProRule annotation
Contains 38 kringle domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000170962.
HOVERGENiHBG004270.
OrthoDBiEOG75B84T.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.40.20.10. 38 hits.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00051. Kringle. 38 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00130. KR. 38 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 38 hits.
PROSITEiPS00021. KRINGLE_1. 38 hits.
PS50070. KRINGLE_2. 38 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08519 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MEHKEVVLLL LLFLKSAAPE QSHVVQDCYH GDGQSYRGTY STTVTGRTCQ
60 70 80 90 100
AWSSMTPHQH NRTTENYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC
110 120 130 140 150
NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
160 170 180 190 200
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP
210 220 230 240 250
YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR
260 270 280 290 300
PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
310 320 330 340 350
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP
360 370 380 390 400
SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH
410 420 430 440 450
SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
460 470 480 490 500
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV
510 520 530 540 550
TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG
560 570 580 590 600
VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH
610 620 630 640 650
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP
660 670 680 690 700
DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ
710 720 730 740 750
APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY
760 770 780 790 800
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP
810 820 830 840 850
TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW
860 870 880 890 900
SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL
910 920 930 940 950
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG
960 970 980 990 1000
TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC
1010 1020 1030 1040 1050
YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG
1060 1070 1080 1090 1100
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM
1110 1120 1130 1140 1150
NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL
1160 1170 1180 1190 1200
EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH
1210 1220 1230 1240 1250
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG
1260 1270 1280 1290 1300
TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG
1310 1320 1330 1340 1350
RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR
1360 1370 1380 1390 1400
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN
1410 1420 1430 1440 1450
GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA
1460 1470 1480 1490 1500
VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP
1510 1520 1530 1540 1550
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP
1560 1570 1580 1590 1600
NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV
1610 1620 1630 1640 1650
TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS
1660 1670 1680 1690 1700
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ
1710 1720 1730 1740 1750
CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY
1760 1770 1780 1790 1800
STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT
1810 1820 1830 1840 1850
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ
1860 1870 1880 1890 1900
ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY
1910 1920 1930 1940 1950
CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA
1960 1970 1980 1990 2000
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR
2010 2020 2030 2040 2050
TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA
2060 2070 2080 2090 2100
VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT
2110 2120 2130 2140 2150
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE
2160 2170 2180 2190 2200
YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ
2210 2220 2230 2240 2250
SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA
2260 2270 2280 2290 2300
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE
2310 2320 2330 2340 2350
QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA
2360 2370 2380 2390 2400
GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP
2410 2420 2430 2440 2450
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT
2460 2470 2480 2490 2500
PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS
2510 2520 2530 2540 2550
DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST
2560 2570 2580 2590 2600
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD
2610 2620 2630 2640 2650
PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC
2660 2670 2680 2690 2700
YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR
2710 2720 2730 2740 2750
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS
2760 2770 2780 2790 2800
EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP
2810 2820 2830 2840 2850
EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA
2860 2870 2880 2890 2900
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ
2910 2920 2930 2940 2950
AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC
2960 2970 2980 2990 3000
NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
3010 3020 3030 3040 3050
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP
3060 3070 3080 3090 3100
YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR
3110 3120 3130 3140 3150
PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
3160 3170 3180 3190 3200
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP
3210 3220 3230 3240 3250
SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH
3260 3270 3280 3290 3300
SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
3310 3320 3330 3340 3350
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV
3360 3370 3380 3390 3400
TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDPVA APYCYTRDPS
3410 3420 3430 3440 3450
VRWEYCNLTQ CSDAEGTAVA PPTITPIPSL EAPSEQAPTE QRPGVQECYH
3460 3470 3480 3490 3500
GNGQSYQGTY FITVTGRTCQ AWSSMTPHSH SRTPAYYPNA GLIKNYCRNP
3510 3520 3530 3540 3550
DPVAAPWCYT TDPSVRWEYC NLTRCSDAEW TAFVPPNVIL APSLEAFFEQ
3560 3570 3580 3590 3600
ALTEETPGVQ DCYYHYGQSY RGTYSTTVTG RTCQAWSSMT PHQHSRTPEN
3610 3620 3630 3640 3650
YPNAGLTRNY CRNPDAEIRP WCYTMDPSVR WEYCNLTQCL VTESSVLATL
3660 3670 3680 3690 3700
TVVPDPSTEA SSEEAPTEQS PGVQDCYHGD GQSYRGSFST TVTGRTCQSW
3710 3720 3730 3740 3750
SSMTPHWHQR TTEYYPNGGL TRNYCRNPDA EISPWCYTMD PNVRWEYCNL
3760 3770 3780 3790 3800
TQCPVTESSV LATSTAVSEQ APTEQSPTVQ DCYHGDGQSY RGSFSTTVTG
3810 3820 3830 3840 3850
RTCQSWSSMT PHWHQRTTEY YPNGGLTRNY CRNPDAEIRP WCYTMDPSVR
3860 3870 3880 3890 3900
WEYCNLTQCP VMESTLLTTP TVVPVPSTEL PSEEAPTENS TGVQDCYRGD
3910 3920 3930 3940 3950
GQSYRGTLST TITGRTCQSW SSMTPHWHRR IPLYYPNAGL TRNYCRNPDA
3960 3970 3980 3990 4000
EIRPWCYTMD PSVRWEYCNL TRCPVTESSV LTTPTVAPVP STEAPSEQAP
4010 4020 4030 4040 4050
PEKSPVVQDC YHGDGRSYRG ISSTTVTGRT CQSWSSMIPH WHQRTPENYP
4060 4070 4080 4090 4100
NAGLTENYCR NPDSGKQPWC YTTDPCVRWE YCNLTQCSET ESGVLETPTV
4110 4120 4130 4140 4150
VPVPSMEAHS EAAPTEQTPV VRQCYHGNGQ SYRGTFSTTV TGRTCQSWSS
4160 4170 4180 4190 4200
MTPHRHQRTP ENYPNDGLTM NYCRNPDADT GPWCFTMDPS IRWEYCNLTR
4210 4220 4230 4240 4250
CSDTEGTVVA PPTVIQVPSL GPPSEQDCMF GNGKGYRGKK ATTVTGTPCQ
4260 4270 4280 4290 4300
EWAAQEPHRH STFIPGTNKW AGLEKNYCRN PDGDINGPWC YTMNPRKLFD
4310 4320 4330 4340 4350
YCDIPLCASS SFDCGKPQVE PKKCPGSIVG GCVAHPHSWP WQVSLRTRFG
4360 4370 4380 4390 4400
KHFCGGTLIS PEWVLTAAHC LKKSSRPSSY KVILGAHQEV NLESHVQEIE
4410 4420 4430 4440 4450
VSRLFLEPTQ ADIALLKLSR PAVITDKVMP ACLPSPDYMV TARTECYITG
4460 4470 4480 4490 4500
WGETQGTFGT GLLKEAQLLV IENEVCNHYK YICAEHLARG TDSCQGDSGG
4510 4520 4530 4540
PLVCFEKDKY ILQGVTSWGL GCARPNKPGV YARVSRFVTW IEGMMRNN
Length:4,548
Mass (Da):501,319
Last modified:August 1, 1988 - v1
Checksum:i96921BE96A465C5F
GO

Polymorphismi

The reference genome sequence encodes a variant that contains 16 Kringle domains and that lack residues 533 to 3040. Depending on the individual, the encoded protein contains 2-43 copies of kringle-type domains. The allele represented here contains 38 copies of the kringle-type repeats.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3498 – 34981R → Q.
Corresponds to variant rs41259144 [ dbSNP | Ensembl ].
VAR_047293
Natural varianti3866 – 38661L → V.
Corresponds to variant rs7765803 [ dbSNP | Ensembl ].
VAR_047294
Natural varianti3880 – 38801L → V.
Corresponds to variant rs7765781 [ dbSNP | Ensembl ].
VAR_047295
Natural varianti3907 – 39071T → P.
Corresponds to variant rs41272110 [ dbSNP | Ensembl ].
VAR_047296
Natural varianti3929 – 39291R → Q.
Corresponds to variant rs41272112 [ dbSNP | Ensembl ].
VAR_047297
Natural varianti4106 – 41061M → T.
Corresponds to variant rs41264308 [ dbSNP | Ensembl ].
VAR_047298
Natural varianti4187 – 41871M → T.
Corresponds to variant rs1801693 [ dbSNP | Ensembl ].
VAR_047299
Natural varianti4193 – 41931W → R Loss of lysine-sepharose binding. 1 Publication
VAR_006633
Natural varianti4330 – 43301G → A.
Corresponds to variant rs41265936 [ dbSNP | Ensembl ].
VAR_047300
Natural varianti4399 – 43991I → M.
Corresponds to variant rs3798220 [ dbSNP | Ensembl ].
VAR_047301
Natural varianti4524 – 45241R → C.
Corresponds to variant rs3124784 [ dbSNP | Ensembl ].
VAR_047302

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06290 mRNA. Translation: CAA29618.1.
AL109933, AL596089 Genomic DNA. Translation: CAI22905.1.
AL596089, AL109933 Genomic DNA. Translation: CAH73590.1.
PIRiS00657.
UniGeneiHs.520120.

Genome annotation databases

EnsembliENST00000316300; ENSP00000321334; ENSG00000198670.
ENST00000447678; ENSP00000395608; ENSG00000198670.

Polymorphism databases

DMDMi114062.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06290 mRNA. Translation: CAA29618.1 .
AL109933 , AL596089 Genomic DNA. Translation: CAI22905.1 .
AL596089 , AL109933 Genomic DNA. Translation: CAH73590.1 .
PIRi S00657.
UniGenei Hs.520120.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I71 X-ray 1.45 A 3781-3863 [» ]
1JFN NMR - A 3665-3770 [» ]
1KIV X-ray 2.10 A 4124-4201 [» ]
2FEB NMR - A 3885-3980 [» ]
3KIV X-ray 1.80 A 4123-4201 [» ]
4BV5 X-ray 2.10 A/B 4123-4201 [» ]
4BV7 X-ray 1.70 A 4123-4201 [» ]
4BVC X-ray 1.60 A 4123-4201 [» ]
4BVD X-ray 1.68 A 4123-4201 [» ]
4BVV X-ray 1.80 A 4227-4307 [» ]
4BVW X-ray 2.00 A/B 3781-3859 [» ]
4KIV X-ray 2.20 A 4123-4201 [» ]
ProteinModelPortali P08519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110202. 4 interactions.
IntActi P08519. 2 interactions.
STRINGi 9606.ENSP00000321334.

Chemistry

DrugBanki DB00513. Aminocaproic Acid.

Protein family/group databases

MEROPSi S01.999.

PTM databases

PhosphoSitei P08519.
UniCarbKBi P08519.

Polymorphism databases

DMDMi 114062.

Proteomic databases

MaxQBi P08519.
PaxDbi P08519.
PRIDEi P08519.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316300 ; ENSP00000321334 ; ENSG00000198670 .
ENST00000447678 ; ENSP00000395608 ; ENSG00000198670 .

Organism-specific databases

GeneCardsi GC06M160952.
H-InvDB HIX0057735.
HGNCi HGNC:6667. LPA.
HPAi CAB000668.
CAB016072.
CAB016678.
MIMi 152200. gene+phenotype.
neXtProti NX_P08519.
PharmGKBi PA30432.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000170962.
HOVERGENi HBG004270.
OrthoDBi EOG75B84T.
TreeFami TF329901.

Enzyme and pathway databases

Reactomei REACT_6934. LDL-mediated lipid transport.

Miscellaneous databases

EvolutionaryTracei P08519.
NextBioi 15766.
PROi P08519.
SOURCEi Search...

Gene expression databases

Bgeei P08519.
CleanExi HS_LPA.
ExpressionAtlasi P08519. baseline and differential.
Genevestigatori P08519.

Family and domain databases

Gene3Di 2.40.20.10. 38 hits.
InterProi IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00051. Kringle. 38 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00130. KR. 38 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 38 hits.
PROSITEi PS00021. KRINGLE_1. 38 hits.
PS50070. KRINGLE_2. 38 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence of human apolipoprotein(a) is homologous to plasminogen."
    McLean J.W., Tomlison J.E., Kuang W.-J., Eaton D.L., Chen E.Y., Fless G.M., Scanu A.M., Lawn R.M.
    Nature 330:132-137(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Amplification of human APO(a) kringle 4-37 from blood lymphocyte DNA."
    Pfaffinger D., Mc Lean J., Scanu A.M.
    Biochim. Biophys. Acta 1225:107-109(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4184-4208.
    Tissue: Lymphocyte.
  4. "Lipoprotein(a) binds to fibronectin and has serine proteinase activity capable of cleaving it."
    Salonen E.-M., Jauhiainen M., Zardi L., Vaheri A., Ehnholm C.
    EMBO J. 8:4035-4040(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A SERINE PROTEASE.
  5. "The mysteries of lipoprotein(a)."
    Utermann G.
    Science 246:904-910(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Structural elucidation of the N- and O-glycans of human apolipoprotein(a): role of o-glycans in conferring protease resistance."
    Garner B., Merry A.H., Royle L., Harvey D.J., Rudd P.M., Thillet J.
    J. Biol. Chem. 276:22200-22208(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF N-LINKED AND O-LINKED CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Crystal structures of apolipoprotein(a) kringle IV37 free and complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic acid: existence of novel and expected binding modes."
    Mikol V., Lograsso P.V., Boettcher B.R.
    J. Mol. Biol. 256:751-761(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4121-4208.
  8. "A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a)."
    Scanu A.M., Pfaffinger D., Lee J.C., Hinman J.
    Biochim. Biophys. Acta 1227:41-45(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-4193.

Entry informationi

Entry nameiAPOA_HUMAN
AccessioniPrimary (citable) accession number: P08519
Secondary accession number(s): Q5VTD7, Q9UD88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 29, 2014
This is version 145 of the entry and version 1 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

Miscellaneous

Apo(a) is known to be proteolytically cleaved, leading to the formation of the so-called mini-Lp(a). Apo(a) fragments accumulate in atherosclerotic lesions, where they may promote thrombogenesis. O-glycosylation may limit the extent of proteolytic fragmentation. Homology with plasminogen kringles IV and V is thought to underlie the atherogenicity of the protein, because the fragments are competing with plasminogen for fibrin(ogen) binding.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3