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Protein

Poly(U)-specific endoribonuclease

Gene

ENDOU

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

Functioni

Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini.1 Publication

Cofactori

Mn2+1 Publication

GO - Molecular functioni

  • endoribonuclease activity Source: UniProtKB
  • growth factor activity Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • polysaccharide binding Source: InterPro
  • RNA binding Source: UniProtKB
  • scavenger receptor activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  • female pregnancy Source: UniProtKB
  • immune response Source: InterPro
  • proteolysis Source: UniProtKB
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Manganese, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(U)-specific endoribonuclease (EC:3.1.-.-)
Alternative name(s):
Placental protein 11
Short name:
PP11
Protein endoU
Uridylate-specific endoribonuclease
Gene namesi
Name:ENDOU
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:14369. ENDOU.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: ProtInc
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi284 – 2841E → Q: Abolishes endoribonuclease activity and increases RNA-binding activity. 1 Publication
Mutagenesisi285 – 2851H → A: Abolishes endoribonuclease activity without affecting RNA-binding activity. 1 Publication
Mutagenesisi290 – 2901E → Q: Abolishes endoribonuclease activity without affecting RNA-binding activity. 1 Publication
Mutagenesisi300 – 3001H → A: Abolishes endoribonuclease activity without affecting RNA-binding activity. 1 Publication
Mutagenesisi343 – 3431K → A: Strongly impairs endoribonuclease activity without affecting RNA-binding activity. 1 Publication

Organism-specific databases

PharmGKBiPA165512645.

Polymorphism and mutation databases

BioMutaiENDOU.
DMDMi296434493.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 410392Poly(U)-specific endoribonucleasePRO_0000036405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 40AlternatePROSITE-ProRule annotation
Disulfide bondi24 ↔ 28AlternatePROSITE-ProRule annotation
Disulfide bondi28 ↔ 58AlternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 51AlternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 40AlternatePROSITE-ProRule annotation
Disulfide bondi44 ↔ 50PROSITE-ProRule annotation
Disulfide bondi51 ↔ 58AlternatePROSITE-ProRule annotation
Disulfide bondi90 ↔ 106AlternatePROSITE-ProRule annotation
Disulfide bondi90 ↔ 94AlternatePROSITE-ProRule annotation
Disulfide bondi94 ↔ 124AlternatePROSITE-ProRule annotation
Disulfide bondi104 ↔ 117AlternatePROSITE-ProRule annotation
Disulfide bondi104 ↔ 106AlternatePROSITE-ProRule annotation
Disulfide bondi110 ↔ 116PROSITE-ProRule annotation
Disulfide bondi117 ↔ 124AlternatePROSITE-ProRule annotation

Post-translational modificationi

It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP21128.
PRIDEiP21128.
TopDownProteomicsiP21128-2. [P21128-2]

PTM databases

PhosphoSiteiP21128.

Expressioni

Tissue specificityi

Placental-specific, but also associated with various malignant neoplasms.

Gene expression databases

BgeeiP21128.
GenevisibleiP21128. HS.

Organism-specific databases

HPAiHPA012388.

Interactioni

Subunit structurei

Monomer.By similarity

GO - Molecular functioni

  • growth factor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi114423. 2 interactions.
STRINGi9606.ENSP00000397679.

Structurei

3D structure databases

ProteinModelPortaliP21128.
SMRiP21128. Positions 22-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 6243SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini86 – 13045SMB 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ENDOU family.Curated
Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG2849. Eukaryota.
ENOG410XX8E. LUCA.
GeneTreeiENSGT00530000063825.
HOGENOMiHOG000247015.
HOVERGENiHBG008236.
InParanoidiP21128.
KOiK14648.
OMAiHQNRYGS.
OrthoDBiEOG7J9VR8.
PhylomeDBiP21128.
TreeFamiTF319848.

Family and domain databases

InterProiIPR018998. Endoribonuclease_XendoU.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF01033. Somatomedin_B. 2 hits.
PF09412. XendoU. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P21128-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRACISLVLA VLCGLAWAGK IESCASRCNE KFNRDAACQC DRRCLWHGNC
60 70 80 90 100
CEDYEHLCTE DHKESEPLPQ LEEETEEALA SNLYSAPTSC QGRCYEAFDK
110 120 130 140 150
HHQCHCNARC QEFGNCCKDF ESLCSDHEVS HSSDAITKEE IQSISEKIYR
160 170 180 190 200
ADTNKAQKED IVLNSQNCIS PSETRNQVDR CPKPLFTYVN EKLFSKPTYA
210 220 230 240 250
AFINLLNNYQ RATGHGEHFS AQELAEQDAF LREIMKTAVM KELYSFLHHQ
260 270 280 290 300
NRYGSEQEFV DDLKNMWFGL YSRGNEEGDS SGFEHVFSGE VKKGKVTGFH
310 320 330 340 350
NWIRFYLEEK EGLVDYYSHI YDGPWDSYPD VLAMQFNWDG YYKEVGSAFI
360 370 380 390 400
GSSPEFEFAL YSLCFIARPG KVCQLSLGGY PLAVRTYTWD KSTYGNGKKY
410
IATAYIVSST
Length:410
Mass (Da):46,872
Last modified:May 18, 2010 - v2
Checksum:iCC19484F40355129
GO
Isoform 2 (identifier: P21128-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-59: Missing.

Show »
Length:369
Mass (Da):42,121
Checksum:iF5935AE12D7E924C
GO
Isoform 3 (identifier: P21128-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-82: GKIESCASRCNEKFNRDAACQCDRRCLWHGNCCEDYEHLCTEDHKESEPLPQLEEETEEALASN → D

Note: No experimental confirmation available.
Show »
Length:347
Mass (Da):39,629
Checksum:iD7F5B74604503201
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231L → P in BAG37240 (PubMed:14702039).Curated
Sequence conflicti387 – 3871Y → H in BAG37240 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721E → Q.
Corresponds to variant rs6504 [ dbSNP | Ensembl ].
VAR_014793
Natural varianti72 – 721E → V.
Corresponds to variant rs6505 [ dbSNP | Ensembl ].
VAR_014794

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei19 – 8264GKIES…ALASN → D in isoform 3. 1 PublicationVSP_039215Add
BLAST
Alternative sequencei19 – 5941Missing in isoform 2. 3 PublicationsVSP_039216Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32402 mRNA. Translation: AAA36464.1.
M36109 mRNA. Translation: AAA36465.1.
AK075446 mRNA. Translation: BAG52139.1.
AK300169 mRNA. Translation: BAH13227.1.
AK314688 mRNA. Translation: BAG37240.1.
AC004241 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57940.1.
BC069715 mRNA. Translation: AAH69715.1.
BC074763 mRNA. Translation: AAH74763.1.
BC111782 mRNA. Translation: AAI11783.1.
CCDSiCCDS53784.1. [P21128-3]
CCDS53785.1. [P21128-1]
CCDS8754.1. [P21128-2]
PIRiA34614.
RefSeqiNP_001165910.1. NM_001172439.1. [P21128-1]
NP_001165911.1. NM_001172440.1. [P21128-3]
NP_006016.1. NM_006025.3. [P21128-2]
UniGeneiHs.997.

Genome annotation databases

EnsembliENST00000229003; ENSP00000229003; ENSG00000111405. [P21128-2]
ENST00000422538; ENSP00000397679; ENSG00000111405. [P21128-1]
ENST00000545824; ENSP00000445004; ENSG00000111405. [P21128-3]
GeneIDi8909.
KEGGihsa:8909.
UCSCiuc001rpt.3. human. [P21128-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32402 mRNA. Translation: AAA36464.1.
M36109 mRNA. Translation: AAA36465.1.
AK075446 mRNA. Translation: BAG52139.1.
AK300169 mRNA. Translation: BAH13227.1.
AK314688 mRNA. Translation: BAG37240.1.
AC004241 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57940.1.
BC069715 mRNA. Translation: AAH69715.1.
BC074763 mRNA. Translation: AAH74763.1.
BC111782 mRNA. Translation: AAI11783.1.
CCDSiCCDS53784.1. [P21128-3]
CCDS53785.1. [P21128-1]
CCDS8754.1. [P21128-2]
PIRiA34614.
RefSeqiNP_001165910.1. NM_001172439.1. [P21128-1]
NP_001165911.1. NM_001172440.1. [P21128-3]
NP_006016.1. NM_006025.3. [P21128-2]
UniGeneiHs.997.

3D structure databases

ProteinModelPortaliP21128.
SMRiP21128. Positions 22-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114423. 2 interactions.
STRINGi9606.ENSP00000397679.

PTM databases

PhosphoSiteiP21128.

Polymorphism and mutation databases

BioMutaiENDOU.
DMDMi296434493.

Proteomic databases

PaxDbiP21128.
PRIDEiP21128.
TopDownProteomicsiP21128-2. [P21128-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229003; ENSP00000229003; ENSG00000111405. [P21128-2]
ENST00000422538; ENSP00000397679; ENSG00000111405. [P21128-1]
ENST00000545824; ENSP00000445004; ENSG00000111405. [P21128-3]
GeneIDi8909.
KEGGihsa:8909.
UCSCiuc001rpt.3. human. [P21128-1]

Organism-specific databases

CTDi8909.
GeneCardsiENDOU.
HGNCiHGNC:14369. ENDOU.
HPAiHPA012388.
MIMi606720. gene.
neXtProtiNX_P21128.
PharmGKBiPA165512645.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2849. Eukaryota.
ENOG410XX8E. LUCA.
GeneTreeiENSGT00530000063825.
HOGENOMiHOG000247015.
HOVERGENiHBG008236.
InParanoidiP21128.
KOiK14648.
OMAiHQNRYGS.
OrthoDBiEOG7J9VR8.
PhylomeDBiP21128.
TreeFamiTF319848.

Miscellaneous databases

GenomeRNAii8909.
NextBioi33477.
PROiP21128.
SOURCEiSearch...

Gene expression databases

BgeeiP21128.
GenevisibleiP21128. HS.

Family and domain databases

InterProiIPR018998. Endoribonuclease_XendoU.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF01033. Somatomedin_B. 2 hits.
PF09412. XendoU. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a cDNA encoding human placental protein 11, a putative serine protease with diagnostic significance as a tumor marker."
    Grundmann U., Roemisch J., Siebold B., Bohn H., Amann E.
    DNA Cell Biol. 9:243-250(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS.
    Tissue: Placenta.
  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] (ISOFORMS 1; 2 AND 3).
    Tissue: Placenta.
  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. 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] (ISOFORM 2).
    Tissue: Brain.
  6. "Homology of placental protein 11 and pea seed albumin 2 with vitronectin."
    Jenne D.E.
    Biochem. Biophys. Res. Commun. 176:1000-1006(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN SOMATOMEDIN-B.
  7. Cited for: FUNCTION, RNA-BINDING, COFACTOR, MUTAGENESIS OF GLU-284; HIS-285; GLU-290; HIS-300 AND LYS-343.

Entry informationi

Entry nameiENDOU_HUMAN
AccessioniPrimary (citable) accession number: P21128
Secondary accession number(s): B2RBJ3
, B3KQS7, B7Z6E1, Q2NKJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 18, 2010
Last modified: March 16, 2016
This is version 140 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

Caution

Was originally (PubMed:2350438) thought to be a serine protease. However, PubMed:18936097 showed it is not the case.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

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.