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Protein

Arginyl aminopeptidase-like 1

Gene

RNPEPL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi122 – 1221Zinc; catalyticBy similarity
Active sitei123 – 1231Proton acceptorBy similarity
Metal bindingi126 – 1261Zinc; catalyticBy similarity
Metal bindingi145 – 1451Zinc; catalyticBy similarity
Sitei211 – 2111Transition state stabilizerBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginyl aminopeptidase-like 1 (EC:3.4.11.-)
Short name:
RNPEP-like 1
Gene namesi
Name:RNPEPL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10079. RNPEPL1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34452.

Polymorphism and mutation databases

BioMutaiRNPEPL1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Arginyl aminopeptidase-like 1PRO_0000095094Add
BLAST

Proteomic databases

EPDiQ9HAU8.
MaxQBiQ9HAU8.
PaxDbiQ9HAU8.
PRIDEiQ9HAU8.

PTM databases

iPTMnetiQ9HAU8.
PhosphoSiteiQ9HAU8.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at relatively higher levels in heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ9HAU8.
CleanExiHS_RNPEPL1.
ExpressionAtlasiQ9HAU8. baseline and differential.
GenevisibleiQ9HAU8. HS.

Organism-specific databases

HPAiHPA036772.

Interactioni

Protein-protein interaction databases

BioGridi121399. 2 interactions.
IntActiQ9HAU8. 1 interaction.
STRINGi9606.ENSP00000270357.

Structurei

3D structure databases

ProteinModelPortaliQ9HAU8.
SMRiQ9HAU8. Positions 14-432.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 995Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiKOG1047. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00530000063003.
HOGENOMiHOG000293296.
HOVERGENiHBG001274.
InParanoidiQ9HAU8.
KOiK09605.
OMAiVCNRSFF.
PhylomeDBiQ9HAU8.
TreeFamiTF300758.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HAU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATRSAYME EEGVFHFHME HPVPAYLVAL VAGDLKPADI GPRSRVWAEP
60 70 80 90 100
CLLPTATSKL SGAVEQWLSA AERLYGPYMW GRYDIVFLPP SFPIVAMENP
110 120 130 140 150
CLTFIISSIL ESDEFLVIDV IHEVAHSWFG NAVTNATWEE MWLSEGLATY
160 170 180 190 200
AQRRITTETY GAAFTCLETA FRLDALHRQM KLLGEDSPVS KLQVKLEPGV
210 220 230 240 250
NPSHLMNLFT YEKGYCFVYY LSQLCGDPQR FDDFLRAYVE KYKFTSVVAQ
260 270 280 290 300
DLLDSFLSFF PELKEQSVDC RAGLEFERWL NATGPPLAEP DLSQGSSLTR
310 320 330 340 350
PVEALFQLWT AEPLDQAAAS ASAIDISKWR TFQTALFLDR LLDGSPLPQE
360 370 380 390 400
VVMSLSKCYS SLLDSMNAEI RIRWLQIVVR NDYYPDLHRV RRFLESQMSR
410 420 430 440 450
MYTIPLYEDL CTGALKSFAL EVFYQTQGRL HPNLRRAIQQ ILSQGLGSST
460 470 480 490
EPASEPSTEL GKAEADTDSD AQALLLGDEA PSSAISLRDV NVSA
Length:494
Mass (Da):55,518
Last modified:October 17, 2006 - v2
Checksum:iB58739D82376642B
GO

Sequence cautioni

The sequence BAA91823.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti378 – 3781V → E in AAG22080 (PubMed:11017071).Curated
Sequence conflicti378 – 3781V → E in BAA91823 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti247 – 2471V → M in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036046

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300795 mRNA. Translation: AAG22080.1.
AC124862 Genomic DNA. Translation: AAX88943.1.
BC017301 mRNA. Translation: AAH17301.2.
BC067258 mRNA. Translation: AAH67258.2.
BC082975 mRNA. Translation: AAH82975.1.
AK001668 mRNA. Translation: BAA91823.1. Different initiation.
AL512754 mRNA. Translation: CAC21674.1.
RefSeqiNP_060696.4. NM_018226.4.
UniGeneiHs.5345.

Genome annotation databases

EnsembliENST00000270357; ENSP00000270357; ENSG00000142327.
GeneIDi57140.
KEGGihsa:57140.
UCSCiuc061uih.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF300795 mRNA. Translation: AAG22080.1.
AC124862 Genomic DNA. Translation: AAX88943.1.
BC017301 mRNA. Translation: AAH17301.2.
BC067258 mRNA. Translation: AAH67258.2.
BC082975 mRNA. Translation: AAH82975.1.
AK001668 mRNA. Translation: BAA91823.1. Different initiation.
AL512754 mRNA. Translation: CAC21674.1.
RefSeqiNP_060696.4. NM_018226.4.
UniGeneiHs.5345.

3D structure databases

ProteinModelPortaliQ9HAU8.
SMRiQ9HAU8. Positions 14-432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121399. 2 interactions.
IntActiQ9HAU8. 1 interaction.
STRINGi9606.ENSP00000270357.

Protein family/group databases

MEROPSiM01.022.

PTM databases

iPTMnetiQ9HAU8.
PhosphoSiteiQ9HAU8.

Polymorphism and mutation databases

BioMutaiRNPEPL1.

Proteomic databases

EPDiQ9HAU8.
MaxQBiQ9HAU8.
PaxDbiQ9HAU8.
PRIDEiQ9HAU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270357; ENSP00000270357; ENSG00000142327.
GeneIDi57140.
KEGGihsa:57140.
UCSCiuc061uih.1. human.

Organism-specific databases

CTDi57140.
GeneCardsiRNPEPL1.
H-InvDBHIX0200261.
HGNCiHGNC:10079. RNPEPL1.
HPAiHPA036772.
MIMi605287. gene.
neXtProtiNX_Q9HAU8.
PharmGKBiPA34452.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1047. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00530000063003.
HOGENOMiHOG000293296.
HOVERGENiHBG001274.
InParanoidiQ9HAU8.
KOiK09605.
OMAiVCNRSFF.
PhylomeDBiQ9HAU8.
TreeFamiTF300758.

Miscellaneous databases

ChiTaRSiRNPEPL1. human.
GenomeRNAii57140.
PROiQ9HAU8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAU8.
CleanExiHS_RNPEPL1.
ExpressionAtlasiQ9HAU8. baseline and differential.
GenevisibleiQ9HAU8. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR001930. Peptidase_M1.
IPR015211. Peptidase_M1_C.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF09127. Leuk-A4-hydro_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
SMARTiSM01263. Leuk-A4-hydro_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Pancreas and PNS.
  4. "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] OF 116-494.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 242-494.
    Tissue: Lymph node.
  6. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-247.

Entry informationi

Entry nameiRNPL1_HUMAN
AccessioniPrimary (citable) accession number: Q9HAU8
Secondary accession number(s): Q5XKC3
, Q6NX56, Q96AC9, Q9H033, Q9NVD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 137 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. 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.