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Protein

Keratinocyte-associated protein 2

Gene

KRTCAP2

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

Names & Taxonomyi

Protein namesi
Recommended name:
Keratinocyte-associated protein 2
Short name:
KCP-2
Gene namesi
Name:KRTCAP2
Synonyms:KCP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28942. KRTCAP2.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55LumenalSequence analysis
Transmembranei6 – 2318HelicalSequence analysisAdd
BLAST
Topological domaini24 – 3411CytoplasmicSequence analysisAdd
BLAST
Transmembranei35 – 5521HelicalSequence analysisAdd
BLAST
Topological domaini56 – 7520LumenalSequence analysisAdd
BLAST
Transmembranei76 – 10833HelicalSequence analysisAdd
BLAST
Topological domaini109 – 13628CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134967679.

Polymorphism and mutation databases

DMDMi557952588.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 136136Keratinocyte-associated protein 2PRO_0000226992Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N6L1.
MaxQBiQ8N6L1.
PaxDbiQ8N6L1.
PRIDEiQ8N6L1.
TopDownProteomicsiQ8N6L1-2. [Q8N6L1-2]

PTM databases

iPTMnetiQ8N6L1.
PhosphoSiteiQ8N6L1.
SwissPalmiQ8N6L1.

Expressioni

Tissue specificityi

Expressed in skin, heart, placental, liver, skeletal muscle, kidney, pancreas, keratinocytes and dermal fibroblasts.1 Publication

Gene expression databases

BgeeiQ8N6L1.
CleanExiHS_KRTCAP2.
GenevisibleiQ8N6L1. HS.

Interactioni

Subunit structurei

Component of the oligosaccharyltransferase (OST) complex. OST seems to exist in different forms which contain at least RPN1, RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST can form stable complexes with the Sec61 complex or with both the Sec61 and TRAP complexes. Interacts with STT3A.1 Publication

Protein-protein interaction databases

BioGridi128307. 9 interactions.
IntActiQ8N6L1. 7 interactions.
STRINGi9606.ENSP00000295682.

Structurei

3D structure databases

ProteinModelPortaliQ8N6L1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi133 – 1364Prevents secretion from ER

Sequence similaritiesi

Belongs to the KRTCAP2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4615. Eukaryota.
ENOG4111ZNW. LUCA.
GeneTreeiENSGT00390000003552.
HOGENOMiHOG000006286.
HOVERGENiHBG057832.
InParanoidiQ8N6L1.
OMAiAGMQIYS.
OrthoDBiEOG7Z3F6N.
TreeFamiTF324347.

Family and domain databases

InterProiIPR018614. Uncharacterised_KRTCAP2.
[Graphical view]
PfamiPF09775. Keratin_assoc. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q8N6L1-1) [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
MVVGTGTSLA LSSLLSLLLF AGMQMYSRQL ASTEWLTIQG GLLGSGLFVF
60 70 80 90 100
SLTAFNNLEN LVFGKGFQAK IFPEILLCLL LALFASGLIH RVCVTTCFIF
110 120 130
SMVGLYYINK ISSTLYQAAA PVLTPAKVTG KSKKRN
Length:136
Mass (Da):14,679
Last modified:November 13, 2013 - v2
Checksum:i090926F115D7532B
GO
Isoform 2 (identifier: Q8N6L1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRIANRTRFSSPFLARGAGWTHGRGMM

Note: Produced at low levels due to suboptimal Kozak context.
Show »
Length:162
Mass (Da):17,595
Checksum:i4351A6485FA2CC75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871G → S in AAO13161 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41G → V.1 Publication
Corresponds to variant rs17854920 [ dbSNP | Ensembl ].
VAR_025531

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRIANRTRFSSPFLARGAGW THGRGMM in isoform 2. 2 PublicationsVSP_053439

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157577 mRNA. Translation: AAO13161.2.
AK311907 mRNA. Translation: BAG34848.1.
AL607067 Genomic DNA. No translation available.
BC029806 mRNA. Translation: AAH29806.1.
BC048205 mRNA. Translation: AAH48205.1.
BC057233 mRNA. Translation: AAH57233.1.
CCDSiCCDS1096.1. [Q8N6L1-2]
RefSeqiNP_776251.1. NM_173852.3. [Q8N6L1-2]
UniGeneiHs.516671.
Hs.704676.

Genome annotation databases

EnsembliENST00000295682; ENSP00000295682; ENSG00000163463. [Q8N6L1-2]
GeneIDi200185.
KEGGihsa:200185.
UCSCiuc001fho.4. human. [Q8N6L1-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157577 mRNA. Translation: AAO13161.2.
AK311907 mRNA. Translation: BAG34848.1.
AL607067 Genomic DNA. No translation available.
BC029806 mRNA. Translation: AAH29806.1.
BC048205 mRNA. Translation: AAH48205.1.
BC057233 mRNA. Translation: AAH57233.1.
CCDSiCCDS1096.1. [Q8N6L1-2]
RefSeqiNP_776251.1. NM_173852.3. [Q8N6L1-2]
UniGeneiHs.516671.
Hs.704676.

3D structure databases

ProteinModelPortaliQ8N6L1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128307. 9 interactions.
IntActiQ8N6L1. 7 interactions.
STRINGi9606.ENSP00000295682.

PTM databases

iPTMnetiQ8N6L1.
PhosphoSiteiQ8N6L1.
SwissPalmiQ8N6L1.

Polymorphism and mutation databases

DMDMi557952588.

Proteomic databases

EPDiQ8N6L1.
MaxQBiQ8N6L1.
PaxDbiQ8N6L1.
PRIDEiQ8N6L1.
TopDownProteomicsiQ8N6L1-2. [Q8N6L1-2]

Protocols and materials databases

DNASUi200185.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295682; ENSP00000295682; ENSG00000163463. [Q8N6L1-2]
GeneIDi200185.
KEGGihsa:200185.
UCSCiuc001fho.4. human. [Q8N6L1-1]

Organism-specific databases

CTDi200185.
GeneCardsiKRTCAP2.
HGNCiHGNC:28942. KRTCAP2.
neXtProtiNX_Q8N6L1.
PharmGKBiPA134967679.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4615. Eukaryota.
ENOG4111ZNW. LUCA.
GeneTreeiENSGT00390000003552.
HOGENOMiHOG000006286.
HOVERGENiHBG057832.
InParanoidiQ8N6L1.
OMAiAGMQIYS.
OrthoDBiEOG7Z3F6N.
TreeFamiTF324347.

Miscellaneous databases

ChiTaRSiKRTCAP2. human.
GenomeRNAii200185.
PROiQ8N6L1.

Gene expression databases

BgeeiQ8N6L1.
CleanExiHS_KRTCAP2.
GenevisibleiQ8N6L1. HS.

Family and domain databases

InterProiIPR018614. Uncharacterised_KRTCAP2.
[Graphical view]
PfamiPF09775. Keratin_assoc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel genes for secreted and membrane-anchored proteins in human keratinocytes."
    Bonkobara M., Das A., Takao J., Cruz P.D. Jr., Ariizumi K.
    Br. J. Dermatol. 148:654-664(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Keratinocyte.
  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] (ISOFORM 2).
    Tissue: Testis.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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] (ISOFORM 2), VARIANT VAL-4.
    Tissue: Brain, Colon, Kidney and Stomach.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Keratinocyte-associated protein 2 is a bona fide subunit of the mammalian oligosaccharyltransferase."
    Roboti P., High S.
    J. Cell Sci. 125:220-232(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, ER RETENTION MOTIF, TOPOLOGY, ALTERNATIVE INITIATION, INTERACTION WITH STT3A.

Entry informationi

Entry nameiKTAP2_HUMAN
AccessioniPrimary (citable) accession number: Q8N6L1
Secondary accession number(s): B2R4Q1
, Q6PG45, Q86XW2, Q8IWS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 13, 2013
Last modified: June 8, 2016
This is version 103 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 1
    Human chromosome 1: 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. 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.